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Acyl CoA:monoacylglycerol acyltransferase (MGAT) catalyzes the resynthesis of triacylglycerol, a crucial step in the absorption of dietary fat. Mice lacking the gene Mogat2, which codes for an MGAT highly expressed in the small intestine, are resistant to obesity and other metabolic disorders induced by high-fat feeding. Interestingly, these Mogat2−/− mice absorb normal amounts of dietary fat but exhibit a reduced rate of fat absorption, increased energy expenditure, decreased respiratory exchange ratio, and impaired metabolic efficiency. MGAT2 is expressed in tissues besides intestine. To test the hypothesis that intestinal MGAT2 enhances metabolic efficiency and promotes the storage of metabolic fuels, we introduced the human MOGAT2 gene driven by the intestine-specific villin promoter into Mogat2−/− mice. We found that the expression of MOGAT2 in the intestine increased intestinal MGAT activity, restored fat absorption rate, partially corrected energy expenditure, and promoted weight gain upon high-fat feeding. However, the changes in respiratory exchange ratio were not reverted, and the recoveries in metabolic efficiency and weight gain were incomplete. These data indicate that MGAT2 in the intestine plays an indispensable role in enhancing metabolic efficiency but also raise the possibility that MGAT2 in other tissues may contribute to the regulation of energy metabolism. Acyl CoA:monoacylglycerol acyltransferase (MGAT) catalyzes the resynthesis of triacylglycerol, a crucial step in the absorption of dietary fat. Mice lacking the gene Mogat2, which codes for an MGAT highly expressed in the small intestine, are resistant to obesity and other metabolic disorders induced by high-fat feeding. Interestingly, these Mogat2−/− mice absorb normal amounts of dietary fat but exhibit a reduced rate of fat absorption, increased energy expenditure, decreased respiratory exchange ratio, and impaired metabolic efficiency. MGAT2 is expressed in tissues besides intestine. To test the hypothesis that intestinal MGAT2 enhances metabolic efficiency and promotes the storage of metabolic fuels, we introduced the human MOGAT2 gene driven by the intestine-specific villin promoter into Mogat2−/− mice. We found that the expression of MOGAT2 in the intestine increased intestinal MGAT activity, restored fat absorption rate, partially corrected energy expenditure, and promoted weight gain upon high-fat feeding. However, the changes in respiratory exchange ratio were not reverted, and the recoveries in metabolic efficiency and weight gain were incomplete. These data indicate that MGAT2 in the intestine plays an indispensable role in enhancing metabolic efficiency but also raise the possibility that MGAT2 in other tissues may contribute to the regulation of energy metabolism. Acyl CoA:monoacylglycerol acyltransferase (MGAT) catalyzes the esterification of monoacylglycerol and fatty acids (in the form of acyl CoA) to generate diacylglycerol, a precursor of triacylglycerol and phospholipids (1Bell R.M. Coleman R.A. Enzymes of glycerolipid synthesis in eukaryotes.Annu. Rev. Biochem. 1980; 49: 459-487Crossref PubMed Scopus (456) Google Scholar). The enzyme plays a prominent role in the intestine, where monoacylglycerol and fatty acids resulting from the digestion of dietary triacylglycerol are resynthesized in the enterocytes. This triacylglycerol resynthesis is required for the assembly of chylomicrons, which transport the absorbed dietary fat and other lipid-soluble nutrients in the circulation (2Mansbach C.M. Siddiqi S.A. The biogenesis of chylomicrons.Annu. Rev. Physiol. 2010; 72: 315-333Crossref PubMed Scopus (142) Google Scholar, 3Kayden H.J. Senior J.R. Mattson F.H. Monoglyceride pathway of fat absorption on man.J. Clin. Invest. 