LPGAT1 controls the stearate/palmitate ratio of phosphatidylethanolamine and phosphatidylcholine in sn-1 specific remodeling

Abstract

Most mammalian phospholipids contain a saturated fatty acid at the sn-1 carbon atom and an unsaturated fatty acid at the sn-2 carbon atom of the glycerol backbone group. While the sn-2 linked chains undergo extensive remodeling by deacylation and reacylation (Lands cycle), it is not known how the composition of saturated fatty acids is controlled at the sn-1 position. Here, we demonstrate that lysophosphatidylglycerol acyltransferase 1 (LPGAT1) is an sn-1 specific acyltransferase that controls the stearate/palmitate ratio of phosphatidylethanolamine (PE) and phosphatidylcholine. Bacterially expressed murine LPGAT1 transferred saturated acyl-CoAs specifically into the sn-1 position of lysophosphatidylethanolamine (LPE) rather than lysophosphatidylglycerol and preferred stearoyl-CoA over palmitoyl-CoA as the substrate. In addition, genetic ablation of LPGAT1 in mice abolished 1-LPE:stearoyl-CoA acyltransferase activity and caused a shift from stearate to palmitate species in PE, dimethyl-PE, and phosphatidylcholine. Lysophosphatidylglycerol acyltransferase 1 KO mice were leaner and had a shorter life span than their littermate controls. Finally, we show that total lipid synthesis was reduced in isolated hepatocytes of LPGAT1 knockout mice. Thus, we conclude that LPGAT1 is an sn-1 specific LPE acyltransferase that controls the stearate/palmitate homeostasis of PE and the metabolites of the PE methylation pathway and that LPGAT1 plays a central role in the regulation of lipid biosynthesis with implications for body fat content and longevity. Most mammalian phospholipids contain a saturated fatty acid at the sn-1 carbon atom and an unsaturated fatty acid at the sn-2 carbon atom of the glycerol backbone group. While the sn-2 linked chains undergo extensive remodeling by deacylation and reacylation (Lands cycle), it is not known how the composition of saturated fatty acids is controlled at the sn-1 position. Here, we demonstrate that lysophosphatidylglycerol acyltransferase 1 (LPGAT1) is an sn-1 specific acyltransferase that controls the stearate/palmitate ratio of phosphatidylethanolamine (PE) and phosphatidylcholine. Bacterially expressed murine LPGAT1 transferred saturated acyl-CoAs specifically into the sn-1 position of lysophosphatidylethanolamine (LPE) rather than lysophosphatidylglycerol and preferred stearoyl-CoA over palmitoyl-CoA as the substrate. In addition, genetic ablation of LPGAT1 in mice abolished 1-LPE:stearoyl-CoA acyltransferase activity and caused a shift from stearate to palmitate species in PE, dimethyl-PE, and phosphatidylcholine. Lysophosphatidylglycerol acyltransferase 1 KO mice were leaner and had a shorter life span than their littermate controls. Finally, we show that total lipid synthesis was reduced in isolated hepatocytes of LPGAT1 knockout mice. Thus, we conclude that LPGAT1 is an sn-1 specific LPE acyltransferase that controls the stearate/palmitate homeostasis of PE and the metabolites of the PE methylation pathway and that LPGAT1 plays a central role in the regulation of lipid biosynthesis with implications for body fat content and longevity. Phospholipids contain two fatty acids attached to the sn-1 and sn-2 carbon atoms of the glycerol group. In general, the sn-1 position is occupied by saturated fatty acids, primarily palmitate (C16:0) or stearate (C18:0). In contrast, the sn-2 position contains predominantly unsaturated fatty acids, the composition of which is regulated by fatty acid remodeling. The canonical remodeling pathway, widely known as the Lands cycle, starts with the removal of the sn-2 linked fatty acid (phospholipase A2) and is completed by the transfer of another fatty acid from acyl-CoA (acyltransferase). The cycle balances the composition of unsaturated fatty acids in the sn-2 position (1Lands W.E.M. Stories about acyl chains.Biochim. Biophys. Acta. 2000; 1483: 1-14Google Scholar), which is thought to be critical for the physical properties, the metabolic fate, and the cellular function of phospholipids (2Hishikawa D. Hashidate T. Shimizu T. Shindou H. Diversity and function of membrane glycerophospholipids generated by the remodeling pathway in mammalian cells.J. Lipid Res. 2014; 55: 799-807Google Scholar, 3Yamashita