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Phosphatidylinositol hydrolysis by human plasma phospholipase D
Author(s) -
Balsinde Jesus,
Mollinedo Faustino
Publication year - 1990
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 - 10.1016/0014-5793(90)80017-d
Subject(s) - phosphatidylinositol , phosphatidate , phosphatidylethanol , phospholipase d , phospholipase c , egta , chemistry , phospholipase , phosphatidylinositol 4,5 bisphosphate , inositol , biochemistry , hydrolysis , enzyme , phosphatidic acid , phospholipase a2 , substrate (aquarium) , cytosol , phospholipid , diacylglycerol kinase , biology , signal transduction , calcium , protein kinase c , membrane , receptor , organic chemistry , ecology
A phospholipase D activity able to hydrolyze phosphatidylinositol has previously been described in the cytosol of human neutrophils. The experiments reported here demonstrate that this phosphatidylinositol‐hydrolyzing phospholipase D activity is also present in human plasma. This activity was assessed by free inositol release from phosphatidylinositol substrate, by phosphatidate formation and by phosphatidylethanol formation through its capacity of catalyzing a transphosphatidylation reaction. This plasma enzyme activity shows an optimum pH of 8.0 and is inhibited by EGTA.