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Glucosamine

Medlines Search


Results for your query on February 25, 1999:: Search all fields for: glucosamine; Published in 1966 through 1999; Only select references with abstracts available; Show references published in English only; Show references pertaining to humans; With an article type of: REVIEW

Documents: 1 to 42 of 42

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Number	Title	Comments
...1...	Glucosamine [see comments]	An excellent overview of the use of glucosamine
...2...	Enhanced synovial production of hyaluronic acid may explain rapid clinical response to high-dose glucosamine in osteoarthritis.
...3...	An evaluation of the potential side-effects of alpha-glucosidase inhibitors used for the management of diabetes mellitus.
...4...	Type 2 diabetes: glycemic targets and oral therapies for older patients.
...5...	Potential of alpha-glucosidase inhibitors in elderly patients with diabetes mellitus and impaired glucose tolerance.
...6...	Glucosamine sulfate for osteoarthritis [see comments]
...7...	The role of glucosamine sulfate and chondroitin sulfates in the treatment of degenerative joint disease.	Successful treatment of osteoarthritis must effectively control pain, and should slow down or reverse progression of the disease. Biochemical and pharmacological data combined with animal and human studies demonstrate glucosamine sulfate is capable of satisfying these criteria.
...8...	Pharmacology of alpha-glucosidase inhibition.
...9...	The neglect of glucosamine as a treatment for osteoarthritis--a personal perspective.	. . . medical researchers and physicians in the US have totally ignored this rational and safe therapeutic strategy.
...10...	Glucosamine for psoriasis?
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...11...	Glucosamine may retard atherogenesis by promoting endothelial production of heparan sulfate proteoglycans.	It is reasonable to speculate that exogenous glucosamine will likewise enhance heparan sulfate proteoglycans production by vascular endothelial cells, and, when administered orally in regimens comparable to those effective in osteoarthritis, will thereby act to retard atherogenesis.
...12...	Conservative management of spinal osteoarthritis with glucosamine sulfate and chiropractic treatment.	CONCLUSION: The rationales for using NSAIDs in the treatment of osteoarthritis is controversial and openly contested. Given the detrimental effects of NSAIDs on joints and other organs, their use should be discouraged and their classification as a first choice conservative treatment should be abolished. A truly effective and conservative approach to the treatment of osteoarthritis should include chiropractic manipulation, essential nutrient supplementation, exogenous administration of glucosamine sulfate and rehabilitative stretches and exercises to maintain joint function. Because there is no correlation between pain levels and the extent of degeneration detected by radiographic or physical examination, conservative treatment should be initiated and sustained based on functional, objective findings and not strictly on how the patient feels. The use of NSAIDs should be limited to the treatment of gross inflammation and analgesics should only be used in the short-term when absolutely necessary for pain palliation. The present conservative approach could lead not only to a better quality of life but also to the saving of health care dollars by reducing the iatrogenic morbidity and mortality associated with NSAID use.
...13...	Drug treatment of arthritis. Update on conventional and less conventional methods.
...14...	Severe rheumatoid arthritis: current options in drug therapy.
...15...	The actions of parathyroid hormone on bone: relation to bone remodeling and turnover, calcium homeostasis, and metabolic bone diseases. II. PTH and bone cells: bone turnover and plasma calcium regulation.
...16...	Carbohydrate metabolism and the glucoreceptor mechanism.
...17...	Aspartylglycosaminuria: an inborn error of glycoprotein catabolism.
...18...	Clinical research in osteoarthritis: design and results of short-term and long-term trials with disease-modifying drugs.
...19...	Structure-activity relationships in lipopolysaccharides of Bacteroides fragilis.
...20...	Heparan sulphate in the binding and activation of basic fibroblast growth factor.
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...21...	Prostate-specific antigen and history of its discovery.
...22...	The role of phosphometabolites in cell proliferation, energy metabolism, and tumor therapy.
...23...	How does hyperglycaemia predispose to diabetic nephropathy?
...24...	Interactions of human malaria parasites, Plasmodium vivax and P.falciparum, with the midgut of Anopheles mosquitoes.
...25...	Shedding of CD9 antigen in acute lymphoblastic leukemia.
...26...	Ectodomain interactions of leukocyte integrins and pro-inflammatory GPI-linked membrane proteins.
...27...	Effect of low molecular weight heparin preparations on the inhibition of thrombin by heparin cofactor II.
...28...	The PIG-A gene somatic mutation responsible for paroxysmal nocturnal hemoglobinuria.
...29...	Mucin glycoproteins as tumor markers.
...30...	Involvement of heparan sulfate and related molecules in sequestration and growth promoting activity of fibroblast growth factor.
Menu Position #30
...31...	Oral adhesion of yeasts.
...32...	Proposal for a pathway to mediate the metabolic effects of insulin.
...33...	Diagnostic procedures in immunodermatology.
...34...	Stimulation of fibroblast biosynthetic activity by serum of patients with pretibial myxedema.
...35...	Basement membranes: current concepts of structure and synthesis.
...36...	Biochemistry and lectin binding properties of mammalian salivary mucous glycoproteins.
...37...	Interactions between cells of the immune system and hyaluronate synthesis by human dermal fibroblasts.
...38...	Evidence for multidrug-resistant cells in human tumor cell populations.
...39...	Glycolipid membrane-binding domain of human erythrocyte acetylcholinesterase.
...40...	Invasion of erythrocytes by malaria merozoites: evidence for specific receptors involved in attachment and entry.
Menu Position #40
...41...	Receptors and recognition mechanisms of Trypanosoma cruzi.
...42...	Studies on the biochemical basis of the interaction of the merozoites of Plasmodium falciparum and the human red cell.

Record 1 from database: MEDLINE
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Title: Glucosamine [see comments]
Author: Barclay TS; Tsourounis C; McCart GM
Address: School of Pharmacy, University of California, San Francisco 94143, USA.
Source: Ann Pharmacother, 1998 May, 32:5, 574-9
Abstract: OBJECTIVE: To review the pharmacology and pharmacokinetics of glucosamine and critically evaluate currently available literature regarding its safety and efficacy. DATA SOURCE: A MEDLINE search was conducted between January 1965 and May 1997. Key words used in the search were osteoarthritis, osteoarthrosis, gonarthrosis, and glucosamine. In addition, references cited in articles obtained from the MEDLINE search were reviewed for additional literature. STUDY SELECTION AND DATA EXTRACTION: All articles were considered for inclusion in the review. Articles were excluded from critical evaluation for lack of randomization, lack of a control group, 30 or fewer study participants, inconsistent treatment regimen, incomplete dosing information, or incomplete reporting of results. DATA SYNTHESIS: Osteoarthritis affects approximately 12% of the US population; the incidence increases with increasing age. Currently used pharmacologic treatments, including acetaminophen and nonsteroidal antiinflammatory drugs, do not slow or reverse the degenerative process in osteoarthritis. Glucosamine has recently received a great deal of attention from the public as a potential treatment of osteoarthritis, prompting healthcare professionals to investigate its clinical usefulness and potential for adverse effects. The drug has been proposed to stop and possibly reverse the degenerative process in osteoarthritis. Following absorption of an oral dose, glucosamine is incorporated into plasma proteins during first-pass metabolism, resulting in 26% bioavailability. Unbound glucosamine is concentrated in the articular cartilage. Each of the three critically evaluated studies reported a decrease in the symptoms of osteoarthritis (e.g., decreased Lequesne index, decreased pain severity, increased range of motion) for the glucosamine group, which was greater than that obtained in the control group. Flaws in study design, however, prevent the use of these results in modifying current clinical practice. Reported short-term adverse effects include mild gastrointestinal problems, drowsiness, skin reactions, and headache. CONCLUSIONS: Improvement in the symptoms of osteoarthritis associated with the use of glucosamine has been observed in clinical trials; however, those trials have flaws in design and data analysis. Further research needs to be conducted before glucosamine can be recommended as a treatment for osteoarthritis.
Language of Publication: English
Unique Identifier: 98269324

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MeSH Heading (Major): Glucosamine|AD/AE/*PD/PK; Osteoarthritis|*DT/ME
MeSH Heading: Clinical Trials; Human; Metabolic Clearance Rate

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 1060-0280
Country of Publication: UNITED STATES

Record 2 from database: MEDLINE
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Title: Enhanced synovial production of hyaluronic acid may explain rapid clinical response to high-dose glucosamine in osteoarthritis.
Author: McCarty MF
Address: Nutrition 21, San Diego, CA 92109, USA.
Source: Med Hypotheses, 1998 Jun, 50:6, 507-10
Abstract: Anecdotal reports of rapid symptomatic response to high-dose glucosamine in osteoarthritis are not credibly explained by the traditional view that glucosamine promotes synthesis of cartilage proteoglycans. An alternative or additional possibility is that glucosamine stimulates synovial production of hyaluronic acid (HA), which is primarily responsible for the lubricating and shock-absorbing properties of synovial fluid. Many clinical and veterinary studies have shown that intra-articular injections of high-molecular-weight HA produce rapid pain relief and improved mobility in osteoarthritis. HA has anti-inflammatory and analgesic properties, and promotes anabolic behavior in chondrocytes. The concentration and molecular weight of synovial fluid HA are decreased in osteoarthritis; by reversing this abnormality, high-dose glucosamine may provide rapid symptomatic benefit, and in the longer term aid the repair of damaged cartilage.
Language of Publication: English
Unique Identifier: 98374099

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MeSH Heading (Major): Glucosamine|AD/*TU; Hyaluronic Acid|*BI; Osteoarthritis|*DT; Synovial Membrane|DE/*ME
MeSH Heading: Animal; Human

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0306-9877
Country of Publication: ENGLAND
CAS Registry/EC Number: 3416-24-8 (Glucosamine); 9004-61-9 (Hyaluronic Acid)

Record 3 from database: MEDLINE
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Title: An evaluation of the potential side-effects of alpha-glucosidase inhibitors used for the management of diabetes mellitus.
Author: Reuser AJ; Wisselaar HA
Address: Department of Clinical Genetics, Erasmus University Rotterdam, The Netherlands.
Source: Eur J Clin Invest, 1994 Aug, 24 Suppl 3:, 19-24
Abstract: Orally taken alpha-glucosidase inhibitors are used for the management of diabetes mellitus. These drugs can prevent the postprandial rise of the blood glucose level by inhibiting the enzymatic digestion of carbohydrates in the intestinal lumen. Non-absorbable inhibitors such as acarbose are expected to function exclusively in the intestine, but absorbable inhibitors such as miglitol may exert an inhibitory effect on non-intestinal alpha-glucosidases present in the various cell types of the body. The potential side-effects of absorbable inhibitors are evaluated in this literature review. It is concluded that there is little risk of inducing unwanted side-effects when miglitol is taken in an oral dose of approximately 1 mg kg-1 body weight. The use of absorbable inhibitors is, however, not advised in case of kidney dysfunction.
Language of Publication: English
Unique Identifier: 95094871

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MeSH Heading (Major): alpha-Glucosidases|*AI; Diabetes Mellitus|BL/*DT; Glucosamine|*AA/AE/PD; Hypoglycemic Agents|AE/CT/*PD; Trisaccharides|*AE/PD
MeSH Heading: Administration, Oral; Animal; Blood Glucose|DE/ME; Carbohydrate Sequence; Diabetic Nephropathies|PP; Glycogen|ME; Glycogen Storage Disease|ME; Glycoproteins|BI/CH; Human; Molecular Sequence Data; Sucrase-Isomaltase Complex|DF

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0014-2972
Country of Publication: ENGLAND

