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Abstract
BackgroundDe novo glycerolipid synthesis begins with the acylation of glycerol-3 phosphate catalyzed by glycerol-3-phosphate acyltransferase (GPAT). In mammals, at least four GPAT isoforms have been described, differing in their cell and tissue locations and sensitivity to sulfhydryl reagents. In this work we show that mitochondrial GPAT2 overexpression in CHO-K1 cells increased TAG content and both GPAT and AGPAT activities 2-fold with arachidonoyl-CoA as a substrate, indicating specificity for this fatty acid.Methods and ResultsIncubation of GPAT2-transfected CHO-K1 cells with [1-14C]arachidonate for 3 h increased incorporation of [14C]arachidonate into TAG by 40%. Consistently, arachidonic acid was present in the TAG fraction of cells that overexpressed GPAT2, but not in control cells, corroborating GPAT2's role in synthesizing TAG that is rich in arachidonic acid. In rat and mouse testis, Gpat2 mRNA was expressed only in primary spermatocytes; the protein was also detected in late stages of spermatogenesis. During rat sexual maturation, both the testicular TAG content and the arachidonic acid content in the TAG fraction peaked at 30 d, matching the highest expression of Gpat2 mRNA and protein.ConclusionsThese results strongly suggest that GPAT2 expression is linked to arachidonoyl-CoA incorporation into TAG in spermatogenic germ cells.
Highlights
The de novo synthesis of glycerolipids begins with the acylation of glycerol-3-phosphate which is catalyzed by glycerol-3-phosphate acyltransferase (GPAT, EC 2.3.1.15)
These results strongly suggest that GPAT2 expression is linked to arachidonoyl-CoA incorporation into TAG in spermatogenic germ cells
We focus on the function of GPAT2, a mitochondrial isoform that was first identified in liver mitochondria from Gpat12/2 mice
Summary
The de novo synthesis of glycerolipids begins with the acylation of glycerol-3-phosphate which is catalyzed by glycerol-3-phosphate acyltransferase (GPAT, EC 2.3.1.15). Four different genes encode GPAT isoforms 1–4, which differ in tissue expression pattern, subcellular location, fatty acyl-CoA substrate preference, and sensitivity to N-ethylmaleimide (NEM) [1]. PA is the precursor for the synthesis of both triacylglycerol (TAG) and glycerophospholipids Both the specific activity and regulation of the different GPAT isoforms differ, depending on the tissue and the metabolic state of the animal [2,3]. We focus on the function of GPAT2, a mitochondrial isoform that was first identified in liver mitochondria from Gpat12/2 mice. In this work we show that mitochondrial GPAT2 overexpression in CHO-K1 cells increased TAG content and both GPAT and AGPAT activities 2-fold with arachidonoyl-CoA as a substrate, indicating specificity for this fatty acid
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