1967; 46: 1695-1703Crossref PubMed Scopus (84) Google Scholar). MGAT activity has also been reported in a few other tissues of vertebrates, including liver and adipose tissues (4Schultz F.M. Johnston J.M. The synthesis of higher glycerides via the monoglyceride pathway in hamster adipose tissue.J. Lipid Res. 1971; 12: 132-138Abstract Full Text PDF PubMed Google Scholar, 5Coleman R.A. Haynes E.B. Hepatic monoacylglycerol acyltransferase - characterization of an activity associated with the suckling period in rats.J. Biol. Chem. 1984; 259: 8934-8938Abstract Full Text PDF PubMed Google Scholar), where its physiological roles remain to be determined. In contrast, enzymes that catalyze triacylglycerol synthesis through sequential acylation of glycerol-3-phosphate are expressed in most cells, and this alternative GPAT pathway is dominant in most tissues (6Coleman R.A. Mashek D.G. Mammalian triacylglycerol metabolism: synthesis, lipolysis, and signaling.Chem. Rev. 2011; 111: 6359-6386Crossref PubMed Scopus (170) Google Scholar). Three homologous genes, Mogat1–3, have been identified to encode MGAT enzymes in mammals (7Yen C-L.E. Stone S.J. Cases S. Zhou P. Farese Jr, R.V. Identification of a gene encoding MGAT1, a monoacylglylcerol acyltransferase.Proc. Natl. Acad. Sci. USA. 2002; 99: 8512-8517Crossref PubMed Scopus (151) Google Scholar, 8Yen C.L. Farese Jr, R.V. MGAT2, a monoacylglycerol acyltransferase expressed in the small intestine.J. Biol. Chem. 2003; 278: 18532-18537Abstract Full Text Full Text PDF PubMed Scopus (145) Google Scholar, 9Cao J. Lockwood J. Burn P. Shi Y. Cloning and functional characterization of a mouse intestinal acyl-CoA:monoacylglycerol acyltransferase, MGAT2.J. Biol. Chem. 2003; 278: 13860-13866Abstract Full Text Full Text PDF PubMed Scopus (109) Google Scholar–10Cheng D. Nelson T.C. Chen J. Walker S.G. Wardwell-Swanson J. Meegalla R. Taub R. Billheimer J.T. Ramaker M. Feder J.N. Identification of acyl coenzyme A:monoacylglycerol acyltransferase 3, an intestinal specific enzyme implicated in dietary fat absorption.J. Biol. Chem. 2003; 278: 13611-13614Abstract Full Text Full Text PDF PubMed Scopus (120) Google Scholar). Among them, Mogat2 is highly expressed in the intestine of both humans and rodents (8Yen C.L. Farese Jr, R.V. MGAT2, a monoacylglycerol acyltransferase expressed in the small intestine.J. Biol. Chem. 2003; 278: 18532-18537Abstract Full Text Full Text PDF PubMed Scopus (145) Google Scholar, 11Cao J. Burn P. Shi Y. Properties of the mouse intestinal acyl-CoA:monoacylglycerol acyltransferase, MGAT2.J. Biol. Chem. 2003; 278: 25657-25663Abstract Full Text Full Text PDF PubMed Scopus (54) Google Scholar). Consistent with an essential role in intestinal fat absorption, mice with the gene disrupted (Mogat2−/−) are protected from obesity and other metabolic disorders induced by high-fat feeding (12Yen C.L. Cheong M.L. Grueter C. Zhou P. Moriwaki J. wong J.S. Hubbard B. Marmor S. Farese Jr, R.V. Deficiency of the intestinal enzyme acyl CoA:monoacylglycerol acyltransferase-2 protects mice from metabolic disorders induced by high-fat feeding.Nat. Med. 2009; 15: 442-446Crossref PubMed Scopus (133) Google Scholar). However, these mice consume and absorb normal quantities of fat. Associated with a delay in the entry of dietary fat into the circulation, Mogat2−/− mice exhibit an unexpected increase in energy expenditure, accounting for decreases in metabolic efficiency (12Yen C.L. Cheong M.L. Grueter C. Zhou P. Moriwaki J. wong J.S. Hubbard B. Marmor S. Farese Jr, R.V. Deficiency of the intestinal enzyme acyl CoA:monoacylglycerol acyltransferase-2 protects mice from metabolic disorders induced by high-fat feeding.Nat. Med. 2009; 15: 442-446Crossref PubMed Scopus (133) Google Scholar). Interestingly, Mogat2−/− mice exhibit increases in energy expenditure even when fed a fat-free diet, and inactivating MGAT2 in the absence of high-fat feeding also protects the hyperphagic Agouti yellow mouse from excess weight gain (13Nelson D.W. Gao Y. Spencer N.M. Banh T. Yen C.L. Deficiency of MGAT2 increases energy expenditure without high-fat feeding and protects genetically obese mice from excessive weight gain.J. Lipid Res. 