نتایج جستجو برای: group ii phospholipases a2
تعداد نتایج: 1517520 فیلتر نتایج به سال:
Platelet-activating factor (PAF), a phospholipid autacoid with potent effects throughout the innate immune system, is selectively degraded by two small families of PAF acetylhydrolases (PAF-AHs). These Ca2+-independent phospholipases A2 display remarkable specificity for the length of the sn-2 residue, but this selectivity is lost as the residue gains oxygen functions. Two of the PAF-AHs theref...
5-Hydroxy-3-vinyl-2(5H)-furanone, a potent and selective inhibitor of human synovial phospholipase A2 was isolated from fermentations of a Calyptella species. Its structure as identified by spectroscopic methods is identical to PA 147, an antibiotic previously isolated from a streptomycete. 5-hydroxy-3-vinyl-2(5H)-furanone inhibits the aggregation of human and bovine platelets stimulated by dif...
Background: Group IIA secreted phospholipase A2 (hGIIA) is a bifunctional protein that regulates arachidonic acid metabolism by both catalysis-dependent and catalysis–independent mechanisms. Results: Selective inhibition of the catalysisindependent signaling function perturbs a hGIIA-vimentin interaction in rheumatoid synoviocytes. Conclusion: The signaling and catalytic functions of hGIIA are ...
Phospholipase A2 (EC 3.1.1.4) is a key enzyme in inflammation and is thought to play an important part in inflammatory diseases of the gastrointestinal tract. To investigate the nature and regulation of phospholipase A2 activity in the gastrointestinal mucosa, the distribution of messenger ribonucleic acid (mRNA) for group II phospholipase A2 in various parts of the rat gastrointestinal tract w...
Cinatrins A, B and C3 inhibited phospholipase A2 purified from rat platelets in a dose-dependent manner. Cinatrin C3, the most potent component (IC50 70 microM), was noncompetitive with a Ki value of 36 microM. Cinatrins B and C3 also inhibited both porcine pancreas and Naja naja venom phospholipase A2. Inhibition of rat platelet phospholipase A2 by cinatrin C3 was independent of Ca2+ and subst...
We have found that chitosan, a polysaccharide present in fungal cell walls, is able to activate macrophages for enhanced mobilization of arachidonic acid in a dose- and time-dependent manner. Studies aimed at identifying the intracellular effector(s) implicated in chitosan-induced arachidonate release revealed the involvement of the cytosolic Group IV phospholipase A2 (PLA2), as judged by the i...
Journal of Lipid Research Volume 51, 201
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