A. Hayashi Y. Nemoto-Sasaki Y. Ito M. Oka S. Tanikawa T. Waku K. Sugiura T. Acyltransferases and transacylases that determine the fatty acid composition of glycerolipids and the metabolism of bioactive lipid mediators in mammalian cells and model organisms.Prog. Lipid Res. 2014; 53: 18-81Google Scholar). Several acyltransferases have been identified and shown to have distinct phospholipid head group and acyl specificities, confirming the importance of acyltransferases for the phospholipid species composition (4Shindou H. Shimizu T. Acyl-CoA:Lysophospholipid acyltransferases.J. Biol. Chem. 2009; 284: 1-5Google Scholar). In addition to the Lands cycle, a separate pathway has been postulated for sn-1 linked fatty acids (5Thompson W. Belina H. Rapid accumulation of diacyl lipid in rat liver microsomes by selective acylation of 2-acyl-sn-glycero-3-phosphorylserine.Biochim. Biophys. Acta. 1986; 876: 379-386Google Scholar, 6Tijburg L.B.M. Samborski R.W. Vance D.E. Evidence that remodeling of the fatty acids of phosphatidylcholine is regulated in isolated rat hepatocytes and involves both the sn-1 and sn-2 positions.Biochim. Biophys. Acta. 1991; 1085: 184-190Google Scholar). This pathway requires the combined action of a phospholipase A1 and an sn-1 specific acyltransferase. The idea of sn-1 remodeling has been tentatively supported by the discovery of an acyltransferase that incorporates stearic acid into the sn-1 position of phosphatidylinositol (PI) (7Imae R. Inoue T. Kimura M. Kanamori T. Tomioka N.H. Kage-Nakadai E. Mitani S. Arai H. Intracellular phospholipase A1 and acyltransferase, which are involved in Caenorhabditis elegans stem cell divisions, determine the sn-1 fatty acyl chain of phosphatidylinositol.Mol. Biol. Cell. 2010; 21: 3114-3124Google Scholar, 8Imae R. Inoue T. Nakasaki Y. Uchida Y. Ohba Y. Kono N. Nakanishi H. Sasaki T. Mitani S. Arai H. LYCAT, a homologue of C. elegans acl-8, acl-9, and acl-10, determines the fatty acid composition of phosphatidylinositol in mice.J. Lipid Res. 2012; 53: 335-347Google Scholar, 9Kawana H. Kano K. Shindou H. Inoue A. Shimizu T. Aoki J. An accurate and versatile method for determining the acyl group-introducing position of lysophospholipid acyltransferases.Biochim. Biophys. Acta Mol. Cell Biol. Lipids. 2019; 1864: 1053-1060Google Scholar, 10Le Guédard M. Bessoule J.J. Boyer V. Ayciriex S. Velours G. Kulik W. Ejsing C.S. Shevchenko A. Coulon D. Lessire R. Testet E. PSI1 is responsible for the stearic acid enrichment that is characteristic of phosphatidylinositol in yeast.FEBS J. 2009; 276: 6412-6424Google Scholar) and by the data, suggesting the active reacylation of partially oxidized 1-lyso-phospholipids (11Liu G.Y. Moon S.H. Jenkins C.M. Sims H.F. Guan S. Gross R.W. Synthesis of oxidized phospholipids by sn-1 acyltransferase using 2–15-HETE lysophospholipids.J. Biol. Chem. 2019; 294: 10146-10159Google Scholar). However, sn-1 remodeling is not nearly as well established as sn-2 remodeling. In particular, it is not known whether sn-1 remodeling is a widespread phenomenon among phospholipids and whether it has functional significance. Here, we establish lysophosphatidylglycerol acyltransferase 1 (LPGAT1) as a pivotal sn-1 remodeling enzyme and show that it is of central importance for the regulation of lipid metabolism. Lysophosphatidylglycerol acyltransferase 1 was first identified as acyltransferase based on sequence homology and expressed in insect cells, which suggested that lysophosphatidylglycerol (LPG) and stearoyl-CoA are the preferred substrates. This led to the assumption that LPGAT1 remodels phosphatidylglycerol (PG), an intermediate on the cardiolipin (CL) pathway, hence the name LPG acyltransferase 1 (12Yang Y. Cao J. Shi Y. Identification and characterization of a gene encoding human LPGAT1, an endoplasmic reticulum-associated lysophosphatidylglycerol acyltransferase.J. Biol. Chem. 2004; 279: 55866-55874Google Scholar). However, a number of contradictions have emerged. First, LPGAT1 is located in the endoplasmic reticulum (12Yang Y. Cao J. Shi Y. Identification and characterization of a gene encoding human LPGAT1, an endoplasmic reticulum-associated lysophosphatidylglycerol acyltransferase.J. Biol. Chem. 2004; 279: 55866-55874Google Scholar) whereas PG is formed and converted to CL in the inner mitochondrial membrane (13Hostetler K.Y. van den Bosch