Phospholipase A2 modulation of cyclic GMP metabolism: characteristics of guanylate cyclase activation.
Characteristics of phospholipase A2 (PLA2) modulation of guanylate cyclase were evaluated. Addition of phospholipase A2 from Vipera russelli venom led to a significant increase in the activity of guanylate cyclase in various rat organs. The activation of the enzyme was selective and was only observed in the particulate fractions of tissue homogenate. The soluble guanylate cyclase from all the tissue tested exhibited lack of stimulation. The treatment of membranes with PLA2 resulted in solubilization of cyclase activity. The increase in enzyme by PLA2 was not altered by antioxidants or reducing agents. Addition of calcium ions led to further enhancement in PLA2-dependent increases in cyclic GMP formation. Peak calcium responses were observed in micromolar concentration ranges. These observations suggest a potential role for PLA2 and calcium ions in the hormonal regulation of cyclic GMP metabolism.
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D000818:Animals; D001921:Brain / Q000187:drug effects / Q000201:enzymology; D002118:Calcium / Q000502:physiology; D002462:Cell Membrane / Q000187:drug effects; D004789:Enzyme Activation / Q000187:drug effects; D006162:Guanylate Cyclase / Q000378:metabolism*; D066298:In Vitro Techniques; D008099:Liver / Q000187:drug effects / Q000201:enzymology; D008297:Male; D010084:Oxidation-Reduction; D010740:Phospholipases / Q000494:pharmacology*; D010741:Phospholipases A / Q000494:pharmacology*; D054467:Phospholipases A2; D051381:Rats; D011919:Rats, Inbred Strains; D012995:Solubility
D010740:Phospholipases; D010741:Phospholipases A; D054467:Phospholipases A2; D006162:Guanylate Cyclase; D002118:Calcium