Record 4 from database: MEDLINE
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Title: Type 2 diabetes: glycemic targets and oral therapies for older patients.
Author: Lardinois CK
Address: University of Nevada School of Medicine, USA.
Source: Geriatrics, 1998 Nov, 53:11, 22-3, 27-8, 33-4 passim
Abstract: In older patients with type 2 diabetes, life expectancy and the presence of microvascular complications determine the appropriate intensity of glucose control. The available antidiabetic agents offer many options for achieving glycemic targets, based on the needs of the individual patient. New stimulators of insulin secretion include glimepiride (a sulfonylurea) and repaglinide (a meglitinide). The biguanide metformin is especially useful in obese, insulin-resistant patients. Alpha-glucosidase inhibitors such as acarbose and miglitol act locally in the GI tract to reduce postprandial excursion in glucose levels. The insulin-sensitizing drug troglitazone enhances insulin-mediated glucose disposal. When troglitazone is used, careful monitoring of patients' liver function is required.
Language of Publication: English
Unique Identifier: 99042415

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MeSH Heading (Major): Diabetes Mellitus, Non-Insulin-Dependent|CO/*DT/ME; Hypoglycemic Agents|CL/PD/*TU
MeSH Heading: Age Factors; Aged; Blood Glucose|AN; Carbamates|TU; Glucosamine|AA/TU; Human; Metformin|TU; Piperidines|TU; Sulfonylurea Compounds|TU; Trisaccharides|TU

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0016-867X
Country of Publication: UNITED STATES

Record 5 from database: MEDLINE
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Title: Potential of alpha-glucosidase inhibitors in elderly patients with diabetes mellitus and impaired glucose tolerance.
Author: Rabasa Lhoret R; Chiasson JL
Address: Research Group on Diabetes and Metabolic Regulation Research Center, Centre Hospitalier de l'UniversitÆe de MontrÆeal, Campus HÈotel-Dieu, MontrÆeal, QuÆebec, Canada.
Source: Drugs Aging, 1998 Aug, 13:2, 131-43
Abstract: The prevalence of diabetes mellitus (DM) among the elderly, who constitute > 20% of the population in developed countries, is high (up to 40%). Indeed, elderly people represent the bulk (approximately 50%) of the diabetic population. There is much evidence that better glycaemic control can reduce the morbidity associated with this disease. alpha-Glucosidase inhibitors are well tolerated in the treatment of DM in this population. They reduce postprandial hyperglycaemia and have a moderate effect on fastign plasma glucose levels, resulting in a significant reduction in glycated haemoglobin (HbA1C) levels. alpha-Glucosidase inhibitors can be used either as monotherapy or in combination with other oral hypoglycaemic agents or insulin. The good safety profile of these drugs makes them suitable for use in elderly patients with type 2 (non-insulin-dependent) DM, because they can achieve substantial metabolic improvements without any additional risks. Thus, the use of alpha-glucosidase inhibitors should be considered: (i) as a first-choice treatment in newly diagnosed patients; (ii) in individuals whose DM is not well controlled with any other type of treatment; (iii) as an alternative to sulphonylureas or biguanides in patients at risk from hypoglycaemia or lactic acidosis, respectively. Despite the numerous potential advantages of alpha-glucosidase inhibitors in elderly patients with type 2 DM, there is a lack of studies focusing specifically on that population. However, such studies are under way. In addition, the potential of alpha-glucosidase inhibitors in the prevention of type 2 DM and/or on macrovascular disease is currently under study.
Language of Publication: English
Unique Identifier: 98411819

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MeSH Heading (Major): alpha-Glucosidases|*AI; Diabetes Mellitus, Non-Insulin-Dependent|CO/DH/*DT/PC; Enzyme Inhibitors|*TU; Glucose Intolerance|*CO; Hypoglycemic Agents|AE/*TU
MeSH Heading: Aged; Body Weight|DE; Cognition|DE; Glucosamine|AA/TU; Human; Trisaccharides|TU

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 1170-229X
Country of Publication: NEW ZEALAND

Record 6 from database: MEDLINE
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Title: Glucosamine sulfate for osteoarthritis [see comments]
Author: da Camara CC; Dowless GV
Address: School of Pharmacy, Campbell University, Buies Creek, NC, USA.
Source: Ann Pharmacother, 1998 May, 32:5, 580-7
Abstract: OBJECTIVE: To characterize the usefulness of glucosamine sulfate in the treatment of patients with osteoarthritis (OA). DATA SOURCES AND STUDY SELECTION: Pertinent citations were identified via a MEDLINE search (January 1975-March 1997). Only trials available in the English language involving human subjects, OA, and glucosamine sulfate were selected for review. DATA SYNTHESIS: OA is the most common form of arthritis and represents a major cause of morbidity and disability in the elderly. The main symptom of OA is pain and most of the commonly prescribed medications (e.g. acetaminophen, nonsteroidal antiinflammatory drugs) have been targeted at relieving the pain. Some of these medications have serious adverse effects and do not necessarily change the natural course of the disease. Glucosamine sulfate, a nutritional supplement, has recently emerged as an alternative treatment option for patients with OA. The beneficial effects of this chondroprotective agent have been reported to reverse or at least stop the progression of the disease without inducing serious adverse effects. Limited data from short-term human trials suggest that glucosamine sulfate administered orally, intravenously, intramuscularly, and intraarticularly may produce a gradual and progressive reduction in joint pain and tenderness, as well as improved range of motion and walking speed. Results of the trials have also shown that glucosamine has produced consistent benefits (> 50% overall improvement in symptom scores) in patients with OA and that, in some cases, it may be equal or superior to ibuprofen in controlling symptoms. CONCLUSIONS: There is evidence that glucosamine sulfate may provide pain relief, reduce tenderness, and improve mobility in patients with OA. Most of the current data, however, are derived from the European and Asian literature and there are no studies supporting the use of this agent in the US. The studies published to date have been done in small numbers of patients; adequate long-term trials examining the safety, efficacy, and optimal dosage requirements of glucosamine sulfate are lacking. Most of the available clinical data are difficult to interpret due to serious deficiencies in study design. Furthermore, studies evaluating the appropriate place of glucosamine sulfate in the therapeutic armamentarium of OA remain to be done.
Language of Publication: English
Unique Identifier: 98269325

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MeSH Heading (Major): Glucosamine|AE/*TU; Osteoarthritis|*DT
MeSH Heading: Anti-Inflammatory Agents, Non-Steroidal|TU; Clinical Trials; Human

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 1060-0280
Country of Publication: UNITED STATES

Record 7 from database: MEDLINE
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Title: The role of glucosamine sulfate and chondroitin sulfates in the treatment of degenerative joint disease.
Author: Kelly GS
Address
Source: Altern Med Rev, 1998 Feb, 3:1, 27-39
Abstract: Successful treatment of osteoarthritis must effectively control pain, and should slow down or reverse progression of the disease. Biochemical and pharmacological data combined with animal and human studies demonstrate glucosamine sulfate is capable of satisfying these criteria. Glucosamine sulfate's primary biological role in halting or reversing joint degeneration appears to be directly due to its ability to act as an essential substrate for, and to stimulate the biosynthesis of, the glycosaminoglycans and the hyaluronic acid backbone needed for the formation of proteoglycans found in the structural matrix of joints. Chondroitin sulfates, whether they are absorbed intact or broken into their constituent components, similarly provide additional substrates for the formation of a healthy joint matrix. Evidence also supports the oral administration of chondroitin sulfates for joint disease, both as an agent to slowly reduce symptoms and to reduce the need for non-steroidal anti-inflammatory drugs. The combined use of glucosamine sulfate and chondroitin sulfates in the treatment of degenerative joint disease has become an extremely popular supplementation protocol in arthritic conditions of the joints. Although glucosamine sulfate and chondroitin sulfates are often administered together, there is no information available to demonstrate the combination produces better results than glucosamine sulfate alone.
Language of Publication: English
Unique Identifier: 98262758

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MeSH Heading (Major): Chondroitin Sulfates|CH/ME/*TU; Glucosamine|ME/*TU; Osteoarthritis|*DT
MeSH Heading: Drug Therapy, Combination; Human

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 1089-5159
Country of Publication: UNITED STATES

Record 8 from database: MEDLINE
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Title: Pharmacology of alpha-glucosidase inhibition.
Author: Bischoff H
Address: Institute for Cardiovascular and Arteriosclerosis Research, Wuppertal, Germany.
Source: Eur J Clin Invest, 1994 Aug, 24 Suppl 3:, 3-10
Abstract: The development of alpha-amylase and brush-border alpha-glucosidase inhibitors is reviewed. The mode of action as well as pharmacological and pharmacodynamic properties of selected inhibitors with special regard to the most thoroughly investigated alpha-glucosidase inhibitor acarbose are discussed. Inhibition of intestinal alpha-glucosidases delays the digestion of starch and sucrose, flattens the postprandial blood glucose excursions, and thus mimics the effects of dieting on hyperglycaemia, hyperinsulinaemia and hypertriglyceridaemia. Therefore, the mechanism of alpha-glucosidase inhibition represents the pharmacological optimization of the dietary principle of delayed carbohydrate absorption. In pre-clinical studies using diabetic animals the oral administration of acarbose improved the metabolic state and reduced the blood glucose area under the curve. As a consequence, the process of non-enzymatic glycation of proteins was retarded as indicated by reduced glycated haemoglobin, glomerular basement membranes or advanced glycation end-products (AGEs) in collagen. These improved biochemical parameters correlated with beneficial effects against the development of diabetic nephropathy and neuropathy. Thus, the treatment of diabetic animals with acarbose does not only improve the metabolic state but has also the potential to delay, or possibly prevent, the development of diabetic complications.
Language of Publication: English
Unique Identifier: 95094873

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MeSH Heading (Major): alpha-Glucosidases|*AI; Dietary Carbohydrates|*; Hypoglycemic Agents|*PD; Trisaccharides|CH/*PD/TU
MeSH Heading: Animal; Blood Glucose|DE/ME; Carbohydrate Sequence; Diabetes Mellitus, Experimental|DT; Diabetic Nephropathies|PC; Diabetic Neuropathies|PC; Digestion; Glucosamine|AA/PD; Glycosylation End Products, Advanced|AI; Human; Insulin|BL; Molecular Sequence Data

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0014-2972
Country of Publication: ENGLAND

Record 9 from database: MEDLINE
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Title: The neglect of glucosamine as a treatment for osteoarthritis--a personal perspective.
Author: McCarty MF
Address
Source: Med Hypotheses, 1994 May, 42:5, 323-7
Abstract: Osteoarthritis results from progressive catabolic loss of cartilage proteoglycans, owing to an imbalance between synthesis and degradation. Standard drug therapy is only of palliative benefit and may exacerbate loss of cartilage. Glucosamine is an intermediate in mucopolysaccharide synthesis, and its availability in cartilage tissue culture can be rate-limiting for proteoglycan production. A number of double-blind studies dating from the early 1980s demonstrate that oral glucosamine decreases pain and improves mobility in osteoarthritis, without side effects. Nevertheless, medical researchers and physicians in the US have totally ignored this rational and safe therapeutic strategy. By mechanisms that are still unclear, the natural methyl donor S-adenosylmethionine also promotes production of cartilage proteoglycans, and is therapeutically beneficial in osteoarthritis in well-tolerated oral doses. These and other safe nutritional measures supporting proteoglycan synthesis, may offer a practical means of preventing or postponing the onset of osteoarthritis in older people or athletes.
Language of Publication: English
Unique Identifier: 95020811

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MeSH Heading (Major): Glucosamine|AE/*TU; Osteoarthritis|*DT/ME
MeSH Heading: Animal; Cartilage|DE/ME; Clinical Trials; Controlled Clinical Trials; Drug Tolerance; Human; Models, Biological; Proteoglycans|ME; S-Adenosylmethionine|TU