2011; 52: 1723-1732Abstract Full Text Full Text PDF PubMed Scopus (32) Google Scholar). These findings suggest that intestinal MGAT2 regulates systemic energy metabolism but cannot rule out a role of the low levels of MGAT2 expression in other tissues, including brown and white adipose tissues (12Yen C.L. Cheong M.L. Grueter C. Zhou P. Moriwaki J. wong J.S. Hubbard B. Marmor S. Farese Jr, R.V. Deficiency of the intestinal enzyme acyl CoA:monoacylglycerol acyltransferase-2 protects mice from metabolic disorders induced by high-fat feeding.Nat. Med. 2009; 15: 442-446Crossref PubMed Scopus (133) Google Scholar). Indeed, in the adipose tissues of genetically identical C57Bl/6J mice, the expression levels of MGAT2 are higher in mice that gain more weight in response to high-fat feeding (14Koza R.A. Nikonova L. Hogan J. Rim J.S. Mendoza T. Faulk C. Skaf J. Kozak L.P. Changes in gene expression foreshadow diet-induced obesity in genetically identical mice.PLoS Genet. 2006; 2: e81Crossref PubMed Scopus (271) Google Scholar), suggesting that MGAT2 may play a functional role in that tissue. To test the hypothesis that MGAT2 in the intestine mediates triacylglycerol synthesis required for maximizing the assimilation of dietary fat and to determine the extent to which intestinal MGAT2 contributes to metabolic efficiency, in this study we examined whether expressing MGAT2 specifically in the intestine of Mogat2−/− mice is sufficient to normalize intestinal lipid processing and systemic energy balance upon high-fat feeding. To generate a transgene for overexpressing MGAT2 in the intestine specifically, human MGAT2 cDNA into the the of the villin gene of D. of which expression the intestinal of mice L. of the villin gene expression in of the and of the intestine.J. Biol. Chem. 2002; Full Text Full Text PDF PubMed Scopus Google Scholar). The the villin to MGAT2 cDNA were and into of C57Bl/6J mice. were with C57Bl/6J mice to generate and with low expression of human MOGAT2 were and and for reported in this Mogat2−/− mice in the C57Bl/6J were reported (12Yen C.L. Cheong M.L. Grueter C. Zhou P. Moriwaki J. wong J.S. Hubbard B. Marmor S. Farese Jr, R.V. Deficiency of the intestinal enzyme acyl CoA:monoacylglycerol acyltransferase-2 protects mice from metabolic disorders induced by high-fat feeding.Nat. Med. 2009; 15: 442-446Crossref PubMed Scopus (133) Google Scholar). mice the transgene were with mice without the transgene to generate for of of mice mice with gene but not the mice without and mice without gene but with a low of and from both were in the in metabolic were more (12Yen C.L. Cheong M.L. Grueter C. Zhou P. Moriwaki J. wong J.S. Hubbard B. Marmor S. Farese Jr, R.V. Deficiency of the intestinal enzyme acyl CoA:monoacylglycerol acyltransferase-2 protects mice from metabolic disorders induced by high-fat feeding.Nat. Med. 2009; 15: 442-446Crossref PubMed Scopus (133) Google Scholar), mice were for Mice were on a of mice and changes of and were and were by the of and and were in with the on and of To the of the a on and with a The a and a from mouse Mogat2 and human MOGAT2 To determine the absence of the mouse in Mogat2−/− mice, (12Yen C.L. Cheong M.L. Grueter C. Zhou P. Moriwaki J. wong J.S. Hubbard B. Marmor S. Farese Jr, R.V. Deficiency of the intestinal enzyme acyl CoA:monoacylglycerol acyltransferase-2 protects mice from metabolic disorders induced by high-fat feeding.Nat. Med. 2009; 15: 442-446Crossref PubMed Scopus (133) Google Scholar). Mice were fed a of from fat were to the of with dietary fat on and energy expenditure and In these were were and fat and to increase fat from to and are from mice fed a fat for were and and through to and with and with the expression levels were by the of in the expression an The to the in gene expression of gene expression data and the PubMed Scopus Google Scholar). The to both mouse and human MGAT2 to to where the human and mouse Mogat2 the is and the is The of gene are and MGAT activity were with (7Yen C-L.E. Stone