Molecular cloning of pancreatic group I phospholipase A2 receptor.
نویسندگان
چکیده
منابع مشابه
Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2.
Two new cloned human cDNAs encode paralogs of the 85-kDa cytosolic phospholipase A2 (cPLA2). We propose to call these cPLA2beta (114 kDa) and cPLA2gamma (61 kDa), giving the name cPLA2alpha to the well known 85-kDa enzyme. cPLA2beta mRNA is expressed more highly in cerebellum and pancreas and cPLA2gamma more highly in cardiac and skeletal muscle. Sequence-tagged site mapping places cPLA2beta on...
متن کاملMolecular cloning and expression of human Ca(2+)-sensitive cytosolic phospholipase A2.
Phospholipases A2 (PLA2s) play a key role in inflammatory processes through production of precursors of eicosanoids and platelet-activating factor. Recently, we described the purification of a novel approximately 100-kDa cytosolic PLA2 (cPLA2) from human monoblast U937 cells that is activated by physiological (intracellular) concentrations of Ca2+ (Kramer, R. M., Roberts, E. F., Manetta, J., an...
متن کاملGroup V phospholipase A2 induces leukotriene biosynthesis in human neutrophils through the activation of group IVA phospholipase A2.
We reported previously that exogenously added human group V phospholipase A(2) (hVPLA(2)) could elicit leukotriene B(4) (LTB(4)) biosynthesis in human neutrophils (Han, S. K., Kim, K. P., Koduri, R., Bittova, L., Munoz, N. M., Leff, A. R., Wilton, D. C., Gelb, M. H., and Cho, W. (1999) J. Biol. Chem. 274, 11881-11888). To determine the mechanism of the hVPLA(2)-induced LTB(4) biosynthesis in ne...
متن کاملStructure and properties of a human non-pancreatic phospholipase A2.
We have purified a human non-pancreatic phospholipase A2 that is present in platelets and is enriched in rheumatoid synovial fluid. The enzyme is calcium-dependent, has a pH optimum of 8-10, and shows a striking preference for substrate presented in the form of Escherichia coli membranes. In the E. coli phospholipase A2 assay the phospholipase exhibits an apparent specific activity of 300 mumol...
متن کاملPurification and characterization of human pancreatic phospholipase A2.
We purified human pancreatic phospholipase A2 from postmortem pancreatic tissue by elution of the semi-purified enzyme on CM-Sephadex C-25 with a linear NaCl gradient at pH 6.0. The enzyme appeared as a single polypeptide chain with an isoelectric point of 9.2 +/- 0.1. The relative molecular mass of the enzyme was estimated to be 15 800 +/- 1000 by sodium dodecyl sulfate/polyacrylamide gel elec...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1994
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)37546-4