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0306-9877
Country of Publication: ENGLAND

Record 10 from database: MEDLINE
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Title: Glucosamine for psoriasis?
Author: McCarty MF
Address
Source: Med Hypotheses, 1997 May, 48:5, 437-41
Abstract: Amphiregulin and transforming growth factor-alpha, agonists for the epidermal growth factor receptor, are the major autocrine growth factors for cultured keratinocytes, and their substantial overexpression in psoriatic lesions suggests that they are crucial to the basal hyperplasia that characterizes psoriasis. Amphiregulin binds to heparin and related highly sulfated polysaccharides, and exogenous heparin blocks its growth factor activity, rationalizing previous reports that psoriasis responds to heparin therapy. Differentiating keratinocytes produce increased amounts of protein-bound as well as free-chain heparan sulfates, which may function physiologically as amphiregulin antagonists. By promoting keratinocyte synthesis of these heparan sulfates, glucosamine administration may inhibit amphiregulin function and thus provide therapeutic benefit in psoriasis. Concurrent ingestion of fish oil, by impeding the excessive activation of protein kinase C, may decrease keratinocyte production of amphiregulin and other autocrine growth factors, thus complementing the postulated benefits of glucosamine.
Language of Publication: English
Unique Identifier: 97328595

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MeSH Heading (Major): Glucosamine|AD/*TU; Psoriasis|*DT/ET/PP
MeSH Heading: Fish Oils|AD; Glycoproteins|PH; Growth Substances|PH; Heparitin Sulfate|PH; Human; Models, Biological; Receptors, Epidermal Growth Factor-Urogastrone|PH; Transforming Growth Factor alpha|PH

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0306-9877
Country of Publication: ENGLAND

Record 11 from database: MEDLINE
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Title: Glucosamine may retard atherogenesis by promoting endothelial production of heparan sulfate proteoglycans.
Author: McCarty MF
Address: Nutrition 21, San Diego, CA 92109, USA.
Source: Med Hypotheses, 1997 Mar, 48:3, 245-51
Abstract: Heparan sulfate proteoglycans produced by vascular endothelium may function physiologically to restrain the migration, multiplication, and phenotypic transition of vascular smooth-muscle cells, and to maintain an anticoagulant luminal surface by bonding and activating antithrombin III. Thus, ample production of heparan sulfate proteoglycans may act to prevent atherosclerosis and its thrombotic complications. The ability of exogenous heparin to stimulate synthesis of heparan sulfate proteoglycans by vascular endothelium may be largely responsible for the positive outcomes of most controlled evaluations of low-dose heparin as a long-term therapy for coronary disease. Glucosamine, a biosynthetic precursor of mucopolysaccharides, can substantially enhance mucopolysaccharide production when added to cultured fibroblasts or chondrocytes; the clinical utility of oral glucosamine in osteoarthritis may reflect increased synthesis of cartilage proteoglycans. It is reasonable to speculate that exogenous glucosamine will likewise enhance heparan sulfate proteoglycans production by vascular endothelial cells, and, when administered orally in regimens comparable to those effective in osteoarthritis, will thereby act to retard atherogenesis.
Language of Publication: English
Unique Identifier: 97285672

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MeSH Heading (Major): Atherosclerosis|*PC/PP; Endothelium, Vascular|DE/*ME; Glucosamine|*PD/*TU; Heparitin Sulfate|*BI; Models, Cardiovascular|*; Proteoglycans|*BI
MeSH Heading: Animal; Cartilage|DE/ME; Cells, Cultured; Coronary Disease|DT; Fibroblasts|DE/ME; Glycosaminoglycans|BI; Heparin|TU; Human

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0306-9877
Country of Publication: ENGLAND

Record 12 from database: MEDLINE
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Title: Conservative management of spinal osteoarthritis with glucosamine sulfate and chiropractic treatment.
Author: Gottlieb MS
Address
Source: J Manipulative Physiol Ther, 1997 Jul, 20:6, 400-14
Abstract: OBJECTIVE: To evaluate the rationale behind the most commonly used treatments of osteoarthritis, including nonsteroidal anti-inflammatory drugs (NSAIDs), and to assess more effective conservative treatment options. SUMMARY OF BACKGROUND DATA: This review includes a description of the pathophysiology and prevalence of osteoarthritis, joint physiology and NSAID treatment of osteoarthritis, as well as side effects on joints, the gastrointestinal tract, kidneys and livers. Several studies of conservative treatment, consisting of supplementation of glucosamine sulfate (which occurs naturally in the human body), exercise, and the use of chiropractic treatment for maintaining joint function and preventing further destruction, are reviewed. DATA SOURCES: A computerized search of Medline using the key indexing terms osteoarthritis, degenerative joint disease, nonsteroidal anti-inflammatory drugs, glucosamine sulfate, chiropractic and manipulation. RESULTS: Numerous studies wee obtained under each subheading and reviewed by category. Human and animal-model studies are described. CONCLUSION: The rationales for using NSAIDs in the treatment of osteoarthritis is controversial and openly contested. Given the detrimental effects of NSAIDs on joints and other organs, their use should be discouraged and their classification as a first choice conservative treatment should be abolished. A truly effective and conservative approach to the treatment of osteoarthritis should include chiropractic manipulation, essential nutrient supplementation, exogenous administration of glucosamine sulfate and rehabilitative stretches and exercises to maintain joint function. Because there is no correlation between pain levels and the extent of degeneration detected by radiographic or physical examination, conservative treatment should be initiated and sustained based on functional, objective findings and not strictly on how the patient feels. The use of NSAIDs should be limited to the treatment of gross inflammation and analgesics should only be used in the short-term when absolutely necessary for pain palliation. The present conservative approach could lead not only to a better quality of life but also to the saving of health care dollars by reducing the iatrogenic morbidity and mortality associated with NSAID use.
Language of Publication: English
Unique Identifier: 97418499

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MeSH Heading (Major): Anti-Inflammatory Agents, Non-Steroidal|*TU; Chiropractic|*; Glucosamine|*TU; Osteoarthritis|DT/PP/*TH; Spinal Diseases|DT/*TH
MeSH Heading: Combined Modality Therapy; Diet; Glycosaminoglycans|ME; Human; Joints|DE/PH

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0161-4754
Country of Publication: UNITED STATES

Record 13 from database: MEDLINE
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Title: Drug treatment of arthritis. Update on conventional and less conventional methods.
Author: Spencer-Green G
Address: Dartmouth-Hitchcock Medical Center, Lebanon, NH 03756.
Source: Postgrad Med, 1993 May 15, 93:7, 129-40
Abstract: Nonsteroidal anti-inflammatory drugs comprise an important class of medications that reduce the signs and symptoms of osteoarthritis and rheumatoid arthritis. They bring relief to millions of people but do not eliminate underlying disease. Disease-modifying antirheumatic drugs also bring relief, but these drugs are often ineffective and not well tolerated. Failure to provide long-term benefits combined with the high toxicity of most of the disease-modifying agents has prompted a search for more effective treatments. New methods using modern technologies have generated much enthusiasm and hold promise for the future. In the meantime, administration of nonsteroidal anti-inflammatory drugs and judicious use of disease-modifying agents remain the cornerstone of therapy for arthritis.
Language of Publication: English
Unique Identifier: 93261929

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MeSH Heading (Major): Anti-Inflammatory Agents, Non-Steroidal|PD/*TU; Arthritis, Rheumatoid|*DT; Osteoarthritis|*DT
MeSH Heading: Adrenal Cortex Hormones|TU; Aurothioglucose|TU; Azathioprine|TU; Glucosamine|AA/TU; Gold Sodium Thiomalate|TU; Human; Hydroxychloroquine|TU; Methotrexate|TU

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0032-5481
Country of Publication: UNITED STATES
CAS Registry/EC Number: 0 (Adrenal Cortex Hormones); 0 (Anti-Inflammatory Agents, Non-Steroidal); 118-42-3 (Hydroxychloroquine); 12192-57-3 (Aurothioglucose); 12244-57-4 (Gold Sodium Thiomalate); 3416-24-8 (Glucosamine); 446-86-6 (Azathioprine); 56824-20-5 (amiprilose); 59-05-2 (Methotrexate)

Record 14 from database: MEDLINE
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Title: Severe rheumatoid arthritis: current options in drug therapy.
Author: Kremer JM
Address: Division of Rheumatology, Albany Medical College, New York.
Source: Geriatrics, 1990 Dec, 45:12, 43-8
Abstract: Therapeutic advances have been made in rheumatoid arthritis (RA), but patients (and sometimes physicians) may become frustrated at the apparent lack of breakthrough treatments. The latest advances in the treatment of severe RA are discussed, along with what investigators are using experimentally both in combination with other drugs and alone to treat RA now and, possibly, in the future. These agents include methotrexate, cyclosporine, gamma-interferon, and omega-3 fatty acids.
Language of Publication: English
Unique Identifier: 91071618

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MeSH Heading (Major): Arthritis, Rheumatoid|*DT/TH; Clinical Protocols|*ST
MeSH Heading: Anti-Inflammatory Agents, Non-Steroidal|TU; Antibodies, Monoclonal|TU; Aspirin|TU; Cyclosporins|TU; Drug Therapy, Combination; Fatty Acids, Omega-3|TU; Glucosamine|AA/TU; Human; Hydroxychloroquine|TU; Interferon Type II|TU; Methotrexate|TU

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0016-867X
Country of Publication: UNITED STATES
CAS Registry/EC Number: 0 (Antibodies, Monoclonal); 0 (Cyclosporins); 0 (Fatty Acids, Omega-3); 118-42-3 (Hydroxychloroquine); 3416-24-8 (Glucosamine); 50-78-2 (Aspirin); 56824-20-5 (amiprilose); 59-05-2 (Methotrexate); 82115-62-6 (Interferon Type II)

Record 15 from database: MEDLINE
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Title: The actions of parathyroid hormone on bone: relation to bone remodeling and turnover, calcium homeostasis, and metabolic bone diseases. II. PTH and bone cells: bone turnover and plasma calcium regulation.
Author: Parfitt AM
Address
Source: Metabolism, 1976 Aug, 25:8, 909-55
Abstract: Kinetic and morphologic studies in patients with parathyroid disease, and a wide variety of studies in experimental animals indicate that one major effect of PTH is to increase the proliferation of osteoprogenitor cells into osteoclasts and so to increase bone turnover. PTH stimulates bone cells by increasing cell membrane permeability to calcium and consequently increasing calcium influx and by activating membrane-bound adenyl-cyclase. It is likely that the former event precedes the latter and that calcium is the second messenger and cyclic AMP the third messenger. PTH increases the production by bone cells of lactate, citric and carbonic acids, lysosomal enzymes, collagenase, and hyaluronic acid, some or all of which are concerned in the mechanism of bone resorption. With the exception of lactate which probably comes mainly from osteocytes, the increase in metabolic activity is largely due to the increase in the number of osteoclasts. There is also ultrastructural, biochemical, and biophysical evidence that PTH stimulates existing osteoclasts, but this most likely represents the transformation of inactive cells into an active state, and is a transient and nonsustainable effect. As yet, there is no evidence that either increased osteoprogenitor cell proliferation or increased osteoclast activity is mediated by adenyl-cyclase activation. PTH also acts on the deep osteocyte to cause rapid mobilization of calcium from the zone of hypomineralized metabolically active perilacunar bone. This effect is mediated by adenyl-cyclase activation and is preceded by a slight fall in plasma calcium probably due to the movement of calcium into bone cells. The function of this rapid hypercalcemic response to PTH is correct errors in the prevailing steady-state level of plasma calcium...
Language of Publication: English
Unique Identifier: 76242326

