Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.4 (trypsin)
42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An extracellular toxic substance was separated from the cell-free culture filtrate of Vibrio anguillarum (strain NCMB571). Two fractions (GI and GII + III) obtained by Sephadex G-200 chromatography following DEAE-cellulose chromatography were lethal to rainbow trout and mice. Material separated from the GI fraction by Sepharose 4B affinity chromatography (GI-A fraction) was lethal to these animals. By sodium dodecylsulfate polyacrylamide gel electrophoresis, the GI and GI-A fractions were found to be composed of components with molecular weights of 44K and 34K, and 44K, respectively. The 44K protein band was associated with carbohydrate. Peripheral vascular disorder was observed in fish and mice that died after inoculation with GI or GI-A fraction. The toxic substance was sensitive to potassium periodate but was resistant to trypsin and acetone. Heat inactivation of the toxic substance was almost complete at 100 C for 20 min and complete at 121 C for 20 min. The toxic activity was not associated with hemolytic or proteolytic activity. Homologous antitoxin completely neutralized the toxic activity.
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PMID:Characterization of extracellular substance of Vibrio anguillarum toxic for rainbow trout and mice. 407 43

Although there is relatively little evidence of inflammation in osteoarthritis (OA), increases in mast cell numbers and mast cell activation are prominent features of the synovial tissue. As little is known of the types of mast cells which may be involved, the numbers and distribution of mast cell subpopulations have been investigated as defined according to their content of proteases. Tissue was obtained from patients with OA undergoing total knee replacement surgery (n = 14) and from control subjects either post-mortem (n = 11) or following leg amputation for peripheral vascular disease (n = 3); a double-labelling immunocytochemical procedure with monoclonal antibodies specific for tryptase and chymase was applied to identify those mast cells which contain both tryptase and chymase (MCTC) and those with tryptase but not chymase (MCT). There was considerable variation between individual tissues and between sites of tissue sampling, but cells of the MCTC subset were predominant in the synovial layer of both groups of subjects without joint disease, accounting for some 60 per cent of all mast cells present. In tissue from OA patients, however, there appeared to have been a striking shift in the relative proportions of mast cells from the MCTC to the MCT phenotype, with many more MCT cells present in the synovial tissues of OA patients (median 53 MCT/mm2) than in tissue from post-mortem (7.5 MCT/mm2, P < 0.0001) or amputation controls (12 MCT/mm2). In contrast, numbers of synovial MCTC cells in the synovium of OA patients (20 MCTC/mm2) differed little from those in either of the control groups (both 12 MCTC/mm2). In several other conditions, the MCT cells have been linked with inflammatory events, but it seems that in OA, other factors may be operating to induce a selective expansion of this subpopulation.
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PMID:Mast cell subpopulations in the synovial tissue of patients with osteoarthritis: selective increase in numbers of tryptase-positive, chymase-negative mast cells. 987 42

Gamma-glutamyltransferase (GGT) activity in human platelet sonicates was 13.6 u/g of protein (range: 7.9-25.0) in 13 healthy, non-smoking, female volunteers; corresponding values in 16 males were: 20.3 (10.1-26.0). These values Mered significantly (p = 0.034). Platelet and serum GGT activity correlated significantly (p > 0.04). Platelets seem to contain only the isoenzyme GGT 4. Part of this enzyme activity is in the form of aggregates or linked with membranes/proteins. This activity is released by Triton X-100 and trypsin and migrates as GGT 4. Serum GGT activity, a measurement in routine use, could be influenced by GGT released by platelets. It is therefore of interest that serum GGT activity can be increased in clinical conditions (e.g. myocardial infarction, diabetes, peripheral vascular disease) associated with platelet hyperactivity. Platelet GGT may influence intracellular S-nitrosoglutathione (a putative nitric oxide donor) levels. Potential associations between serum GGT activity and platelet function indices deserve investigation.
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PMID:Gamma-glutamyl Transferase Activity in Human Platelets: Quantification of Activity, Isoenzyme Characterization and Potential Clinical Relevance. 2104 29