S.J. Cases S. Zhou P. Farese Jr, R.V. Identification of a gene encoding MGAT1, a monoacylglylcerol acyltransferase.Proc. Natl. Acad. Sci. USA. 2002; 99: 8512-8517Crossref PubMed Scopus (151) Google Scholar). were by to the and were by of The were by on with and with were identified by with the of lipid The of into lipid by an by and in a To the and processing of were into intestine in mice L. J. metabolism in human intestinal for metabolic and Biol. Chem. 2002; Full Text Full Text PDF PubMed Scopus Google Scholar). were by and with to of and The with of in and for Mice were for a the of the in the and the To an in the intestine, a the small intestine to the of the and and and to the of the In a an in the intestine in the of the to the the into of the the and the small intestinal were The out and from the small intestine the small intestine were with and by a by and by The to triacylglycerol monoacylglycerol and phospholipids were into for of To that few were from the small intestine the and adipose tissues were also and absorption an of an Mice to high-fat feeding for were for of a of were with of the from to the of J.S. Billheimer J.T. in of with Lipid Res. 46: Full Text Full Text PDF PubMed Scopus Google Scholar). To the rate which dietary fat circulation, and mice were with of for and metabolic with and to the to to energy including of and of and (13Nelson D.W. Gao Y. Spencer N.M. Banh T. Yen C.L. Deficiency of MGAT2 increases energy expenditure without high-fat feeding and protects genetically obese mice from excessive weight gain.J. Lipid Res. 2011; 52: 1723-1732Abstract Full Text Full Text PDF PubMed Scopus (32) Google Scholar). mice were to and metabolic for and were fed for To whether a on by the weight for mouse on In and both with and without for weight Kozak L.P. with the of energy expenditure in expressing and obese 2010; PubMed Scopus Google Scholar, B. Identification of fat a of metabolic rate in 2010; PubMed Scopus Google on of fat a of metabolic rate in 2011; Scholar). triacylglycerol by on in the a Hepatic triacylglycerol of the of in PubMed Scopus Google Scholar). liver in were in and were in and by with the by to and were and a by Hepatic and were an of of in Biochem. PubMed Scopus Google Scholar). of liver in of of the with of The other for with in both were a The the the the and the the with a by data are for data in in which were to to of the were by the with and for weight the the in J. Scholar). weight and were by by test other were by by the protected To generate mice expressing MGAT2 in an intestine-specific we into from mice a transgene the cDNA of human MGAT2 to the of the villin gene which expression in intestinal by and L. of the villin gene expression in of the and of the intestine.J. Biol. Chem. 2002; Full Text Full Text PDF PubMed Scopus Google Scholar). with specific to human mouse MGAT2 and a we identified mice The of the transgene in the also with not These were with mice (Mogat2−/−) to generate of mice expressing MGAT2 in the intestine To the expression levels of human MGAT2 in the mice to of mouse MGAT2 in the mice, we a of to the identical mouse and human cDNA in the of mice, to and were for characterization in this expressed MGAT2 and of the levels in the intestine but not in other tissues, including the liver and fat and MGAT2 in Mogat2−/− mice levels of MGAT2 expression that of the were in the small intestine of and the these not levels of MGAT2 expression were in the of mice of levels found in the villin promoter increased expression in and mice which has been reported in other L. of the villin gene expression in of the and of the intestine.J. Biol. Chem. 2002; Full Text Full Text PDF PubMed Scopus Google Scholar, D. S. D. of the mouse villin gene that expression in and of small and Biol. Chem. Full Text Full Text PDF PubMed Scopus Google Scholar). In in acyltransferase Mogat2−/− mice MGAT activity of levels in both and small intestine. This activity from other enzymes MGAT activity, acyl acyltransferase