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MeSH Heading (Major): Bone and Bones|DE/*PH; Calcium|BL/*ME/PD; Parathyroid Hormones|*PH
MeSH Heading: Animal; Bone Development; Bone Resorption; Carbonic Acid|ME; Glucosamine|ME; Homeostasis; Human; Hypercalcemia|ET; Hyperparathyroidism|ME; Hypoparathyroidism|ME; Lysosomes|EN; Mast Cells|PH; Microbial Collagenase|ME; Models, Biological; Osteoclasts|PH; Osteocytes|PH; Parathyroid Glands|PH; Phosphates|PH

Publication Type: JOURNAL ARTICLE; REVIEW
ISSN: 0026-0495
Country of Publication: UNITED STATES

Record 16 from database: MEDLINE
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Title: Carbohydrate metabolism and the glucoreceptor mechanism.
Author: Ashcroft SJ; Sugden MC; Williams IH
Address
Source: Horm Metab Res Suppl, 1980, Suppl 10:, 1-7
Abstract: Current views on the recognition of sugars as signals for insulin biosynthesis and release are discussed. Evidence is presented that the initial steps in the metabolism of N-acetyl-glucosamine differ from those in glucose metabolism in that for the former transport into the islet represents the rate-limiting step. Different enzymes phosphorylate these two sugar, but it is suggested that N-acetylglucosamine and glucose enter the beta-cell via the same carrier since 3-O-methylglucose is shown to be a competitive inhibitor of N-acetylglucosamine oxidation. Inhibitory effects on N-acetylglucosamine oxidation are also observed with caffeine, 3-isobutyl-methylxanthine and phloretin. Inhibition of N-acetylglucosamine metabolism is associated with inhibition of N-acetylglucosamine-stimulated insulin release and biosynthesis. Methylxanthines also inhibit uptake of 45Ca2+ by islet mitochondria. The possible physiological role of islet mitochondrial Ca2+ uptake in the regulation of beta-cell cytosolic Ca2+ concentration is discussed.
Language of Publication: English
Unique Identifier: 81092241

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MeSH Heading (Major): Acetylglucosamine|*ME; Glucosamine|*AA; Glucose|*ME; Islets of Langerhans|DE/*ME; Receptors, Cell Surface|*ME
MeSH Heading: Animal; Caffeine|PD; Calcium|ME; Cyclic AMP|ME; Human; Insulin|ME; Mitochondria|ME; Support, Non-U.S. Gov't; 1-Methyl-3-isobutylxanthine|PD

Publication Type: JOURNAL ARTICLE; REVIEW
ISSN: 0018-5043
Country of Publication: GERMANY, WEST
CAS Registry/EC Number: 0 (glucose receptor); 0 (Receptors, Cell Surface); 11061-68-0 (Insulin); 28822-58-4 (1-Methyl-3-isobutylxanthine); 3416-24-8 (Glucosamine); 50-99-7 (Glucose); 58-08-2 (Caffeine); 60-92-4 (Cyclic AMP); 7440-70-2 (Calcium); 7512-17-6 (Acetylglucosamine)

Record 17 from database: MEDLINE
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Title: Aspartylglycosaminuria: an inborn error of glycoprotein catabolism.
Author: Maury CP
Address
Source: J Inherit Metab Dis, 1982, 5:4, 192-6
Abstract: Aspartylglycosaminuria (AGU, McKusick 20840) is a metabolic disorder affecting the catabolism of glycoproteins. It was first described in 1967, by Jenner and Pollitt, in two mentally retarded English siblings. Subsequently several cases were reported from Finland (Palo and Mattsson, 1970; Autio, 1972; Autio et al., 1973). Today the number of known cases is about 140, most of them Finnish or of Finnish origin (Aula et al., 1980). The incidence of AGU in Finland has been estimated to be approximately 1:26000 and the disease is inherited as an autosomal recessive trait (Autio et al., 1973). Clinical manifestations include progressive mental retardation, coarse gargoyle-like facial features, skeletal abnormalities and recurrent infections. Early development of the patients is usually normal, but by the age of 5-15 years they are already severely retarded (Autio, 1972; Autio et al., 1973). Morphologically AGU is a generalized storage disease (Haltia et al., 1975). Affected tissues show enlarged lysosomes. Vacuolization is a prominent feature of liver and nerve cells (Haltia et al., 1975) and of peripheral lymphocytes (Aula et al., 1975).
Language of Publication: English
Unique Identifier: 83190526

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MeSH Heading (Major): Acetylglucosamine|*AA/PH/UR; Glucosamine|*AA; Glycoproteins|*ME; Metabolism, Inborn Errors|DI/*ME/UR
MeSH Heading: Brain|ME; Human; Liver|ME

Publication Type: JOURNAL ARTICLE; REVIEW
ISSN: 0141-8955
Country of Publication: ENGLAND
CAS Registry/EC Number: 0 (Glycoproteins); 2776-93-4 (N-acetylglucosaminylasparagine); 3416-24-8 (Glucosamine); 7512-17-6 (Acetylglucosamine)

Record 18 from database: MEDLINE
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Title: Clinical research in osteoarthritis: design and results of short-term and long-term trials with disease-modifying drugs.
Author: Rovati LC
Address: Department of Clinical Pharmacology, Rotta Research Laboratorium S.p.A., Monza, Italy.
Source: Int J Tissue React, 1992, 14:5, 243-51
Abstract: Putative disease-modifying drugs are usually clinically used in osteoarthritis with two main aims: not only stopping or reducing the cartilage degenerative process after a long-term treatment, but also controlling the symptoms of the disease within a few days or weeks, thus avoiding or diminishing the use of symptomatic medications. Due to the difficulties of implementing the first aim, the latter aim was more often investigated, even if most often with inadequate study design and insufficient numbers of patients. We have recently carried out three double-blind, controlled, parallel groups, randomized, 4-6 week trials of glucosamine sulphate versus placebo or the NSAID ibuprofen on a total of 606 gonarthrosic out-patients. Movement limitation and pain were scored according to the Lequesne index, and the efficacy goals were strictly pre-determined. Access to other medications was not allowed. Glucosamine was significantly more effective than placebo, while no difference was detected in comparison with the NSAID (p < 0.025 and p = 0.77, respectively: Fisher's two-tailed exact test). On the other hand, glucosamine was as well tolerated as placebo, while the percentage of patients suffering adverse drug reactions was higher in the ibuprofen group (37% vs 7%: p < 0.001). Long-term trials are in progress and several aspects are to be considered in their design: they must be double-blind, placebo-controlled, randomized, continued for a period of years and (most importantly) with the careful use of imaging and biochemical techniques capable of generating objective evaluation criteria.
Language of Publication: English
Unique Identifier: 93239409

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MeSH Heading (Major): Osteoarthritis|*DT; Research Design|*
MeSH Heading: Clinical Trials; Double-Blind Method; Drug Administration Schedule; Human; Randomized Controlled Trials; Time Factors

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0250-0868
Country of Publication: SWITZERLAND

Record 19 from database: MEDLINE
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Title: Structure-activity relationships in lipopolysaccharides of Bacteroides fragilis.
Author: Lindberg AA; Weintraub A; Zähringer U; Rietschel ET
Address: Department of Clinical Bacteriology, Karolinska Institute, Huddinge University Hospital, Sweden.
Source: Rev Infect Dis, 1990 Jan-Feb, 12 Suppl 2:, S133-41
Abstract: The endotoxic activity of lipopolysaccharide (LPS) extracted from the envelope of Bacteroides fragilis is low compared with that of LPS from Escherichia coli, Salmonella, and other Enterobacteriaceae. Thus, pyrogenicity, the ability to prepare for or provoke the local Shwartzman reaction, and the ability to induce the production of interleukin 1 are reduced by 100- to 1,000-fold. Structural analyses of characterized B. fragilis LPS have shown that its lipid A is composed of a beta 1,6-linked D-glucosamine disaccharide that has the following properties: (1) a phosphate group on C1 of the reducing amino sugar, (2) amide- and ester-linked 3-hydroxylated branched and nonbranched long-chain (C15-C17) fatty acids, (3) an average of five fatty acids per glucosamine disaccharide, and (4) the core and O-antigenic saccharide chain linked to C6 of the nonreducing glucosamine residue. Although structurally similar to lipid A of E. coli, the lipid A of B. fragilis differs by its lack of the phosphate group on C4 of the nonreducing amino sugar and by the presence of fewer and different fatty acids. These differences explain the low endotoxic activity of B. fragilis LPS. The core and O-antigenic chain are linked to lipid A via a phosphorylated 2-keto-3-deoxyoctonate (KDO) residue. The saccharide chain is short and is composed of L-rhamnose, D-glucose, and D-galactose, with the O-antigenic specificity determined by a beta 1,6-linked D-galactose oligomer. This O-antigenic specificity was present in 14 of 17 strains of B. fragilis that were investigated.
Language of Publication: English
Unique Identifier: 90161741

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MeSH Heading (Major): Bacteroides fragilis|*; Lipopolysaccharides|*AN/TO
MeSH Heading: Animal; Carbohydrate Conformation; Carbohydrate Sequence; Human; Lipid A|AN/TO; Molecular Sequence Data; Monosaccharides|AN; Structure-Activity Relationship; Support, Non-U.S. Gov't

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0162-0886
Country of Publication: UNITED STATES
CAS Registry/EC Number: 0 (Lipid A); 0 (Lipopolysaccharides); 0 (Monosaccharides)

Record 20 from database: MEDLINE
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Title: Heparan sulphate in the binding and activation of basic fibroblast growth factor.
Author: Gallagher JT; Turnbull JE
Address: Department of Medical Oncology, Christie Hospital NHS Trust, Manchester, UK.
Source: Glycobiology, 1992 Dec, 2:6, 523-8
Abstract: Heparan sulphate proteoglycans (HSPGs) are widely distributed in animal tissues, but their most prominent locations are cell surface membranes and basement membranes. Their influence on various fundamental aspects of cell behaviour (e.g. cell adhesion, growth and morphogenesis) are dependent on the specific binding properties of the heparan sulphate (HS) chains. These polysaccharides are complex structures in which N-sulphated glucosamine and ester sulphate groups tend to be clustered in discrete regions of the chain separated by sequences enriched in N-acetylglucosamine residues, but with a low sulphate concentration. The sulphated domains contain the sugar residue sequences for interaction with specific proteins essential for HS function. In this review, we describe the plasma membrane HSPGs and their role in regulating the activity of basic fibroblast growth factor (bFGF).
Language of Publication: English
Unique Identifier: 93113099

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MeSH Heading (Major): Fibroblast Growth Factor, Basic|*ME; Heparitin Sulfate|BI/CH/*ME
MeSH Heading: Animal; Binding Sites; Carbohydrate Sequence; Cell Membrane|ME; Human; Molecular Sequence Data; Proteoglycans|CH/ME; Support, Non-U.S. Gov't

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0959-6658
Country of Publication: ENGLAND
CAS Registry/EC Number: 0 (heparan sulfate proteoglycan); 0 (Fibroblast Growth Factor, Basic); 0 (Proteoglycans); 9050-30-0 (Heparitin Sulfate)

