Journal
AMERICAN JOURNAL OF PHYSIOLOGY-ENDOCRINOLOGY AND METABOLISM
Volume 296, Issue 6, Pages E1195-E1209Publisher
AMER PHYSIOLOGICAL SOC
DOI: 10.1152/ajpendo.90958.2008
Keywords
glycerol-3-phosphate acyltransferase; 1-acylglycerol-3-phosphate acyltransferase; phosphatidate phosphatase
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Funding
- National Heart, Lung, and Blood Institute [HL-28481, HL-90553]
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [P01HL028481, P01HL090553] Funding Source: NIH RePORTER
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Takeuchi K, Reue K. Biochemistry, physiology, and genetics of GPAT, AGPAT, and lipin enzymes in triglyceride synthesis. Am J Physiol Endocrinol Metab 296: E1195-E1209, 2009. First published March 31, 2009; doi:10.1152/ajpendo.90958.2008.-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), acylglycerol-phosphate 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.
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