C.L. M. Farese Jr, R.V. The triacylglycerol synthesis enzyme also catalyzes the synthesis of and Lipid Res. 46: Full Text Full Text PDF PubMed Scopus Google Scholar), which are highly expressed in the intestine. In contrast, mice of the MGAT activity in mice, a increase in MGAT activity in mice with mice in the intestine of in MGAT activity also in the intestine. These data indicate that the transgene expressed in and mice and that the expression MGAT2 activity in the intestine of Mogat2−/− mice. We examined whether expression of MGAT2 increases the of the intestine to and To of and we and fatty acids into that were in the and intestine. We the of dietary fat be from the intestine. The levels of by the of in lipid from the intestine with the levels of MGAT2 the levels were in by and the in Mogat2−/− mice in the intestine These levels were higher in the intestine, with the of the Mogat2−/− mice where were low in both In of mice, the of into In the intestine of mice, we found of triacylglycerol, with diacylglycerol, and the monoacylglycerol In Mogat2−/− mice, the of and triacylglycerol reduced with the role of intestinal MGAT2 in the of increased the esterification of monoacylglycerol into and in mice, the esterification partially restored to and of in the intestine, in mice, the levels of mice in both In contrast, the amounts of into phospholipids monoacylglycerol not with the expression levels of intestinal In the intestine, to levels of monoacylglycerol the of triacylglycerol with in the intestine in the levels of triacylglycerol to the levels of MGAT2 expression Mogat2−/− mice absorb normal quantities of dietary the rate of fat absorption in these mice is reduced with the entry of dietary fat into the circulation is (12Yen C.L. Cheong M.L. Grueter C. Zhou P. Moriwaki J. wong J.S. Hubbard B. Marmor S. Farese Jr, R.V. Deficiency of the intestinal enzyme acyl CoA:monoacylglycerol acyltransferase-2 protects mice from metabolic disorders induced by high-fat feeding.Nat. Med. 2009; 15: 442-446Crossref PubMed Scopus (133) Google Scholar). we examined whether expressing in the intestine increases the rate of fat absorption in Mogat2−/− mice. of mice were with a The dietary fat the circulation a reduced rate in Mogat2−/− mice with mice, In contrast, the increased in both and mice to the extent in mice that of intestinal MGAT activity low of the is sufficient to the rate of fat In the of the in found triacylglycerol Mogat2−/− mice exhibit increased energy expenditure, by in mice, even when fed a (13Nelson D.W. Gao Y. Spencer N.M. Banh T. Yen C.L. Deficiency of MGAT2 increases energy expenditure without high-fat feeding and protects genetically obese mice from excessive weight gain.J. Lipid Res. 2011; 52: 1723-1732Abstract Full Text Full Text PDF PubMed Scopus (32) Google Scholar). To determine whether intestinal MGAT2 is sufficient to the increases in energy expenditure, and mice were in metabolic and fed for of the of from fat. Mogat2−/− mice more mice the with and In contrast, both and mice levels of mice when fed the fat fed high-fat diet, both levels that were Mogat2−/− and mice, the with decreases to Mogat2−/− mice and increases to mice, not when the weight of of Mogat2−/− mice were to not on the the Mogat2−/− mice more In contrast, both and mice an that of were not from that of Mogat2−/− mice more fat in of mice the decreases in respiratory exchange ratio an increased of fatty the diet, the that dietary a energy when mice were and not the of the when mice were in the In contrast, Mogat2−/− mice with mice the when mice were and The in when mice were fed the high-fat and Interestingly, of both and mice that with Mogat2−/− mice, that in the of fat are not The amounts of decreased in mice when were fed more high-fat However, of the fat not We whether expressing MGAT2 in the intestine is sufficient in weight gain in response to high-fat feeding. mice weight upon high-fat feeding but not to the mice on of Mogat2−/− mice of high-fat feeding a