Record 21 from database: MEDLINE
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Title: Prostate-specific antigen and history of its discovery.
Author: Zaviacic M
Address: Institute of Pathology, School of Medicine, Comenius University, Bratislava. Zaviacic@fmed.uniba.sk
Source: Bratisl Lek Listy, 1997 Dec, 98:12, 659-62
Abstract: In contradistinction to prostatic acid phosphatase (PAcP), prostate-specific antigen (PSA) is currently the most reliable and most frequently used marker for identification of normal and pathologically altered prostatic tissues both in the male and female. In clinical practice, it has become an appreciated serum marker in the assessment and management of prostate carcinoma in the male, although it is far from being a perfect "tumor" marker. Our knowledge on female PSA is expected to be broadened by the introduction of novel highly sensitive serological methods (IMMULITE--immunochemiluminiscent third-generation PSA assay and others), which in some females have already demonstrated surprisingly high values. Biochemically, PSA in seminal fluid in its free form has a molecular weight of about 30,000 daltons, while in serum, where it occurs in the complex form with alpha1-chymotrypsin, its molecular weight is approximately 100,000 daltons being comparable to that of PAcP. On immunohistochemical examination, PSA is expressed in the highly specialized apically-superficial layer of male and female secretory (luminal) cells of the prostatic glands, as well as at other sites of the urogenital tract, frequently coinciding with glucosamine glucans, glycoproteins and numerous enzyme proteins. With regard to the increasing interest in PSA evidenced in urology, gynecological urology, in the orthology and pathology of male and female prostates, the interest in the history of discovery of this exceptional prostatic marker appears to be justified. PSA was discovered by Richard Ablin and co-workers in the USA, who published their pioneer work in the Journal of Reproduction and Fertility and in the Journal of Immunology as early as in 1970. Thus their results had been available nine years before the publication of Wang et al. appeared in Investigative Urology (1979), on the basis of which the latter are frequently incorrectly considered and cited as the authors of PSA discovery. (Ref. 46.)
Language of Publication: English
Unique Identifier: 98185775

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MeSH Heading (Major): Prostate-Specific Antigen|*/HI/ME/PH
MeSH Heading: Female; History of Medicine, 20th Cent.; Human; Male; Prostatic Neoplasms|DI; Urethra|ME

Publication Type: HISTORICAL ARTICLE; JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0006-9248
Country of Publication: SLOVAKIA

Record 22 from database: MEDLINE
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Title: The role of phosphometabolites in cell proliferation, energy metabolism, and tumor therapy.
Author: Mazurek S; Boschek CB; Eigenbrodt E
Address: Institute for Biochemistry and Endocrinology, Veterinary Faculty, University of Giessen, Germany.
Source: J Bioenerg Biomembr, 1997 Aug, 29:4, 315-30
Abstract: A common characteristic of tumor cells is the constant overexpression of glycolytic and glutaminolytic enzymes. In tumor cells the hyperactive hexokinase and the partly inactive pyruvate kinase lead to an expansion of all phosphometabolites from glucose 6-phosphate to phosphoenolpyruvate. In addition to the glycolytic phosphometabolites, synthesis of their metabolic derivatives such as P-ribose-PP, NADH, NADPH, UTP, CTP, and UDP-N-acetyl glucosamine is also enhanced during cell proliferation. Another phosphometabolite derived from P-ribose-PP, AMP, inhibits cell proliferation. The accumulation of AMP inhibits both P-ribose-PP-synthetase and the increase in concentration of phosphometabolites derived from P-ribose-PP. In cells with low glycerol 3-phosphate and malate-aspartate shuttle capacities the inhibition of the lactate dehydrogenase by low NADH levels leads to an inhibition of glycolytic ATP production. Several tumor-therapeutic drugs reduce NAD and NADH levels, thereby inhibiting glycolytic energy production. The role of AMP, NADH, and NADPH levels in the success of chemotherapeutic treatment is discussed.
Language of Publication: English
Unique Identifier: 98048333

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MeSH Heading (Major): Cell Division|*; Energy Metabolism|*/DE; Neoplasms|DT/*ME/PA; Phosphates|*ME
MeSH Heading: Antineoplastic Agents|PD; Apoptosis; Glutamine|ME; Glycolysis; Human; Neoplasm Metastasis; Support, Non-U.S. Gov't

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
ISSN: 0145-479X
Country of Publication: UNITED STATES

Record 23 from database: MEDLINE
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Title: How does hyperglycaemia predispose to diabetic nephropathy?
Author: Wardle EN
Address
Source: QJM, 1996 Dec, 89:12, 943-51
Abstract: Diabetic nephropathy is preceded by 'hyperfiltration' mediated by dilatation of the afferent arterioles to the glomeruli by means of IGF-1, prostaglandins, bradykinin, nitric oxide and atrial natriuretic peptide, together with constriction of the efferent arterioles by local thromboxane A2. Raised glomerular intracapillary pressures might then contribute to glomerulosclerosis, but in any case there is permeability of the vascular endothelium. AGEPs and lipid peroxides can explain this. AGEPs, or simply intermittently high levels of glucose, also account for synthesis of extracellular matrix proteins that lead to thickening of the basement membrane and glomerulosclerosis. Another glucose product, glucosamine-6-phosphate, is formed when there is hexosamine flux along with insulin resistance in tissues, and is implicated in glomerulosclerosis, since it also stimulates TGF-beta transcription. In seeking to explain proteinuria, depletion of heparan sulphates from the endothelial cells and GBM is now established as a principal cause. In addition to a high glucose reducing the synthesis of heparan sulphates, it has now been shown that high glucose may depress the synthesis of heparin sulphate proteoglycan.
Language of Publication: English
Unique Identifier: 97167871

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MeSH Heading (Major): Diabetic Nephropathies|*ET/ME/PA; Hyperglycemia|*CO/ME/PA
MeSH Heading: Enzyme Activation; Glycosylation; Heparin|ME; Human; Kidney|PA; Protein Kinase C|ME; Thromboxane A2|ME

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
Country of Publication: ENGLAND

Record 24 from database: MEDLINE
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Title: Interactions of human malaria parasites, Plasmodium vivax and P.falciparum, with the midgut of Anopheles mosquitoes.
Author: Ramasamy MS; Kulasekera R; Wanniarachchi IC; Srikrishnaraj KA; Ramasamy R
Address: Division of Life Sciences, Institute of Fundamental Studies, Kandy, Sri Lanka.
Source: Med Vet Entomol, 1997 Jul, 11:3, 290-6
Abstract: Present understanding of the development of sexual stages of the human malaria parasites Plasmodium vivax and P.falciparum in the Anopheles vector is reviewed, with particular reference to the role of the mosquito midgut in establishing an infection. The sexual stages of the parasite, the gametocytes, are formed in human erythrocytes. The changes in temperature and pH encountered by the gametocyte induce gametogenesis in the lumen of the midgut. Macromolecules derived from mosquito tissue and second messenger pathways regulate events leading to fertilization. In An.tessellatus the movement of the ookinete from the lumen to the midgut epithelium is linked to the release of trypsin in the midgut and the peritrophic matrix is not a firm barrier to this movement. The passage of the P.vivax ookinete through the peritrophic matrix may take place before the latter is fully formed. The late ookinete development in P.falciparum requires chitinase to facilitate penetration of the peritrophic matrix. Recognition sites for the ookinetes are present on the midgut epithelial cells. N-acetyl glucosamine residues in the oligosaccharide side chains of An.tessellatus midgut glycoproteins and peritrophic matrix proteoglycan may function as recognition sites for P.vivax and P.falciparum ookinetes. It is possible that ookinetes penetrating epithelial cells produce stress in the vector. Mosquito molecules may be involved in oocyst development in the basal lamina, and encapsulation of the parasite occurs in vectors that are refractory to the parasite. Detailed knowledge of vector-parasite interactions, particularly in the midgut and the identification of critical mosquito molecules offers prospects for manipulating the vector for the control of malaria.
Language of Publication: English
Unique Identifier: 97471321

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MeSH Heading (Major): Anopheles|*PS; Digestive System|*PS; Plasmodium falciparum|*PH; Plasmodium vivax|*PH
MeSH Heading: Animal; Erythrocytes|PH; Host-Parasite Relations; Human; Life Cycle Stages; Reproduction; Support, Non-U.S. Gov't

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0269-283X
Country of Publication: ENGLAND

Record 25 from database: MEDLINE
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Title: Shedding of CD9 antigen in acute lymphoblastic leukemia.
Author: Komada Y; Sakurai M
Address: Department of Pediatrics, Mie University School of Medicine, Japan.
Source: Leuk Lymphoma, 1994 Feb, 12:5-6, 365-72
Abstract: A leukemia-associated CD9 glycoprotein antigen released into the extracellular milieu from acute lymphoblastic leukemia cells has been detected using a unique lectin-monoclonal antibody immunoassay. It has been demonstrated that the release of CD9 antigen is an active process and is associated with active cell growth. In addition, the difference of carbohydrate moiety, and hence glycosylation, in the CD9 antigen derived from lymphoblasts and neuroblasts was verified using lectin affinity chromatography. The lectin affinity of the carbohydrate moiety of lymphoblast CD9 antigen would indicate the presence of N-linked oligosaccharide chains having groups of N-acetyl glucosamine residues, a mannose core and a terminal D-galactose. The soluble CD9 antigen is specifically detected in plasma from ALL patients at the time of diagnosis, in cerebrospinal fluid from patients with central nervous system involvement, and spent medium from CD9-positive leukemic blasts obtained at the time of diagnosis. Interestingly when bone marrow cells taken from patients in complete remission were studied, a distinct amount of CD9 antigen was released into spent medium in some of the cases. All of these patients have subsequently developed hematological relapse. The present data suggest that shedding of CD9 antigen by leukemic cells may enable the clinical monitoring of residual leukemic cell burden.
Language of Publication: English
Unique Identifier: 94236127

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MeSH Heading (Major): Antigens, CD|*AN/CF; Leukemia, Lymphocytic, Acute|*IM
MeSH Heading: Human

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 1042-8194
Country of Publication: SWITZERLAND

Record 26 from database: MEDLINE
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Title: Ectodomain interactions of leukocyte integrins and pro-inflammatory GPI-linked membrane proteins.
Author: Petty HR; Kindzelskii AL; Adachi Y; Todd RF 3rd
Address: Department of Biological Sciences, Wayne State University, Detroit, MI 48202, USA.
Source: J Pharm Biomed Anal, 1997 Jun, 15:9-10, 1405-16
Abstract: Although glycosylphosphatidyl-inositol (GPI) linked membrane proteins do not possess transmembrane or cytosolic sequences they elicit transmembrane signals. Using microscopic fluorescence imaging and resonance energy transfer (RET) techniques we have shown that certain pro-inflammatory GPI-linked membrane proteins can interact with leukocyte beta 2 integrins (complement receptor type 3 (CR3) and 4 (CR4) and the leukocyte function-associated antigen-1 (LFA-1)). For example, physical associations between CR3 and Fc gamma RIIIB, CR3 and urokinase receptors, and CR3 and CD14 (lipopolysaccharide receptor) have been found. Although Fc gamma RIIIB appears to be constitutively associated with CR3, urokinase receptors and CD14 associations with CR3 are influenced by their ligation status and cell function (e.g. adherence and locomotion). CR3-to-urokinase receptor interactions have been confirmed by immunoprecipitation techniques. Immunoprecipitation of CR3 from Brij-58 lysates after biotinylation of neutrophil membranes revealed proteins of M(r) = 40,000, 50,000, 74,000 and 120,000, in addition to bands corresponding to the integrin alpha and beta chains. Cell functions such as transmembrane signaling and superoxide release/priming have been linked to these interactions. Importantly, reagents that affect the lectin-like site of CR3, such as N-acetyl-D-glucosamine, alpha-methyl-D-mannoside and beta-glucan alter these interactions and, in parallel, leukocyte functions. Thus, the interactions of GPI-linked proteins and integrins can be highly dynamic events linked to cell activities. Our studies suggest that it may be possible to develop new drugs directed at the lectin-like site of beta 2 integrins that block GPI-linked protein-to-integrin coupling thereby controlling inflammatory cell processes including cell adherence, locomotion and activation. Such drugs may be useful in clinical conditions such as ischemia-reperfusion injury, sepsis, arthritis and others.
Language of Publication: English
Unique Identifier: 97370194

