Transactions of the New York Academy of SciencesVolume 41, Issue 1 Series II p. 173-182 Properties of Acyl Coenzyme A: 1-Acyl-sn-Glycerol 3-Phosphate Acyltransferase from Rat Liver Mitochondria and Microsomes† DIPAK HALDAR, DIPAK HALDAR Department of Biochemistry The Public Health Research Institute of the City of New York, Inc. New York, New York 10016 Present address: Department of Biological Sciences, St. John's University, Jamaica, New York 11439.Search for more papers by this authorHANNA CHROBOCZEK KELKER, HANNA CHROBOCZEK KELKER Department of Biochemistry The Public Health Research Institute of the City of New York, Inc. New York, New York 10016 Present address: Department of Microbiology, New York University Medical Center, New York, New York 10016.Search for more papers by this authorMAYNARD E. PULLMAN, MAYNARD E. PULLMAN Department of Biochemistry The Public Health Research Institute of the City of New York, Inc. New York, New York 10016Search for more papers by this author DIPAK HALDAR, DIPAK HALDAR Department of Biochemistry The Public Health Research Institute of the City of New York, Inc. New York, New York 10016 Present address: Department of Biological Sciences, St. John's University, Jamaica, New York 11439.Search for more papers by this authorHANNA CHROBOCZEK KELKER, HANNA CHROBOCZEK KELKER Department of Biochemistry The Public Health Research Institute of the City of New York, Inc. New York, New York 10016 Present address: Department of Microbiology, New York University Medical Center, New York, New York 10016.Search for more papers by this authorMAYNARD E. PULLMAN, MAYNARD E. PULLMAN Department of Biochemistry The Public Health Research Institute of the City of New York, Inc. New York, New York 10016Search for more papers by this author First published: August 1983 https://doi.org/10.1111/j.2164-0947.1983.tb02799.xCitations: 8 † This investigation was supported in part by Grant AM-08823 from the National Institute of Arthritis, Diabetes, Digestive and Kidney Diseases of the National Institutes of Health. AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat Citing Literature Volume41, Issue1 Series IIAugust 1983Pages 173-182 RelatedInformation

The properties of acyl-CoA:sn-glycerol-3-phosphate acyltransferase in mitochondrial and microsomal fractions from liver and other organs of rat, mouse, guinea pig, rabbit, and beef are described.In liver of all species, the specific activity of the mitochondrial and microsomal enzyme is similar, whereas in other organs the microsomal enzyme is at least 10 times more active.In all types of mitochondria the enzyme shows a strong preference for palmityl-CoA, is insensitive to N-ethylmaleimide, and produces monoacylglycerophosphate as a major product.Microsomal preparations, by contrast, catalyze the acylation of glycerophosphate with both palmityl-CoA and oleyl-CoA, are almost completely inhibited by N-ethylmaleimide, and produce diacylglycerophosphate as the chief reaction product.These criteria, as well as striking differences in response to acetone, are also used to characterize mitochondrial and microsomal associated activities in Ehrlich ascites tumor cells.The properties of the enzyme in the mitochondrial fraction of Ehrlich cells resemble those of its microsomal counterpart.Subcellular distribution studies, using marker enzymes, indicate that glycerophosphate acyltransferase activity in these cells is confined to the microsomes.Taken together, the results raise the possibility that the absence of the acyl-CoA-specific mitochondrial enzyme may have a bearing on the unusual positioning of saturated fatty acids found in certain phospholipids in these tumor cells.Additional experiments indicate that, regardless of whether palmityl-CoA or oleyl-CoA is used as acyl donor, 1-acyl-sn-glycerol 3-phosphate is the major, if not sole product of sn-glycerol a-phosphate acylation in rat liver mitochondria and microsomes as well as in Ehrlich tumor cell microsomes.

The Hippo pathway was initially discovered in Drosophila melanogaster as a key regulator of tissue growth. It is an evolutionarily conserved signaling cascade regulating numerous biological processes, including cell growth and fate decision, organ size ...Read More