Characterization of a novel CI-976-sensitive lysophospholipid acyltransferase that is associated with the Golgi complex.
Biochem Biophys Res Commun
; 313(3): 681-6, 2004 Jan 16.
Article
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| MEDLINE
| ID: mdl-14697244
ABSTRACT
Recent studies have identified a novel lysophospholipid acyltransferase (LPAT) that is associated with the Golgi complex and that is sensitive to the previously characterized acyl-CoA cholesterol acyltransferase inhibitor, 2,2-methyl-N-(2,4,6-trimethoxyphenyl)dodecanamide (CI-976). Here we show that besides acting on exogenous lysophospholipid (LPL) substrates, the CI-976-sensitive LPAT is also capable of reacylating endogenous Golgi LPL substrates, preferentially lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE). Moreover, using exogenous substrates, we find that the CI-976-sensitive LPAT is capable of using a variety of fatty acyl-CoA donors ranging in chain length from 10 to 20 carbons. Additional characterization demonstrates that the CI-976-sensitive LPAT is ubiquitously expressed in rat tissues, is tightly associated with Golgi membranes, and has a pH optimum between pH 7.0 and 8.0. These studies further define a unique LPC/LPE-specific LPAT from Golgi membranes that likely has a novel function in membrane trafficking.
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Base de datos:
MEDLINE
Asunto principal:
Inhibidores Enzimáticos
/
Anilidas
/
1-Acilglicerofosfocolina O-Aciltransferasa
Tipo de estudio:
Diagnostic_studies
/
Risk_factors_studies
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
2004
Tipo del documento:
Article