title: Monoacylglycerol and diacylglycerol acyltransferases and the synthesis of neutral glycerides in Manduca sexta.
abstract: The insect fat body and the adipose tissue of vertebrates store fatty acids (FA) as triacylglycerols (TG). However, the fat body of most insects has the unique ability to rapidly produce and secrete large amounts of diacylglycerol (DG). Monoacylglycerol acyltransferase (MGAT), which catalyzes the synthesis of DG from MG, and a diacylglycerol acyltransferase (DGAT), which catalyzes the synthesis of TG from DG, are key enzymes in the metabolism of neutral glycerides. However, very little is known about these acyltransferases in insects. In the present study we have cloned two predicted MGATs and a DGAT from Manduca sexta and compared their sequences with predicted MGAT and DGAT homologs from a number of insect species. The comparison suggested that insects may only have a single DGAT gene, DGAT1. The apparent absence of a DGAT2 gene in insects would represent a major difference with vertebrates, which contain DGAT1 and DGAT2 genes. Insects seem to have a single MGAT gene which is similar to the MGAT2 of vertebrates. A number of conserved phosphorylation sites of potential physiological significance were identified among insect proteins and among insect and vertebrate proteins. DGAT1 and MGAT are expressed in fat body, midgut and ovaries. The relative rates of utilization of FAs for the synthesis of DG and TG correlated with the relative expression levels of MGAT and DGAT suggesting that regulation of the expression levels of these acyltransferases could be determining whether the fat body secretes DG or stores fatty acids as TG. The expression patterns of the acyltransferases suggest a role of the monoacylglycerol pathway in the production and mobilization of DG in M. sexta fat body.
authors.affiliation: Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA. Electronic address: jose.soulages@okstate.edu.
authors.forename: Jose L
authors.initials: JL
authors.lastname: Soulages
authors.affiliation: Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.
authors.forename: Zengying
authors.initials: Z
authors.lastname: Wu
authors.affiliation: Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.
authors.forename: Sarah J
authors.initials: SJ
authors.lastname: Firdaus
authors.affiliation: Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.
authors.forename: Ramamurthy
authors.initials: R
authors.lastname: Mahalingam
authors.affiliation: Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA.
authors.forename: Estela L
authors.initials: EL
authors.lastname: Arrese
mesh_terms: D000217:Acyltransferases / Q000235:genetics* / Q000378:metabolism; D000818:Animals; D051048:Diacylglycerol O-Acyltransferase / Q000235:genetics* / Q000378:metabolism; D004075:Diglycerides / Q000096:biosynthesis*; D005216:Fat Body / Q000378:metabolism; D005260:Female; D041981:Gastrointestinal Tract / Q000378:metabolism; D005786:Gene Expression Regulation; D008297:Male; D018402:Manduca / Q000235:genetics / Q000378:metabolism*; D050178:Monoglycerides / Q000096:biosynthesis*; D010053:Ovary / Q000378:metabolism; D014280:Triglycerides / Q000096:biosynthesis*
chemical_list: D004075:Diglycerides; D050178:Monoglycerides; D014280:Triglycerides; D000217:Acyltransferases; D051048:Diacylglycerol O-Acyltransferase; C021802:2-acylglycerol O-acyltransferase