mice. In contrast, and mice and which more Mogat2−/− mice but mice of mice of mice the of high-fat feeding. high-fat mice, but not Mogat2−/− mice, by increases in liver and triacylglycerol and mice an not of mice, but triacylglycerol were higher that of Mogat2−/− mice. In contrast, in levels not high-fat mice also a higher of levels the other of mice, were in levels with the that mice to with a of the in were and in mice in the other The the of mice that of Mogat2−/− mice, the not were in the response to and mice We reported that Mogat2−/− mice exhibit increased energy expenditure and are protected from obesity induced by the a role of the MGAT2 enzyme in the and storage of metabolic In this we that MGAT2 in the intestine regulates the and of monoacylglycerol and promotes assimilation of dietary fat into fat in mice. MGAT2 the and physiological in expressing human specifically in the intestine of Mogat2−/− mice, increased intestinal MGAT activity, restored fat absorption, and partially corrected energy high-fat both of mice that MGAT2 in the intestine more weight Mogat2−/− without the This that intestinal MGAT2 is to a to assimilation of dietary fat. However, these mice not gain weight the possibility that the low levels of MGAT2 expressed in other tissues may also contribute to enhancing metabolic efficiency. The of MGAT activity is in the absorption of dietary where MGAT catalyzes the of triacylglycerol (2Mansbach C.M. Siddiqi S.A. The biogenesis of chylomicrons.Annu. Rev. Physiol. 2010; 72: 315-333Crossref PubMed Scopus (142) Google Scholar). MGAT2 is the of MGAT activity in the intestine (8Yen C.L. Farese Jr, R.V. MGAT2, a monoacylglycerol acyltransferase expressed in the small intestine.J. Biol. Chem. 2003; 278: 18532-18537Abstract Full Text Full Text PDF PubMed Scopus (145) Google Scholar, C.L. Cheong M.L. Grueter C. Zhou P. Moriwaki J. wong J.S. Hubbard B. Marmor S. Farese Jr, R.V. Deficiency of the intestinal enzyme acyl CoA:monoacylglycerol acyltransferase-2 protects mice from metabolic disorders induced by high-fat feeding.Nat. Med. 2009; 15: 442-446Crossref PubMed Scopus (133) Google Scholar). MGAT activity in and the to monoacylglycerol into triacylglycerol were reduced in the intestine of Mogat2−/− mice. were restored to the levels of MGAT2 expression when MGAT2 in the intestine of and mice of the intestine that MGAT activity for triacylglycerol synthesis J.M. The of the and monoglyceride in the intestinal of 1967; PubMed Scopus Google Scholar). in the GPAT on the other is a precursor for both triacylglycerol and synthesis of Rev. Biochem. PubMed Scopus Google Scholar). Consistent with these we found that inactivating MGAT2 the amounts of monoacylglycerol into triacylglycerol In contrast, MGAT2 expression not the levels of in by the GPAT the from these not the is in with the that lipid enzymes with specific to lipid data suggest that MGAT2 the rate of monoacylglycerol by the intestine, the levels of MGAT2 expression determine the levels of from the in the intestine. into the intestinal these that the decreased lipid is a to the absence of MGAT2 in the a of systemic which has been reported in Mogat2−/− mice (12Yen C.L. Cheong M.L. Grueter C. Zhou P. Moriwaki J. wong J.S. Hubbard B. Marmor S. Farese Jr, R.V. Deficiency of the intestinal enzyme acyl CoA:monoacylglycerol acyltransferase-2 protects mice from metabolic disorders induced by high-fat feeding.Nat. Med. 2009; 15: 442-446Crossref PubMed Scopus (133) Google Scholar). In mice, we found more in the intestine, where MGAT2 expression is in the intestine The of the in the not In Mogat2−/− mice, the amounts of were low in both with more from the mice in the intestine. of MOGAT2 increased the monoacylglycerol and the levels of expression with the levels of the in both and mice. In contrast, the and of fatty acids were not and Mogat2−/− mice not with an GPAT pathway in these mice. The for monoacylglycerol in the intestine for with fatty has been the of monoacylglycerol is and is by excess