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MeSH Heading (Major): Antigens, CD18|*BL; Glycosylphosphatidylinositols|*CH; Inflammation Mediators|*CH; Leukocytes|*CH; Membrane Proteins|*CH; Protein Structure, Tertiary|*
MeSH Heading: Carbohydrate Conformation; Human; Macrophage-1 Antigen|BL; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0731-7085
Country of Publication: ENGLAND

Record 27 from database: MEDLINE
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Title: Effect of low molecular weight heparin preparations on the inhibition of thrombin by heparin cofactor II.
Author: Tollefsen DM; Sugimori T; Maimone MM
Address: Department of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110.
Source: Semin Thromb Hemost, 1990 Oct, 16 Suppl:, 66-70
Abstract: 1. Heparin molecules approximately 24 to 30 residues in length are required to catalyze the thrombin-HC II reaction. The requirement for heparin molecules of this length is consistent with a model for catalysis in which heparin binds HC II and thrombin simultaneously to form a ternary complex in a manner similar to that proposed for the thrombin-AT III reaction. Smaller molecules (18 or more monosaccharide units in length) are required to catalyze the thrombin-AT III reaction. 2. The specific AT III-binding pentasaccharide containing 3-O-sulfated glucosamine is not required for activity with HC II. 3. Some low molecular weight heparin preparations have significant activity with HC II (approximately 10 to 20% that of standard heparin). This is probably related to the presence of species with molecular weights greater than 6000 to 7500 (24 to 30 monosaccharide units) in these preparations.
Language of Publication: English
Unique Identifier: 91142784

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MeSH Heading (Major): Heparin Cofactor II|*PH; Heparin, Low-Molecular-Weight|*PD; Thrombin|*AI
MeSH Heading: Antithrombin III|PH; Human; Oligosaccharides|PD

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0094-6176
Country of Publication: UNITED STATES
CAS Registry/EC Number: EC 3.4.21.5 (Thrombin); 0 (Heparin, Low-Molecular-Weight); 0 (Oligosaccharides); 81604-65-1 (Heparin Cofactor II); 9000-94-6 (Antithrombin III)

Record 28 from database: MEDLINE
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Title: The PIG-A gene somatic mutation responsible for paroxysmal nocturnal hemoglobinuria.
Author: Rotoli B; Boccuni P
Address: Division of Hematology, Federico II University Medical School, Naples, Italy.
Source: Haematologica, 1995 Nov, 80:6, 539-45
Abstract: Paroxysmal nocturnal hemoglobinuria is the first example of a non neoplastic human disease caused by the somatic mutation of an X-linked gene. The PIG-A gene maps to Xp22.1 and is required for the transfer of N-acetyl glucosamine to phosphoinositol, an early step in the production of the GPI anchor. A deficiency of GPI-linked proteins on the cell surface is responsible for the PNH cell defect, which can be detected by flow cytometry not only on red cells, but also on myeloid cells and in some patients even on lymphoid cells. Its location on the X-chromosome explains how a single recessive mutation can cause the appearance of the abnormal clone. A number of patients may have more than one PNH clone, suggesting that the expansion of GPI-deficient clones occurs under the pressure of a selection mechanism.
Language of Publication: English
Unique Identifier: 96226664

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MeSH Heading (Major): Hemoglobinuria, Paroxysmal|*GE; Point Mutation|*
MeSH Heading: Human; Linkage (Genetics); Support, Non-U.S. Gov't; X Chromosome

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0390-6078
Country of Publication: ITALY

Record 29 from database: MEDLINE
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Title: Mucin glycoproteins as tumor markers.
Author: Feller WF; Henslee JG; Kinders RJ; Manderino GL; Tomita JT; Rittenhouse HG
Address: Georgetown University School of Medicine, Washington, D.C.
Source: Immunol Ser, 1990, 53:, 631-72
Abstract: Extensive biochemical studies have shown that mucin tumor antigens have a range of molecular sizes from 200 to greater than 1000 kDa. The molecular size of mucin antigens can be dramatically affected by the source and method of purification. Mucin antigens vary from 24 to 80% in carbohydrate content and their density is usually greater than 1.40 g/ml. Galactose and N-acetyl glucosamine are the predominant sugar residues in many mucins, whereas mannose is usually present in low levels or absent. The amino acids serine, threonine, alanine, glycine, and proline are abundant in mucins. An O-glycosidic linkage between the carbohydrate and protein of mucins is the most common linkage encountered. The gene encoding the core peptide for at least one mucin tumor marker, HMFG, has been identified, sequenced, and expressed. These findings may lead to a better understanding of the multiepitope nature of mucin tumor markers. The advent of hybridoma technology has yielded several monoclonal antibodies that have been used to identify the presence of tumor-associated mucins in the sera of cancer patients. Elevated levels of mucin antigens have been found in the serum of most patients with advanced adenocarcinomas. Many studies have shown that tumor-associated markers are useful in monitoring patients following cancer treatment. Clinically useful immunoassays have been developed for monitoring patients with ovarian, breast, and pancreatic adenocarcinomas. Although individual mucin tumor markers show limited utility in detecting early adenocarcinoma, recent studies using multiple mucin markers have suggested that early detection, at sensitivities greater than 50%, can be achieved.
Language of Publication: English
Unique Identifier: 91308321

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MeSH Heading (Major): Antigens, Neoplasm|*AN; Glycoproteins|*AN/BI/IM; Mucins|*AN/IM; Neoplasm Proteins|*AN/BI/IM; Neoplasms|*DI; Tumor Markers, Biological|*AN
MeSH Heading: Animal; Antibodies, Monoclonal|DU; Female; Glycosylation; Human; Male; Predictive Value of Tests; Protein Processing, Post-Translational; Species Specificity

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
ISSN: 0092-6019
Country of Publication: UNITED STATES
CAS Registry/EC Number: 0 (Antibodies, Monoclonal); 0 (Antigens, Neoplasm); 0 (Glycoproteins); 0 (Mucins); 0 (Neoplasm Proteins); 0 (Tumor Markers, Biological)

Record 30 from database: MEDLINE
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Title: Involvement of heparan sulfate and related molecules in sequestration and growth promoting activity of fibroblast growth factor.
Author: Vlodavsky I; Miao HQ; Medalion B; Danagher P; Ron D
Address: Department of Oncology, Hadassah-Hebrew University Hospital, Jerusalem, Israel.
Source: Cancer Metastasis Rev, 1996 Jun, 15:2, 177-86
Abstract: Heparan sulfate proteoglycans (HSPGs) are ubiquitous macromolecules associated with the cell surface and extracellular matrix (ECM) of a wide range of cells of vertebrate and invertebrate tissues [1, 2]. The basic HSPG structure consists of a protein core to which several linear heparan sulfate (HS) chains are covalently attached. The polysaccharide chains are typically composed of repeating hexuronic and D-glucosamine disaccharide units that are substituted to a varying extent with N- and O-linked sulfate moieties and N-linked acetyl groups [1, 2]. Beside serving as a scaffold for the attachment of various ECM components (e.g., collagen, laminin, fibronectin), the binding of HS to certain proteins has been suggested to induce a conformational change which may lead to the exposure of novel reactive determinants or conversely stabilize an inert protein configuration [1-4]. Of particular significance is the interaction of HS with fibroblast growth factors (FGFs), mediating their sequestration, stabilization and high affinity receptor binding and signaling [3-7]. Cellular responses to FGFs may hence be modulated by metabolic inhibitors of HS synthesis and sulfation, HS-degrading enzymes, and synthetic mimetics of heparin/HS. In the present review we focus on the involvement of HS in basic FGF (bFGF) receptor binding and mitogenic activity and its modulation by species of heparin, HS, and synthetic polyanionic 'heparin-mimicking' compounds. The results are discussed in relation to the current thoughts on the dual involvement of low and high affinity receptor sites in the growth promoting and angiogenic activities of bFGF and other heparin-binding growth factors.
Language of Publication: English
Unique Identifier: 96440178

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MeSH Heading (Major): Fibroblast Growth Factor, Basic|*PH; Heparitin Sulfate|*PH
MeSH Heading: Animal; Cell Division|PH; Extracellular Matrix|PH; Heparin|PH; Human; Proteoglycans|PH; Support, Non-U.S. Gov't

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0891-9992
Country of Publication: UNITED STATES

Record 31 from database: MEDLINE
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Title: Oral adhesion of yeasts.
Author: Olsen I
Address: Department of Microbiology, Dental Faculty, University of Oslo, Norway.
Source: Acta Odontol Scand, 1990 Feb, 48:1, 45-53
Abstract: Oral adhesion of yeasts probably occurs by interaction between yeast cell adhesins and oral epithelial cell receptors. In Candida albicans mannoprotein, glucan, chitin, cell wall proteins, and lipids are possible adhesins. Mannoprotein appears as a fibrillar or floccular outermost layer in stationary-phase cells grown in sugar-rich medium. Preincubation of buccal epithelial cells (BECs) with concanavalin A inhibits adhesion, as does suppression of mannoprotein production by tunicamycin. Germ tubes adhere more easily to BECs and plastic than do blastospores. Methyl-alpha-D-mannoside may be analogous to the yeast adhesin or epithelial cell receptor because it inhibits adhesion of C. albicans to BECs. L-Fucose, N-acetyl-D-glucosamine, or D-mannose, having the same effect, may also function as epithelial cell receptors. Other factors affecting yeast adhesion may be fibronectin, hydrophobicity, s-IgA, and indigenous bacteria. Growth of yeasts to stationary phase in sugar-rich media promotes adhesion to acrylic, as do divalent cations and serum. Saliva, chlorhexidine, and Streptococcus salivarius inhibit adhesion of yeasts.
Language of Publication: English
Unique Identifier: 90209552

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MeSH Heading (Major): Candida albicans|*PH; Cell Adhesion|*/DE; Cell Adhesion Molecules|*IP
MeSH Heading: Cell Wall|ME; Human; Mouth Mucosa|CY

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0001-6357
Country of Publication: NORWAY
CAS Registry/EC Number: 0 (Cell Adhesion Molecules)

Record 32 from database: MEDLINE
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Title: Proposal for a pathway to mediate the metabolic effects of insulin.
Author: Brautigan DL; Kuplic JD
Address: Section of Biochemistry, Brown University, Providence, RI 02912.
Source: Int J Biochem, 1988, 20:4, 349-56
Abstract: This review seeks to assemble recent discoveries about insulin receptor/kinase, guanine nucleotide-binding proteins, phosphatidyl inositol metabolism, and protein phosphatases to provide a mechanistic pathway by which insulin would alter carbohydrate and fat metabolism. It proposes a hypothetical chain of events that leads from the insulin receptor to protein phosphatase-1. The sequence starts with insulin binding to its receptor, activating the intrinsic receptor/kinase activity. The insulin receptor phosphorylates a guanine nucleotide-binding protein, which activates a particular phospholipase C. This in turn stimulates the production of two lipid-derived messengers: inositol-phospho-glucosamine and diacylglycerol. These messengers trigger the effects of insulin. The diacylglycerol produced by insulin is thought to be analogous to the diacylglycerol produced by alpha-adrenergic stimulation, which activates protein kinase C. Activation of this kinase could account for increases in phosphorylation of certain proteins. The inositol-phospho-glucosamine is the cytosolic messenger for insulin. One of the enzymes activated by insulin is protein phosphatase type-1. It is known that the phosphatase decreases phosphorylation of certain target enzymes. In response to insulin, activation of protein phosphatase type-1 occurs with a stable conformational change that may involve rearrangement of disulfide bonds. Rearrangement is either directly in response to the cytosolic messenger or is catalyzed by an isomerase activated by the insulin messenger. Ultimately, protein phosphatase type-1 and/or the disulfide isomerase may together mediate the pleiotropic effects of insulin on carbohydrate and fat metabolism.
Language of Publication: English
Unique Identifier: 88211977

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MeSH Heading (Major): Energy Metabolism|*; Insulin|*PH
MeSH Heading: Animal; Disulfides|ME; Human; Isomerism; Models, Biological; Phosphoprotein Phosphatase|ME; Protein-Tyrosine Kinase|ME; Receptors, Insulin|AN/ME; Support, U.S. Gov't, P.H.S.