H. Subcellular and submitochondrial localization of the biosynthesis of cardiolipin and related phospholipids in rat liver.Biochim. Biophys. Acta. 1972; 260: 380-386Google Scholar). Second, the preference for saturated acyl-CoA’s of LPGAT1 (12Yang Y. Cao J. Shi Y. Identification and characterization of a gene encoding human LPGAT1, an endoplasmic reticulum-associated lysophosphatidylglycerol acyltransferase.J. Biol. Chem. 2004; 279: 55866-55874Google Scholar) does not match the species composition of either PG or CL (14Zhang X. Zhang J. Sun H. Liu X. Zheng Y. Xu D. Wang J. Jia D. Han X. Liu F. Nie J. Shi Y. Defective phosphatidylglycerol remodeling mitochondrial to Mol. 2019; Scholar). Finally, a LPGAT1 KO model was In of LPGAT1 caused in the species composition of PG and CL in phospholipids (14Zhang X. Zhang J. Sun H. Liu X. Zheng Y. Xu D. Wang J. Jia D. Han X. Liu F. Nie J. Shi Y. Defective phosphatidylglycerol remodeling mitochondrial to Mol. 2019; Scholar). as to whether LPGAT1 is involved in the remodeling of is the is that have suggested a LPGAT1 and metabolism. Lysophosphatidylglycerol acyltransferase 1 is regulated by the that controls the transfer J. J. J. C. and in mice by lipid synthesis and Scholar) and in the LPGAT1 gene are with in S. A. C. Evidence for a role of LPGAT1 in and body fat in 21: Scholar). and of LPGAT1 in mice the of and the fat content of liver (14Zhang X. Zhang J. Sun H. Liu X. Zheng Y. Xu D. Wang J. Jia D. Han X. Liu F. Nie J. Shi Y. Defective phosphatidylglycerol remodeling mitochondrial to Mol. 2019; Scholar, Y. H. S. R. acyltransferase plays an role in Lipid Res. 2010; Scholar). Lysophosphatidylglycerol acyltransferase 1 was to have acyltransferase which in the to metabolism Y. H. S. R. acyltransferase plays an role in Lipid Res. 2010; Scholar). However, it is to that LPGAT1 with and two it is of the the acyltransferase activity of LPGAT1 is to with substrates. In the function of LPGAT1 is that LPGAT1 is to acyltransferases and acyltransferase activity (12Yang Y. Cao J. Shi Y. Identification and characterization of a gene encoding human LPGAT1, an endoplasmic reticulum-associated lysophosphatidylglycerol acyltransferase.J. Biol. Chem. 2004; 279: 55866-55874Google Scholar, Y. H. S. R. acyltransferase plays an role in Lipid Res. 2010; Scholar) the of LPGAT1 have not been Several have suggested an of LPGAT1 in metabolism (14Zhang X. Zhang J. Sun H. Liu X. Zheng Y. Xu D. Wang J. Jia D. Han X. Liu F. Nie J. Shi Y. Defective phosphatidylglycerol remodeling mitochondrial to Mol. 2019; Scholar, J. J. J. C. and in mice by lipid synthesis and Scholar, S. A. C. Evidence for a role of LPGAT1 in and body fat in 21: Scholar, Y. H. S. R. acyltransferase plays an role in Lipid Res. 2010; Scholar) is known about the Thus, we to the function of LPGAT1 and that it is an sn-1 specific acyltransferase involved in the stearate/palmitate functional caused by LPGAT1 we mice from a mice were at the ratio and body at the of However, their body fat content was reduced by about has been in another LPGAT1 KO model it was with a in body (14Zhang X. Zhang J. Sun H. Liu X. Zheng Y. Xu D. Wang J. Jia D. Han X. Liu F. Nie J. Shi Y. Defective phosphatidylglycerol remodeling mitochondrial to Mol. 2019; Scholar). mice a in which reduced their life span to about we in to mice. of in the suggested that were to their which was supported by of the by The in the of LPGAT1 in human and and that it is with (12Yang Y. Cao J. Shi Y. Identification and characterization of a gene encoding human LPGAT1, an endoplasmic reticulum-associated lysophosphatidylglycerol acyltransferase.J. Biol. Chem. 2004; 279: 55866-55874Google Scholar). In the was in whereas in mice the were in and suggested a role of LPGAT1 in liver metabolism (14Zhang X. Zhang J. Sun H. Liu X. Zheng Y. Xu D. Wang J. Jia D. Han X. Liu F. Nie J. Shi Y. Defective phosphatidylglycerol remodeling mitochondrial to Mol. 2019; Scholar, J. J. J. C. and in mice by lipid synthesis and Scholar, Y. H. S. R. acyltransferase plays an role in Lipid Res. 2010; Scholar), we the of LPGAT1 on the the lipid composition and the species composition While the of lipid not in to LPGAT1 we in the species composition of phospholipids the lipid we the by of lipid a to LPGAT1 to phosphatidylethanolamine to phosphatidylcholine and to Thus, the of species by LPGAT1 were with the