fatty acids J. of monoacylglycerol and fatty by human intestinal J. Physiol. Physiol. PubMed Google Scholar). data suggest that MGAT2 may by to fatty acyl fatty Consistent with reduced monoacylglycerol and esterification in the intestine, of MGAT2 the entry of dietary fat into MGAT2 in the intestine corrected and mice of fat absorption to mice, in the levels of intestinal MGAT This that MGAT activity of levels in mice sufficient to fat MGAT activity in mice not a higher rate of fat absorption, other in the and of may to be whether MGAT2 regulates the of chylomicrons, which may in lipid and energy metabolism. The of intestinal MGAT2 in systemic energy balance by findings that expressing MOGAT2 in the intestine is sufficient to metabolic efficiency and energy balance in Mogat2−/− mice. MGAT2 in with mouse enzyme in out and physiological to for the mouse MGAT2 physiological and enhances metabolic efficiency in and mice a in energy expenditure and increases in weight gain in response to high-fat feeding with Mogat2−/− mice. However, these recoveries not the levels and to be incomplete. is that human MGAT2 cannot for the of mouse we cannot the possibility that the expression both and driven by the villin from expression of MGAT2 in of findings with we that the MGAT2 expressed in the tissues in metabolic efficiency. We that energy expenditure were more the when nutrients are through the in contrast, the in the the of fatty were more the when absorption of nutrients is and mice that with Mogat2−/− mice. This that have in with mice and that tissues may have energy metabolism Mogat2−/− mice, to metabolic The energy balance of Mogat2−/− mice are in to mice in of the enzymes the step of triacylglycerol synthesis C.L. Stone S.J. S. C. Farese Jr, R.V. enzymes and triacylglycerol Lipid Res. 49: Full Text Full Text PDF PubMed Scopus Google Scholar, S. S.J. S. C. of a gene encoding an acyl acyltransferase, a enzyme in triacylglycerol Natl. Acad. Sci. USA. PubMed Scopus Google S.J. Cases S. Chen B. J. Farese R.V. and of synthesis in mice lacking Genet. PubMed Scopus Google Scholar). associated with a in rate but normal of fat absorption S.J. Stone S.J. J.S. Jr, Farese Jr, R.V. is not essential for intestinal triacylglycerol absorption Biol. Chem. 2002; Full Text Full Text PDF PubMed Scopus Google Scholar), mice exhibit increased energy expenditure, impaired metabolic efficiency, and to are also protected from and other metabolic disorders to is highly expressed in the intestine and other tissues, including the adipose of intestinal the villin promoter in study the rate of fat absorption and to diet-induced and the role of intestinal lipid metabolism in systemic energy balance B. J. expression of acyl acyltransferase to diet-induced and obesity in Lipid Res. 2010; Full Text Full Text PDF PubMed Scopus Google Scholar). of have been to increases in triacylglycerol in both humans and on weight gain induced by high-fat feeding have been reported in rodents C. M. L. C. M. of for the from a 15: PubMed Scopus Google Scholar, J. Zhou Y. S. T. J. S. acyltransferase with small for the of metabolic Biol. Chem. 2011; Full Text Full Text PDF PubMed Scopus Google S. S. S. and by and Lipid Res. Full Text Full Text PDF PubMed Scopus Google Scholar). of the are for metabolic in humans to be determined. In this we that expressing human MGAT2 in the intestine of Mogat2−/− mice is sufficient to metabolic efficiency, that triacylglycerol metabolism in the intestine fat absorption and systemic energy balance and that the human enzyme may the These findings raise the of MGAT2 in the intestine an to In we found that intestinal MGAT activity partially metabolic efficiency and not in Mogat2−/− mice, the possibility that MGAT2 in other tissues may play a functional role in the and storage of energy The and for in and mouse with acyltransferase monoacylglycerol monoacylglycerol acyltransferase respiratory exchange ratio triacylglycerol
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