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0020-711X
Country of Publication: ENGLAND
CAS Registry/EC Number: EC 2.7.1.- (Insulin Receptor Protein-Tyrosine Kinase); EC 2.7.1.112 (Protein-Tyrosine Kinase); EC 3.1.3.16 (Phosphoprotein Phosphatase); 0 (Disulfides); 0 (Receptors, Insulin); 11061-68-0 (Insulin)

Record 33 from database: MEDLINE
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Title: Diagnostic procedures in immunodermatology.
Author: Cormane RH; Asghar SS
Address
Source: J Invest Dermatol, 1976 Jul, 67:1, 129-35
Abstract: Most immunologic diseases are caused by the derailment of the humoral or cellular pathways of the immunologic defense system. This derailment results from numerous factors such as the inability of the patient to remove the pathogen; the consumption, defect, or deficiency in any component of these pathways, and the overproduction of any of the components. To diagnose these immunologic disorders one has to detect the pathogen and the reactions caused by it and to determine the cause of its nonclearance. The immunofluorescence techniques has been invaluable in detecting both the antigen that causes the disease and the reactions initiated by the antigen, such as the production of antibodies and the activation of the complement system. The immunoperoxidase technique has also been used for these purposes in certain instances. For detecting the circulating immune complexes which occur as intermediates in the chain of reactions initiated by the antigen, various physiochemical and biologic techniques have been used. However, none of these tests seems to be totally reliable for determining whether circulating immune complexes are present. The consumption of complement was detected by hemolytic estimations and radial immunodiffusion or rocket electrphoresis. These techniques were also useful in detecting the hereditary deficiencies in immunoglobulins and components of classical and alternative pathways of complement activation. Since these techniques cannot be used to estimate IgE, the radioallergosorbent test was used to measure such levels in the atopic patients. Cellular hypersensitivity was detected with skin tests together with methods which assess the ability of lymphocytes to produce mediators in response to antigen. Many of these mediator assays, however, are not suitable for this purpose. A satisfactory substitute appears to be to determine the factor in antigen-stimulated, lymphocyte culture supernatants which activates macrophages to take up radiolabeled colloidal gold or radiolabeled glucosamine. In contact allergic dermatitis, an increase in the IgD-bearing lymphocytes and granulocytes has also been correlated with cellular hypersensitivity. Lymphocytes and polymorphonuclear leukocytes coated with antibodies mainly directed against nuclear antigens of the basal layer cells of the noninvolved epidermis have invariably been encountered in psoriasis. The use of these findings for diagnostic purposes and for understanding the mechanisms of certain diseases is being explored.
Language of Publication: English
Unique Identifier: 76216087

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MeSH Heading (Major): Immunologic Diseases|*DI/GE/PA; Skin Diseases|*DI/PA
MeSH Heading: Animal; B-Lymphocytes|IM; Complement 3|COMPLEMENT A 03; Human; Immune Complex Diseases|DI; Immunity, Cellular; Immunologic Deficiency Syndromes|DI; T-Lymphocytes|IM

Publication Type: JOURNAL ARTICLE; REVIEW
ISSN: 0022-202X
Country of Publication: UNITED STATES

Record 34 from database: MEDLINE
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Title: Stimulation of fibroblast biosynthetic activity by serum of patients with pretibial myxedema.
Author: Cheung HS; Nicoloff JT; Kamiel MB; Spolter L; Nimni ME
Address
Source: J Invest Dermatol, 1978 Jul, 71:1, 12-7
Abstract: Skin fibroblasts from the shoulder and lower extremities of normal individuals, as well as from patients with pretibial myxedema (PTM) were grown in culture. When cells reached the monolayer stage, they were labeled with 3H-glucosamine and tested for hyaluronic acid synthesis in the presence of either serum from PTM patients or normal human serum. All the fibroblasts from the pretibial area synthesized 2 to 3 times more hyaluronic acid when incubated with PTM sera than when incubated in normal human serum. Fibroblasts cultured from skin of the back or prepuce did not respond to PTM sera. This heat-stable, protease-sensitive, and dialyzable, fibroblast-stimulating factor is not a 7S gamma-globulin. The enhanced sensitivity to PTM sera exhibited by fibroblasts from the lower extremities may explain why the lesions in this disease are restricted primarily to that area.
Language of Publication: English
Unique Identifier: 78243742

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MeSH Heading (Major): Fibroblasts|*ME; Hyaluronic Acid|*BI; Leg Dermatoses|*BL; Myxedema|*BL
MeSH Heading: Blood; Cells, Cultured; Chemistry; Connective Tissue|ME; Graves' Disease|BL; Human; Molecular Conformation; Skin|UL; Stimulation, Chemical; Support, U.S. Gov't, P.H.S.

Publication Type: JOURNAL ARTICLE; REVIEW
ISSN: 0022-202X
Country of Publication: UNITED STATES

Record 35 from database: MEDLINE
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Title: Basement membranes: current concepts of structure and synthesis.
Author: Kefalides NA
Address
Source: Dermatologica, 1975, 150:1, 4-15
Abstract: Basement membranes are composed of dissimilar protein subunits. The procollagen-like subunit is associated with noncollagenous matrix glycoproteins. The proportion of the latter components varies among basement membranes. The various subunits interact via hydrogen bonds, disulfide bonds and aldehyde-derived cross-links. The extensive degree of cross-linking renders basement membranes highly insoluble. A procollagen-like molecule, extracted from calf anterior lens capsule, exhibits on electron microscopy a filamentous component with a globular portion attached at one end. Treatment of basement membranes with pepsin at low temperature digests the noncollagenous glycoprotein components and allows the collagenous component to come into solution. Purification of the pepsin-solubilized collagen from basement membranes reveals a molecule composed of three identical alpha-chains. Other unique features include 40-50 residues of hydroxylysine, 128-140 residues of 4-hydroxyproline, 12-15 residues of 3-hydroxyproline, 29 residues of arginine, 35 residues alanine, 2-4 residues of half-cystine, 38 residues of glucosyl-galactosyl-hydroxylysine, 3 residues of mannose, 2 residues of glucosamine, and 0.3 residues of fucose. Immunochemical studies indicate the presence of three distinct antigenic components and support the evidence that one is collagenous and the other two are noncollagenous glycoproteins. One of the latter corresponds to the non-helical extension of procollagen. The other is a large-molecular weight highly cross-linked matrix protein.
Language of Publication: English
Unique Identifier: 75209517

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MeSH Heading (Major): Basement Membrane|*ME/UL
MeSH Heading: Amino Acids|ME; Animal; Carbohydrates|ME; Collagen|ME; Descemet's Membrane|ME; Dogs; Extracellular Space|ME; Glycoproteins|ME; Histocytochemistry; Human; Immunochemistry; Rats; Sheep; Support, U.S. Gov't, P.H.S.

Publication Type: JOURNAL ARTICLE; REVIEW
ISSN: 0011-9075
Country of Publication: SWITZERLAND

Record 36 from database: MEDLINE
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Title: Biochemistry and lectin binding properties of mammalian salivary mucous glycoproteins.
Author: Herp A; Borelli C; Wu AM
Address: Dept. of Biochemistry, New York Medical College, Valhalla 10595.
Source: Adv Exp Med Biol, 1988, 228:, 395-435
Abstract: The molecules responsible for the highly viscous properties of mucus are secretory glycoproteins referred to as mucins. Salivary mucins are characterized by a high sugar to protein ratio and are of a broad range of molecular weight from 7 x 10(4) to millions. With a few exceptions, they contain up to 30% of hexosamine (galactosamine and glucosamine), 8-33% of sialic acid, trace to 15% of galactose or fucose and little or no mannose. The size of carbohydrate side chains of these glycoproteins ranges from one to about fifteen units of sugar. These carbohydrate side chains are usually O-glycosidically linked through N-acetylgalactosamine to a peptidyl serine or threonine. In some instances, ester sulfate groups, mainly on N-acetylglucosamine, are also a structural feature. In many of these glycoproteins, the saccharide sequence is the same as that which determines the specificity of blood groups. Carbohydrate sequence analysis shows that salivary mucins exhibit considerable polydispersity, great diversity and remarkable structural flexibility not only among animal species but also within the same mucin molecule. Based on their lectin-binding ability, they can be used for purification of lectins, and lectins coupled to resin may be useful for the isolation of mucin-type glycoproteins. The epithelial mucous secretions modulate oral microbial flora; many secretory components serve as lectin-receptors for the attachment of microbes. The judicious use of lectins with widely differing binding characteristics has already been valuable in the in situ localization of salivary glycoproteins, in elucidating structural details, recording sugar density within a given tissue section, and defining host-parasite interactions. It is hoped that their use, together with monoclonal antibody (158) and tissue culture techniques (159, 160) will further clarify the roles of individual secretory mucous glycoproteins in health and disease.
Language of Publication: English
Unique Identifier: 89022412

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MeSH Heading (Major): Lectins|*ME; Salivary Proteins|IM/*ME
MeSH Heading: Animal; Carbohydrate Conformation; Carbohydrate Sequence; Human; Molecular Sequence Data; Mucins|IM/ME; Support, Non-U.S. Gov't; Support, U.S. Gov't, Non-P.H.S.

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
ISSN: 0065-2598
Country of Publication: UNITED STATES
CAS Registry/EC Number: 0 (Lectins); 0 (Mucins); 0 (Salivary Proteins)

Record 37 from database: MEDLINE
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Title: Interactions between cells of the immune system and hyaluronate synthesis by human dermal fibroblasts.
Author: Whiteside TL; Buckingham RB
Address: Department of Pathology, University of Pittsburgh School of Medicine, Pennsylvania.
Source: Ciba Found Symp, 1989, 143:, 170-81; discussion 182-6, 281-5
Abstract: Mitogen- or alloantigen-activated human peripheral blood mononuclear cells (MNC) produce a soluble factor which selectively stimulates up to twenty-fold the synthesis of glycosaminoglycan (GAG) by cultured normal human fibroblasts. Confluent fibroblast monolayers were incubated with active MNC supernatants and newly synthesized GAG was measured by the incorporation of [3H]glucosamine into cetylpyridinium chloride-precipitable material. The GAG-stimulatory factor (GAG-SF) was a product of T lymphocytes. Alloreactive T cell clones obtained from the peripheral blood produced the factor after reactivation with the irradiated stimulators, and its production was dependent on HLA-DR-mediated recognition. The CD3+CD4+ clones derived from the skin-infiltrating lymphocytes in patients with early scleroderma also produced the GAG-SF upon in vitro activation with a mitogen. The GAG-SF was purified to apparent homogeneity from supernatants of concanavalin A-activated MNC by Sephadex gel filtration, ion-exchange chromatography and reverse-phase HPLC. The GAG-SF is a 67,000 Da glycoprotein with pI of 5.6. It is not mitogenic to fibroblasts and does not modulate collagen synthesis. Its purification and characterization are important, because of a possible involvement of activated lymphocytes and their products in the immunopathogenesis of human diseases characterized by fibrosis, stromal reactions and local lymphocytic infiltrates.
Language of Publication: English
Unique Identifier: 90032063