PE methylation pathway In contrast, the composition of PG and CL the composition of and in to LPGAT1 The PE methylation pathway by PE The enzyme PE first into into and into D.E. methylation in to Biophys. Acta. 2014; Scholar). that LPGAT1 the of and species and the of and species in of the PE methylation species of PE, and the that a in stearate and an in palmitate in to LPGAT1 a the stearate/palmitate ratio in PE, and and in their In contrast, and and from the species composition were in acid and and a to LPGAT1 as the liver In of LPGAT1 led to of stearate species by palmitate species in phospholipids of the PE methylation pathway, PE, and This in the species composition was in and was with the of metabolic body and not on the of LPGAT1, we the of the First, we expressed murine LPGAT1 in insect cells and the the enzyme was active with lysophosphatidylethanolamine (LPE) than with activity with activity with and However, the of LPGAT1 in insect cells was and not from to In to a enzyme we expressed murine LPGAT1 to in a known to of we that be in and to on However, we were to acyltransferase In to an active we the which to of the we of total cells we to an enzyme that was in the the method E. with an acyltransferase activity that was than that of the of we the we a acyltransferase activity with LPE than with LPG or and activity with acid and that LPGAT1 palmitate and fatty acids to the sn-1 we whether LPGAT1 has we the activity of with the and The enzyme had an about activity with suggesting that LPGAT1 to with the sn-1 group as and a activity with the than the their were to the activity with we the acyl of by the and The a preference for saturated acyl-CoAs and a activity with stearoyl-CoA than with palmitoyl-CoA the function of LPGAT1, we the of LPGAT1 on the acyltransferase activity in liver we that microsomes had an about acyltransferase activity with than with of LPGAT1 activity with either suggesting that LPGAT1 is the acyltransferase of liver microsomes LPGAT1 abolished acyltransferase it had on acyltransferase confirming the of the enzyme Finally, we the of LPGAT1 on acyltransferase with and that microsomes and at a than were by LPGAT1 reacylation of with to the of was not by LPGAT1 of whether or was the In demonstrate that LPGAT1 is an LPE acyltransferase with preference for stearoyl-CoA and the sn-1 group. it for of the LPE acyltransferase activity of liver The of LPGAT1 and the of LPGAT1 on the murine that the enzyme in the remodeling of saturated fatty acids at the sn-1 position of PE with for the of the PE methylation we the of LPGAT1 on the lipid by hepatocytes with and the of by have shown that the of be to the of synthesis of the glycerol backbone of lipid species M. Xu Y. H. M. to the of in and Lipid Res. Scholar). we that LPGAT1 reduced the of synthesis of as and However, the was not specific to as the synthesis of the species as well and the synthesis of and at a of LPGAT1 on lipid While the synthesis of PE and about the and which are of the sn-2 remodeling pathway, were not are with the that LPGAT1 is not involved in the Lands of the that LPGAT1 reduced the synthesis of and the synthesis of and PG LPGAT1 had an extensive on lipid we whether it the first which is the of the of species is we were to the two of and Y. H. G. D. Waku K. of the species of and in rat liver microsomes Biophys. Acta. Scholar), and their in of species that LPGAT1 reduced the synthesis of in hepatocytes However, LPGAT1 not in isolated liver microsomes with and palmitoyl-CoA stearoyl-CoA This suggested that was reduced in the of the acyltransferase that LPGAT1 was not involved in of the acyl transfer that converted into In that LPGAT1 the of lipid biosynthesis in While the of phenomenon to be the a central role of LPGAT1 in the cellular of lipid metabolism. and stearate are the two saturated fatty acids linked to the sn-1 carbon atoms of mammalian phospholipid species formed by synthesis contain palmitate and stearate than species L.B.M. Samborski R.W. Vance D.E. Evidence that remodeling of the fatty acids of phosphatidylcholine is regulated in isolated rat hepatocytes and involves both the sn-1 and sn-2 positions.Biochim. Biophys. Acta. 1991; 1085: 184-190Google Scholar, Y. H. G. D. Waku K. of the species of and in rat liver microsomes Biophys. Acta. Scholar), the ratio has to be The of palmitate and stearate to