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Am J Physiol Endocrinol Metab 296: E1195-E1209, 2009. First published March 31, 2009; doi:10.1152/ajpendo.90958.2008
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Biochemistry, physiology, and genetics of GPAT, AGPAT, and lipin enzymes in triglyceride synthesis

Kazuharu Takeuchi and Karen Reue

Department of Human Genetics, David Geffen School of Medicine, University of California Los Angeles, Los Angeles, California

Submitted 29 November 2008 ; accepted in final form 30 March 2009

ABSTRACT

Triacylglycerol (TAG) synthesis and storage in tissues such as adipose tissue and liver have important roles in metabolic homeostasis. The molecular identification of genes encoding enzymes that catalyze steps in TAG biosynthesis from glycerol 3-phosphate has revealed an unexpected number of protein isoforms of the glycerol phosphate acyltransferase (GPAT), acylglycerolphosphate acyltransferase (AGPAT), and lipin (phosphatidate phosphatase) families that appear to catalyze similar biochemical reactions. However, on the basis of available data for a few members in which genetic deficiencies in mouse and/or human have been studied, we postulate that each GPAT, AGPAT, and lipin family member likely has a specialized role that may be uncovered through careful biochemical and physiological analyses.

glycerol-3-phosphate acyltransferase; 1-acylglycerol-3-phosphate acyltransferase; phosphatidate phosphatase


Address for reprint requests and other correspondence: K. Reue, Dept. of Human Genetics, Gonda 6506A, David Geffen School of Medicine at UCLA, 695 Charles E. Young Drive South, Los Angeles, CA 90095 (e-mail: reuek{at}ucla.edu)




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