Glycerolipid synthetic capacity of rat liver peroxisomes.
Investigations on rat liver peroxisomal glycerolipid synthetic capability were performed. Highly purified peroxisomal preparations contained dihydroxyacetone-phosphate acyltransferase, acyldihydroxyacetone-phosphate reductase, and fatty acid-CoA ligase activities. Glycerol-3-phosphate acyltransferase, lysophosphatidic acid acyltransferase, phosphatidic acid phosphatase, diacylglycerol acyltransferase, diacylglycerol cholinephosphotransferase, diacylglycerol ethanolaminephosphotransferase and ethanol acyltransferase activities were low in activity or not detected. These results suggest that the peroxisomes are specialized to contribute to the synthesis of ether-linked glycerolipids. If peroxisomes contribute towards the synthesis of non-ether-linked glycerolipids (i.e., ester-linked) then translocation of acyl glycerophosphatide (acyl dihydroxyacetone phosphatide) from peroxisomes to endoplasmic reticulum would be expected to occur.
D000217:Acyltransferases / Q000378:metabolism; D000818:Animals; D005260:Female; D005989:Glycerides / Q000096:biosynthesis*; D008099:Liver / Q000201:enzymology*; D008830:Microbodies / Q000201:enzymology*; D008862:Microsomes, Liver / Q000201:enzymology; D010770:Phosphotransferases / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains
D005989:Glycerides; D000217:Acyltransferases; D010770:Phosphotransferases