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The role of palmitoyl–protein thioesterase in the palmitoylation of endothelial nitric oxide synthase
Author(s) -
Michel Jeffrey B.,
Michel Thomas
Publication year - 1997
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(97)00222-6
Subject(s) - palmitoylation , enos , caveolae , agonist , biology , microbiology and biotechnology , nitric oxide synthase , thioesterase , messenger rna , endothelial nos , nitric oxide , caveolin , chemistry , biochemistry , receptor , endocrinology , signal transduction , enzyme , biosynthesis , gene , cysteine
Palmitoylation of eNOS is required for targeting to plasmalemmal caveolae and agonist‐promoted depalmitoylation leads to eNOS translocation, modifying the agonist response. To date, one palmitoyl–protein thioesterase (PPT) has been purified and cloned. To explore the role of PPT in eNOS palmitoylation, we first established that PPT mRNA and protein are expressed in endothelial cells. Coexpression of PPT and eNOS in heterologous systems (COS and Sf‐9 cells) resulted in a marked reduction in [ 3 H]palmitate labeling of eNOS. We found, however, that co‐expression did not alter subcellular targeting of eNOS, but that [ 3 H]palmitate incorporation into cellular lipids, in particular palmitoyl‐CoA, was significantly reduced. These results suggest that while PPT expression can significantly alter cellular lipid metabolism, it has no effect on eNOS palmitoylation.