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Acyl chain dependent product inhibition by phosphatidylserine synthases
Author(s) -
Kimura Atsuko Kakio,
Kim Hee-Yong
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.790.14
Subject(s) - phosphatidylethanolamine , phosphatidylserine , chemistry , phosphatidylcholine , phospholipid , biochemistry , serine , membrane , intracellular , oleic acid , enzyme , microbiology and biotechnology , biology
Phosphatidylserine (PS), the major anionic phospholipid in eukaryotic cell membranes, is synthesized by PS synthase 1 (PSS1) and PSS2 through the serine‐base exchange reaction from phosphatidylcholine (PC) and phosphatidylethanolamine (PE), respectively. Membrane PS is critically involved in key cell signaling processes such as Akt, PKC and Raf‐1 activation. The membrane PS profile is well maintained although mechanisms for the regulation of the PS profile are not clearly understood. In this study, we investigated the effect of PS acyl chain on the feedback mechanism in which activities of PSSs are inhibited by product PS. We found that PSS1 and PSS2 have significantly different inhibitory response to two PS molecular species, oleic acid (OA, 18:1n‐9) containing (OA‐PS) and docosahexaenoic acid (DHA, 22:6n‐3) containing PS species (DHA‐PS). PSS1 was inhibited more strongly by OA‐PS, while PSS2 was more by DHA‐PS. Together with the differential expression between PSS1 and PSS2 in variety of cells and tissues, these results indicate that the level of individual PS molecular species is regulated through feedback mechanism by which synthetic activity of each enzyme is inhibited differently. Intramural Program of National Institutes of Health