be have that either the genetic of the ratio in phospholipids T. H. N. T. A. T. Inoue N. M. S. N. H. Y. T. S. T. role of a fatty acid in Scholar) or the of the ratio Xu F. Han D. Zhang J. fat with a ratio metabolic and in Scholar) and body fat Thus, it that the ratio requires than it has been postulated that species be converted into species by sn-1 remodeling the enzyme has L.B.M. Samborski R.W. Vance D.E. Evidence that remodeling of the fatty acids of phosphatidylcholine is regulated in isolated rat hepatocytes and involves both the sn-1 and sn-2 positions.Biochim. Biophys. Acta. 1991; 1085: 184-190Google Scholar). In we LPGAT1 as the acyltransferase for the postulated sn-1 remodeling and that it in with a to be identified phospholipase A1 show that LPGAT1 is an sn-1 specific acyltransferase with a preference for saturated fatty acids over unsaturated fatty acids and a preference for stearoyl-CoA over with the preference for we demonstrate that genetic ablation of LPGAT1 in a in the ratio in The that LPGAT1 in with a phospholipase A1 is supported by the accumulation of unsaturated LPE species in mice discovery a number of First, it the whether a specific phospholipase A1 is involved in the postulated sn-1 remodeling or whether to Thus, a be to the that with Second, the of lipid biosynthesis in mice is and the of how PE remodeling controls phospholipid be to determine whether LPGAT1 lipid the regulation of enzyme or or whether the of LPGAT1 have an on lipid it has to be whether PE methylation or have role in the regulation of lipid LPGAT1 KO the ratio of LPGAT1 not have acyltransferase we that PE is converted to by the PE methylation In of we that LPGAT1 had the on the methylation pathway intermediate as it had on PE and how LPGAT1 is linked to the PE methylation pathway that both LPGAT1 (14Zhang X. Zhang J. Sun H. Liu X. Zheng Y. Xu D. Wang J. Jia D. Han X. Liu F. Nie J. Shi Y. Defective phosphatidylglycerol remodeling mitochondrial to Mol. 2019; Scholar) and Vance Vance D.E. and of a phosphatidylethanolamine specific and for a membrane in rat Biol. Chem. Scholar) are of the endoplasmic The that is as as PE by LPGAT1 PE methylation about of the total synthesis D.E. methylation in to Biophys. Acta. 2014; Scholar) that PE species are to The idea of an is with a of species in to formed by the pathway of phosphatidylcholine synthesis the pathway and phosphatidylethanolamine methylation Biol. Chem. Scholar). Thus, LPGAT1 is involved in the two saturated fatty acids, palmitate and in the two PE and of LPGAT1 in metabolism has been suggested LPGAT1 caused a of and in an of and in liver (14Zhang X. Zhang J. Sun H. Liu X. Zheng Y. Xu D. Wang J. Jia D. Han X. Liu F. Nie J. Shi Y. Defective phosphatidylglycerol remodeling mitochondrial to Mol. 2019; Scholar, Y. H. S. R. acyltransferase plays an role in Lipid Res. 2010; Scholar). show that LPGAT1 which in the of for and the of However, not the idea that LPGAT1 is involved in synthesis acyl transfer to as by Y. H. S. R. acyltransferase plays an role in Lipid Res. 2010; Scholar). that the acyltransferase activity of LPGAT1 with as was about of activity with LPE as substrate. Thus, acyltransferase activity is an function of to two for the of LPGAT1 in metabolism. First, that LPGAT1 to the PE methylation pathway, which is known to be involved in Vance D.E. The active synthesis of phosphatidylcholine is for from rat Biol. Chem. Scholar, Y. Vance D.E. An for phosphatidylethanolamine in the of Biol. Chem. Scholar, Vance D.E. role for phosphatidylethanolamine phosphatidylcholine in the regulation of and in mice.J. Biol. Chem. Scholar). that from both the PE methylation pathway and the pathway, are for D.E. methylation in to Biophys. Acta. 2014; Scholar). LPGAT1 to the PE methylation pathway that which in is for Second, that LPGAT1 is lipid which the of by the of is to establish whether of is The of LPGAT1 as acyltransferase, which led to name (12Yang Y. Cao J. Shi Y. Identification and characterization of a gene encoding human LPGAT1, an endoplasmic reticulum-associated lysophosphatidylglycerol acyltransferase.J. Biol. Chem. 2004; 279: 55866-55874Google Scholar), be in to the of at the the enzyme was and in to the of the of the enzyme in insect cells it to the activity from (12Yang Y. Cao J. Shi Y. Identification and characterization of a gene encoding human LPGAT1, an