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Enhancement and inhibition of snake venom phosphodiesterase activity by lysophospholipids
Author(s) -
Mamillapalli Ramanaiah,
Haimovitz Rachel,
Ohad Mazor,
Shinitzky Meir
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01142-9
Subject(s) - lysophosphatidic acid , autotaxin , phosphodiesterase , venom , chemistry , snake venom , biochemistry , enzyme , microbiology and biotechnology , biology , receptor
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.