Results 211 to 220 of about 343,412 (268)
Exogenous pyruvate is therapeutic against colitis by targeting cytosolic phospholipase A2. [PDF]
Genes DisHasan S +4 more
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Analysis of the clinical value of combined monitoring of methylation transferase Wilms' tumour 1-associating protein and lipoprotein-associated phospholipase A2 in patients with coronary artery disease. [PDF]
Front Cardiovasc MedGuo F, Hu B, Li G.
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Phospholipase A2-A Significant Bio-Active Molecule in Honeybee (<i>Apis mellifera</i> L.) Venom. [PDF]
MoleculesMuntean M, Florea A.
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The level and clinical significance of serum soluble M-type phospholipase A2 receptor in patients with primary membranous nephropathy. [PDF]
Ren FailWang ZH, Gao YM, Deng ZL, Wang Y.
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Phospholipase A2 group IVD mediates the transacylation of glycerophospholipids and acylglycerols. [PDF]
J Lipid ResBreithofer J +14 more
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Journal of Lipid Mediators and Cell Signalling, 1995
To summarize the regulation of cPLA2, we have proposed a model for the activation of cPLA2 based both on our previous studies (Clark et al., 1991; Lin et al., 1993) and the work of many others (Fig. 5). In this model, cPLA2 is tightly regulated by multiple pathways, including those that control Ca2+ concentration, phosphorylation states and cPLA2 ...
James D Clark, Eric A Nalefski, L L Lin
exaly +3 more sources
To summarize the regulation of cPLA2, we have proposed a model for the activation of cPLA2 based both on our previous studies (Clark et al., 1991; Lin et al., 1993) and the work of many others (Fig. 5). In this model, cPLA2 is tightly regulated by multiple pathways, including those that control Ca2+ concentration, phosphorylation states and cPLA2 ...
James D Clark, Eric A Nalefski, L L Lin
exaly +3 more sources
Journal of Biochemistry, 2002
Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins (PGs) and leukotrienes (LTs). The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
I, Kudo, M, Murakami
openaire +3 more sources
Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins (PGs) and leukotrienes (LTs). The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
I, Kudo, M, Murakami
openaire +3 more sources
Seminars in Cell & Developmental Biology, 1997
Mammalian cells contain multiple structurally different phospholipase A2 enzymes that hydrolyse sn-2 fatty acid from membrane phospholipid. The low molecular weight secreted forms act extracellularly both as lipolytic enzymes and as agonists that bind to specific cell surface receptors.
, Gijón, , Leslie
openaire +2 more sources
Mammalian cells contain multiple structurally different phospholipase A2 enzymes that hydrolyse sn-2 fatty acid from membrane phospholipid. The low molecular weight secreted forms act extracellularly both as lipolytic enzymes and as agonists that bind to specific cell surface receptors.
, Gijón, , Leslie
openaire +2 more sources
Prostaglandins & Other Lipid Mediators, 2002
Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
Ichiro, Kudo, Makoto, Murakami
openaire +2 more sources
Phospholipase A2 (PLA2) catalyzes the hydrolysis of the sn-2 position of membrane glycerophospholipids to liberate arachidonic acid (AA), a precursor of eicosanoids including prostaglandins and leukotrienes. The same reaction also produces lysophosholipids, which represent another class of lipid mediators.
Ichiro, Kudo, Makoto, Murakami
openaire +2 more sources
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2004
Phospholipase A2 (PLA2) is an enzyme present in snake and other venoms and body fluids. We measured PLA2 catalytic activity in tissue homogenates of 22 species representing the classes Anthozoa, Hydrozoa, Scyphozoa and Cubozoa of the phylum Cnidaria. High PLA2 levels were found in the hydrozoan fire coral Millepora sp.
Nevalainen, Timo J. +6 more
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Phospholipase A2 (PLA2) is an enzyme present in snake and other venoms and body fluids. We measured PLA2 catalytic activity in tissue homogenates of 22 species representing the classes Anthozoa, Hydrozoa, Scyphozoa and Cubozoa of the phylum Cnidaria. High PLA2 levels were found in the hydrozoan fire coral Millepora sp.
Nevalainen, Timo J. +6 more
openaire +3 more sources