Enhancement and inhibition of snake venom phosphodiesterase activity by lysophospholipids.
Lysophospholipids are liberated during venomous action. In this study we demonstrated that lysophosphatidyl choline (LPC) of various acyl chains enhances considerably the activity of snake venom phosphodiesterase (PDE). Lysophosphatidic acid (LPA) and its cyclic form (cLPA), on the other hand, were found to inhibit this enzyme in a non-competitive (LPA) or competitive (cLPA) manner. Both of these activities may contribute to the progression and subsidence of the poisoning profile. PDE from cellular origin was not substantially affected by any of the above lysophospholipids.
Department of Biological Chemistry, Weizmann Institute of Science, Rehovot, Israel.
R
R
Mamillapalli
R
R
Haimovitz
M
M
Ohad
M
M
Shinitzky
D015056:1-Methyl-3-isobutylxanthine / Q000494:pharmacology; D016475:3T3 Cells; D000818:Animals; D000242:Cyclic AMP / Q000378:metabolism; D004789:Enzyme Activation; D007700:Kinetics; D008246:Lysophospholipids / Q000494:pharmacology*; D051379:Mice; D043264:Phosphodiesterase I; D010726:Phosphodiesterase Inhibitors / Q000494:pharmacology*; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism* / Q000494:pharmacology; D013329:Structure-Activity Relationship
D008246:Lysophospholipids; D010726:Phosphodiesterase Inhibitors; D000242:Cyclic AMP; D010727:Phosphoric Diester Hydrolases; D043264:Phosphodiesterase I; C470790:phosphodiesterase I, snake venom; D015056:1-Methyl-3-isobutylxanthine