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Am J Physiol Endocrinol Metab (March 31, 2009). doi:10.1152/ajpendo.90958.2008
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Submitted on November 29, 2008
Revised on March 30, 2009
Accepted on March 30, 2009

Biochemistry, Physiology, and Genetics of GPAT, AGPAT, and Lipin Enzymes in Triglyceride Synthesis

Kazuharu Takeuchi1 and Karen Reue1*

1 UCLA

* To whom correspondence should be addressed. E-mail: reuek{at}ucla.edu.

Triacylglycerol (TAG) synthesis and storage in tissues such as adipose tissue and liver have an important role 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, based on 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.




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