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MeSH Heading (Major): Cell Communication|*; Epidermis|IM/*PH; Fibroblasts|*PH; Hyaluronic Acid|*BI; Lymphocytes|ME/*PH
MeSH Heading: Human; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

Publication Type: JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
ISSN: 0300-5208
Country of Publication: NETHERLANDS
CAS Registry/EC Number: 9004-61-9 (Hyaluronic Acid)

Record 38 from database: MEDLINE
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Title: Evidence for multidrug-resistant cells in human tumor cell populations.
Author: Shoemaker RH; Curt GA; Carney DN
Address
Source: Cancer Treat Rep, 1983 Oct, 67:10, 883-8
Abstract: Data are presented from two cell culture systems which support the notion that a multi-drug-resistant phenotype occurs in human tumor cell populations. Human small cell lung cancer cell lines derived from patients in relapse following intensive combination chemotherapy demonstrate broad cross-resistance to nine standard drugs in vitro. However, analysis of [14C]glucosamine-labeled glycoproteins in the small cell lung cancer cell lines failed to identify any consistent association between a specific glycoprotein marker and the drug-resistant phenotype. Evaluation of drug sensitivity of human tumor cells in primary culture (colony-forming assay) has indicated that multidrug-resistant cells may be present in tumor cell populations even in the absence of prior drug therapy. Several features of the multidrug-resistant phenotype, as observed in these human tumor cell populations, differ from those observed in Chinese hamster cell systems. In particular, the variability in patterns of resistance to various agents and in expression of glycoprotein markers suggests that a substantial amount of genetic heterogeneity underlies this phenotype in human tumors.
Language of Publication: English
Unique Identifier: 84026181

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MeSH Heading (Major): Antineoplastic Agents|*PD; Neoplasms|*DT
MeSH Heading: Carcinoma, Small Cell|DT; Cell Line; Drug Resistance; Glycoproteins|AN; Human; Lung Neoplasms|DT; Phenotype; Support, U.S. Gov't, P.H.S.

Publication Type: JOURNAL ARTICLE; REVIEW
ISSN: 0361-5960
Country of Publication: UNITED STATES
CAS Registry/EC Number: 0 (Antineoplastic Agents); 0 (Glycoproteins)

Record 39 from database: MEDLINE
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Title: Glycolipid membrane-binding domain of human erythrocyte acetylcholinesterase.
Author: Rosenberry TL; Roberts WL; Haas R
Address
Source: Fed Proc, 1986 Dec, 45:13, 2970-5
Abstract: The membrane-binding domain of human erythrocyte acetylcholinesterase is a small hydrophobic structure at the COOH-terminus of the enzyme subunits. Papain digestion cleaves a COOH-terminal dipeptide linked to the hydrophobic structure with the sequence His-Gly-ethanolamine-Z, where the ethanolamine is in amide linkage to the glycine and Z is a partially characterized glycolipid. This glycolipid includes a second residue of ethanolamine and a residue of glucosamine, both of which have free primary amino groups accessible to radiomethylation. The glycolipid also contains a carbohydrate residue or residues that bind to concanavalin A and nearly stoichiometric amounts of both palmitate and C22 unsaturated fatty acids. Similarities in this membrane-binding structure to those reported for trypanosome variant surface glycoproteins and Thy-1 glycoprotein suggest an important new category of posttranslational modifications involving the attachment of COOH-terminal glycolipid.
Language of Publication: English
Unique Identifier: 87054661

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MeSH Heading (Major): Acetylcholinesterase|*BL; Erythrocytes|*EN; Glycolipids|*BL; Membrane Proteins|*BL
MeSH Heading: Amino Acid Sequence; Binding Sites; Carbohydrates|AN; Comparative Study; Fatty Acids|AN; Human; Papain; Peptide Fragments|BL; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

Publication Type: JOURNAL ARTICLE; REVIEW
ISSN: 0014-9446
Country of Publication: UNITED STATES
CAS Registry/EC Number: EC 3.1.1.7 (Acetylcholinesterase); EC 3.4.22.2 (Papain); 0 (Fatty Acids); 0 (Glycolipids); 0 (Membrane Proteins); 0 (Peptide Fragments)

Record 40 from database: MEDLINE
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Title: Invasion of erythrocytes by malaria merozoites: evidence for specific receptors involved in attachment and entry.
Author: Howard RJ; Miller LH
Address
Source: Ciba Found Symp, 1981, 80:, 202-19
Abstract: Invasion of erythrocytes by malaria merozoites involves attachment of the merozoite membrane at the point of collision with the erythrocytes, then reorientation of the merozoite such that its apex is opposed to the erythrocyte membrane, followed by invaginatin of the erythrocyte membrane and interiorization of the parasite. Specific recognition of erythrocyte surface components by the merozoite has been shown by studies on the specificity of merozoites of different malaria species for a limited range of host-species erythrocytes, for erythrocytes of particular maturity, and for erythrocytes possessing particular blood-group determinants. Different malaria species capable of invading erythrocytes of the same host also exhibit differences in specificity for components on enzyme-treated erythrocytes. The attachment phase of merozoite invasion has been isolated from subsequent steps by treatment of merozoites with cytochalasin B -- they then attach to but do not invade susceptible erythrocytes. There is now evidence for other differences between initial attachment steps and subsequent invasion steps form studies on merozoite treatments in vitro which affect invasion but not attachment. It has also been shown that addition of N-acetyl-D-glucosamine to cultures of Plasmodium falciparum inhibits merozoite invasion. Elucidation of the sequence and nature of molecular interactions of merozoite and erythrocyte membrane molecules during invasion will be based on the fundamental ultrastructural observations and on the specificity of attachment and invasion steps already described.
Language of Publication: English
Unique Identifier: 81260046

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MeSH Heading (Major): Erythrocytes|*PS; Plasmodium|PH/*PY/UL
MeSH Heading: Acetylglucosamine|PD; Adhesiveness; Animal; Antigens, Surface; Duffy Blood-Group System; Erythrocyte Membrane|PS/UL; Human; Protease Inhibitors|PD; Reticulocytes|PS; Species Specificity

Publication Type: JOURNAL ARTICLE; REVIEW
ISSN: 0300-5208
Country of Publication: NETHERLANDS
CAS Registry/EC Number: 0 (Antigens, Surface); 0 (Protease Inhibitors); 7512-17-6 (Acetylglucosamine)

Record 41 from database: MEDLINE
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Title: Receptors and recognition mechanisms of Trypanosoma cruzi.
Author: Snary D
Address
Source: Trans R Soc Trop Med Hyg, 1985, 79:5, 587-90
Abstract: The current state of knowledge on receptor and recognition interactions which take place during the life-cycle of Trypanosoma cruzi is reviewed. Evidence suggests that carbohydrate plays a central role in these recognition mechanisms. Lectin-sugar interactions appear to be involved in uptake of the parasite by host cells including macrophages and a protein on the surface of trypomastigote which binds N-acetyl glucosamine on the host cell has been implicated in host cell invasion. Sugars on a 72,000 molecular weight glycoprotein on epimastigotes have also been implicated in colonization of the gut of the insect vector and in control of the morphological changes which take place in the insect gut.
Language of Publication: English
Unique Identifier: 86152854

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MeSH Heading (Major): Trypanosoma cruzi|PH/*PY
MeSH Heading: Acetylglucosamine; Animal; Binding Sites; Cell Membrane; Chagas Disease|PS; Glycoproteins|PH; Host-Parasite Relations; Human; Lectins; Macrophage Activation; Molecular Weight; Morphogenesis; Phagocytosis; Receptors, Immunologic|PH; Receptors, Mitogen|PH; Triatominae

Publication Type: JOURNAL ARTICLE; REVIEW
ISSN: 0035-9203
Country of Publication: ENGLAND
CAS Registry/EC Number: 0 (glycoprotein receptor); 0 (Glycoproteins); 0 (Lectins); 0 (Receptors, Immunologic); 0 (Receptors, Mitogen); 7512-17-6 (Acetylglucosamine)

Record 42 from database: MEDLINE
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Title: Studies on the biochemical basis of the interaction of the merozoites of Plasmodium falciparum and the human red cell.
Author: Jungery M
Address
Source: Trans R Soc Trop Med Hyg, 1985, 79:5, 591-7
Abstract: The red cell membrane appears to possess receptors for malarial parasites which are species specific. Plasmodium falciparum invades red cells that have the surface sialoglycoproteins, glycophorins A, B and C. Several regions of these molecules are critical to parasite binding. Invasion of red cells by merozoites can be blocked by both antibodies directed to specific sites on glycophorin and tryptic fragments of these molecules. The parasites appear to bind to the red cells in a lectin-like fashion, since three monosaccharides, namely N-acetyl-glucosamine (Glu NAc), N-acetyl-galactosamine (Gal NAc) and N-acetyl-neuraminic acid (Neu NAc), can specifically block parasite invasion in vitro. Neoglycoproteins made by coupling these sugars to BSA are particularly effective. Possible mechanisms of parasite attachment to and invasion of red cells are discussed.
Language of Publication: English
Unique Identifier: 86152855

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MeSH Heading (Major): Erythrocytes|*PS; Plasmodium falciparum|*PY
MeSH Heading: Acetylgalactosamine; Acetylglucosamine; Antibodies; Binding Sites; Binding, Competitive; Glycophorin|IM/PH; Host-Parasite Relations; Human; Lectins; Membrane Proteins; Models, Biological; Sialic Acids; Support, Non-U.S. Gov't; Virulence

Publication Type: JOURNAL ARTICLE; REVIEW
ISSN: 0035-9203
Country of Publication: ENGLAND
CAS Registry/EC Number: 0 (Antibodies); 0 (Glycophorin); 0 (Lectins); 0 (Membrane Proteins); 0 (Sialic Acids); 31022-50-1 (Acetylgalactosamine); 7512-17-6 (Acetylglucosamine)
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Special Pages On The Various of 12 Web Sites Authored by Karl Loren
OC History	Oral Chelation		Testimonials
Family Of Three Oral Chelation Formulas	Life Glow Basic		Life Glow Basic Ingredient List
Life Glow Plus	Life Glow Plus Ingredient List		American Heart Association -- Lies
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Calcium	How Bones Grow		Colloidal Minerals
Jean Ross	Philosophy		The Wednesday Letter
Arthritis & James Coburn's Use Of MSM	Karl Loren Viewpoints		News And Announcements
Dr. Flanagan's Microhydrin	500 Page Book On Heart Disease		Colostrum & Transfer Factor
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Instead Of	Chelation Therapy		Super Colostrum (2)
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Dear Karl,

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You can reach Vibrant Life in many ways, including by mail to Vibrant Life, 2808 N. Naomi St., Burbank, CA 91504. Within the US and Canada, use the toll free number: (800) 523-4521, the local number: (818) 558-1799, the FAX: (818) 558-7299, eMail to kimberly@oralchelation.com or any one of the hundreds of message forms throughout the 50 web sites. Vibrant Life normally ships the same day we get an order. There are message forms on each of the 100,000+ pages on this and other sites where you can communicate with Vibrant Life. Check out our companion site, at: http://www.oralchelation.net where Karl's 2000 page book is published. Karl Loren is the author and webmaster for this BOOK, as well as for another web site about ORAL CHELATION. His personal philosophical articles are at PHILOSOPHY.

Copyright © May 20, 2008 6:24 AM by Karl Loren on behalf of Vibrant Life, ALL RIGHTS RESERVED. Permission is granted for non-commercial downloading, copying, distribution or redistribution on two conditions: One, that some form of copyright notice is included in every copy distributed or copied, showing the copyright belonging to Vibrant Life, Burbank, CA, at www.oralchelation.com . The second condition is that the material is not to be used for any purpose contrary to the purposes and objectives of this site. This permission does not extend to materials on this site which are copyrighted by others.