Results 161 to 170 of about 9,957 (215)
Phospholipase PLA2G5-triggered hemolysis emerges as a contributor to sepsis lethality. [PDF]
J Clin InvestCavaillon JM.
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Cnidarian toxins: omics approaches and recombinant proteins. [PDF]
J Venom Anim Toxins Incl Trop DisVega-Tamayo JE +6 more
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Snake Venom PLA<sub>2</sub> as Anticoagulant Agents: Role of Crotoxin, from <i>Crotalus durissus</i> Rattlesnake, in Hemostasis. [PDF]
Toxins (Basel)Brasileiro-Martins LM +11 more
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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
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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
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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
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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
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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
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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
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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 ...
J D, Clark +3 more
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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 ...
J D, Clark +3 more
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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
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Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2004
Phospholipase A2 (PLA2) catalytic activity was measured in aqueous extracts of 83 freeze-dried specimens representing 55 marine sponge species collected from the east coast of Australia including the Great Barrier Reef. High levels (>500 u/l) of PLA2 activity (defined as the amount of activity that releases 1 micromol of fatty acid per min) were found ...
Nevalainen, TJ, Quinn, RJ, Hooper, JNA
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Phospholipase A2 (PLA2) catalytic activity was measured in aqueous extracts of 83 freeze-dried specimens representing 55 marine sponge species collected from the east coast of Australia including the Great Barrier Reef. High levels (>500 u/l) of PLA2 activity (defined as the amount of activity that releases 1 micromol of fatty acid per min) were found ...
Nevalainen, TJ, Quinn, RJ, Hooper, JNA
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Current Opinion in Lipidology, 2009
As the role of lipids and inflammation in the genesis and progression of the atherosclerosis disease is unquestionable, novel treatment modalities that target both aspects are currently under investigation.For a long time atherosclerosis was regarded as a lipid-driven disease, but now it is evident that it also involves the simultaneous and combined ...
Garcia Garcia, Hector +1 more
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As the role of lipids and inflammation in the genesis and progression of the atherosclerosis disease is unquestionable, novel treatment modalities that target both aspects are currently under investigation.For a long time atherosclerosis was regarded as a lipid-driven disease, but now it is evident that it also involves the simultaneous and combined ...
Garcia Garcia, Hector +1 more
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