Acyl-CoA:dihydroxyacetone phosphate acyltransferase in human skin fibroblasts: study of its properties using a new assay method.

Abstract

In relation to the finding that human skin fibroblasts are capable of de novo either phospholipid biosynthesis, we have studied the properties of acyl-CoA:dihydroxyacetone phosphate acyltransferase in fibroblast homogenates using a new assay method. The results indicate that the acylation of dihydroxyacetone phosphate shows an optimum at pH 5.5 with a broad shoulder of activity up to pH 6.4 and a decline in activity up to pH 8.2. At pH 5.5 the acyltransferase accepts dihydroxyacetone phosphate, but not glycerol 3-phosphate as a substrate. Furthermore, the transferase activity was found to be membrane-bound and inactivated by Triton X-100 at concentrations above 0.025% (w/v). Similar properties have been described for the enzyme as present in rat-liver and guinea-pig liver peroxisomes. These data, together with the finding that acyl-CoA:dihydroxyacetone phosphate acyltransferase is deficient in cultured skin fibroblasts from patients without peroxisomes (Zellweger syndrome), suggest that in cultured skin fibroblasts the enzyme is primarily located in peroxisomes.

• Authors: R B Schutgens, G J Romeyn, R Ofman, H van den Bosch, J M Tager, R J Wanders
• Journal: Biochimica et biophysica acta (Biochim Biophys Acta) Vol. 879 Issue 3 Pg. 286-91 (Dec 05 1986) ISSN: 0006-3002 [Print] Netherlands
• PMID: 3535897 (Publication Type: Journal Article)

Chemical References

• Carbon Radioisotopes
• Acyltransferases
• glycerone-phosphate O-acyltransferase

Topics

• Acyltransferases (metabolism)
• Carbon Radioisotopes
• Cells, Cultured
• Fibroblasts (enzymology)
• Humans
• Kinetics
• Radioisotope Dilution Technique
• Skin (enzymology)