Abstract
Monoacylglycerol O-acyltransferase 2 (MOGAT2) plays critical roles in lipid homeostasis. We reported a cDNA designed BmMOGAT2 encoding an MOGAT2 homologue cloned from the fat body of the silkworm Bombyx mori, by using conserved domain homology search method. The resultant BmMOGAT2 was translated to a protein encoding 352 amino acids with a theoretical isoelectric point of 9.04 and a molecular weight of 39,944.48 Da. Homology analysis revealed that BmMOGAT2 exhibits higher similarity on the amino acid level to those of other species already reported; 48% identity with Homo sapiens, 46% with Mus musculus, 50% with Danio rerio, and 42% with Drosophila melanogaster. The expression of BmMOGAT2 was detected in all tissues tested with 2-fold higher expression in the post-silk gland, as compared to others, and stronger expression of the larval fat body at 1st instar, as compared with other stages. The BmMOGAT2 is a predicted endoplasmic reticulum (ER) transmembrane protein with two ER transmembrane domains; BmMOGAT2 gene expression increases in response to ER stress-inducible drugs. To our knowledge, this is the first report of Bombyx mori MOGAT2 cDNA, BmMOGAT2, and its associated molecular characterization.
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Abbreviations
- BmMOGAT2:
-
Bombyx mori MOGAT2 cDNA
- DAG:
-
diacylglycerol
- DD-PCR:
-
differential display PCR
- ER:
-
endoplasmic reticulum
- MAG:
-
monoacylglycerol
- MGAT:
-
O-acyltransferase
- MOGAT2:
-
monoacylglycerol Oacyltransferase2
- RT-PCR:
-
reverse transcriptional PCR
- TG:
-
triacylglycerol
- VLDL:
-
very low-density lipoprotein
References
Cao J., Hawkins E., Brozinick J., Liu X., Zhang H., Burn P. & Shi Y. 2004. A predominant role of acyl-CoA:monoacylglycerol acyltransferase-2 in dietary fat absorption implicated by tissue distribution, subcellular localization, and up-regulation by high fat diet. J. Biol. Chem. 279: 18878–18886.
Cao J., Lockwood J., Burn P. & Shi Y. 2003. Cloning and functional characterization of a mouse intestinal acyl-CoA:monoacylglycerol acyltransferase, MGAT2. J. Biol. Chem. 278: 13860–13866.
Cheng D.L., Nelson T.C., Chen J., Walker S.G., Wardwell-Swanson J., Meegalla R., Taub R., Billheimer J.T., Ramaker M. & Feder J.N. 2003. Identification of acyl coenzyme A:monoacylglycerol acyltransferase 3, an intestinal specific enzyme implicated in dietary fat absorption. J. Biol. Chem. 278: 13611–13614.
Costa-Leonardo A.M., Laranjo L.T., Janei V. & Haifig I. 2013. The fat body of termites: functions and stored materials. J. Insect Physiol. 59: 577–587.
Gu Z.Y., Li C.F., Wang B.B., Xu K.Z., Ni M., Zhang H., Shen W.D. & Li B. 2015. Differentially expressed genes in the fat body of Bombyx mori in response to phoxim insecticide. Pestic. Biochem. Physiol. 117: 47–53.
Jacome-Sosa M.M. & Parks E.J. 2014. Fatty acid sources and their fluxes as they contribute to plasma triglyceride concentrations and fatty liver in humans. Curr. Opin. Lipidol. 25: 213–220.
Lockwood J.F., Cao J., Burn P. & Shi Y. 2003. Human intestinal monoacylglycerol acyltransferase: differential features in tissue expression and activity. Am. J. Physiol. Endocrinol. Metab. 285: E927–E937.
Matsumoto Y., Sumiya E., Sugita T. & Sekimizu K. 2011. An invertebrate hyperglycemic model for the identification of antidiabetic drugs. PLoS One 6: e18292.
Ogata N., Yokoyama T. & Iwabuchi K. 2012. Transcriptome responses of insect fat body cells to tissue culture environment. PLoS One 7: e34940.
Schachter H. 2010. Mgat1-dependent N-glycans are essential for the normal development of both vertebrate and invertebrate metazoans. Semin. Cell Dev. Biol. 21: 609–615.
Shi Y.L. & Cheng D. 2009. Beyond triglyceride synthesis: the dynamic functional roles of MGAT and DGAT enzymes in energy metabolism. Am. J. Physiol. Endocrinol. Metab. 297: E10-E18.
Turner T.L., Levine M.T., Eckert M.L. & Begun D.J. 2008. Genomic analysis of adaptive differentiation in Drosophila melanogaster. Genetics 179: 455–473.
Wang Y., Schachter H. & Marth J.D. 2002. Mice with a homozygous deletion of the Mgat2 gene encoding UDP-Nacetylglucosamine: a-6-D-mannoside ß1,2-N-acetylglucosaminyltransferase II: a model for congenital disorder of glycosylation type IIa. Biochim. Biophys. Acta 1573: 301–311.
Wang Y.C., Lin C., Chuang M.T., Hsieh W.P., Lan C.Y., Chuang Y.J. & Chen B.S. 2013. Interspecies protein-protein interaction network construction for characterization of hostpathogen interactions: a Candida albicans-zebrafish interaction study. BMC Syst. Biol. 7: 79.
Winter A.L., van Eckeveld M., Bininda-Emonds O.R., Habermann F.A. & Fries R. 2003. Genomic organization of the DGAT2/MOGAT gene family in cattle (Bos taurus) and other mammals. Cytogenet. Genome Res. 102: 42–47.
Wu L. & Parhofer K.G. 2014. Diabetic dyslipidemia. Metabolism 63: 1469–1479.
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Shin, H., Kwon, K., Hong, S.M. et al. Cloning of monoacylglycerol o-acyltransferase 2 cDNA from a silkworm, Bombyx mori. Biologia 71, 695–700 (2016). https://doi.org/10.1515/biolog-2016-0090
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DOI: https://doi.org/10.1515/biolog-2016-0090