endoplasmic reticulum-associated lysophosphatidylglycerol acyltransferase.J. Biol. Chem. 2004; 279: 55866-55874Google Scholar). In contrast, we expressed LPGAT1 in E. and a of substrates. and by confirming the in a KO we were to demonstrate that LPGAT1 is an sn-1 specific LPE acyltransferase. In we identified LPGAT1 as acyltransferase and for Lysophosphatidylglycerol acyltransferase 1 controls the composition of the saturated fatty acids linked to the sn-1 position of PE and the of the PE methylation pathway and it has a on cellular lipid LPGAT1 has for body fat content and life LPGAT1 as a central function is to saturated fatty acids in the sn-1 position of PE and and to lipid biosynthesis in the endoplasmic were by the and of the of and to the for the and of by the of were in a a cycle with to and The LPGAT1 KO was from The as a mice were identified by of The mice were a body composition and fat were using a to the was using the function with the by the The mice were in with with at 1 The mice were in the position and the in position the as The head was of the to body and of for determining in body composition of Res. 2000; Scholar). were from and at were with The were in and at In to were in using a was isolated from using were by the An of of was to first using the was by with the and the by LPGAT1 was with the and the LPGAT1 was with the and the The LPGAT1 was to the of was with the and the was with the and the The were by the method of gene using and the Scholar). were from into as method of total lipid and J. Scholar). In the were in and at for to An of of an from was and were the were and was by The was and in were by using a to a An of was into a that was at a of was with and at a of 1 and 1 and The was the of in a from to from to from to from to from to from to from to from to and from to the of the the of at The was in or The was to and the was to were at a of an of a of and a of to were at a of an of a of a of and an of The was to and the to lipid and the were by the The was with a of a of an of and an of and were as in was as in and phospholipids as in mice were with The was with and was was into the and the was The liver was the with and with was and into a was and to An of of was to the liver and the was to and were by and with of hepatocytes were in hepatocytes were 1 at was and hepatocytes were the was with and The was for to The cells were with a cell at for and at which was as M. Xu Y. H. M. to the of in and Lipid Res. Scholar). were and into the Lipid species were identified by the had the as the and a that was than the were in using a of at their were from the of and at The of the was from the of PG M. Xu Y. H. M. to the of in and Lipid Res. Scholar). were by to the of the LPGAT1 was with the and the The was into the which was to E. of was with the of of and of were by addition of the with to were in 1 and on a The cells were at for which 1 was to a of The cells were for another to at The was and by to cells were by at for The cells were and were by at for and the were isolated by at for 1 at The were in and LPGAT1 was with the were as with Biol. Chem. Scholar). Lysophosphatidylglycerol acyltransferase 1 was into the using the E. cells were with was by to a of The cells were at in an at and at an of to Cell were in with 1 The cells were for to cells and were by at for at E. were by at for 1 at a we E. by the was in with the were as with Biol. Chem. Scholar). were with The was and was The liver was and in and were in and were by at and The was in an at for 1 The was in into and at was as with Biol. Chem. Scholar). acyltransferase were in 1 lysophospholipid or and acyl-CoA at were by either LPGAT1 E. or or liver microsomes The were or by and 1 were and by as of and were in The acyltransferase activity of liver microsomes was as Identification of a acyltransferase in Biol. Chem. 2004; 279: Scholar) in a 1 and The was by liver microsomes to The were at and the was by and 1 were and was by as G. K. Guan S. Han X. Gross R.W. of cellular glycerophospholipids by Chem. Scholar). are the This contains The that have of with the of Y. C. C. K. M. T. S. and M. S. Y. X. C. K. M. M. M. and M. S. C. K. M. and M. M. H. and M. M. H. and M. S. M. S. This was supported in by of M. and and M. M. The content is the of the and does not the of the of

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