Intracellular location of acetyltransferase in the remodeling pathway of PAF biosynthesis in undifferentiated human leukemic cells (HL-60).
In order to determine the site of PAF synthesis via the remodeling pathway in undifferentiated HL-60 cells, a subcellular fractionation procedure (Ribbes et al., 1985) was adapted to separate various membrane fractions and cellular organelles of HL-60 cells across a Percoll gradient. The profile of alkyllyso-GPC:acetyl-CoA acetyltransferase activity closely paralleled the subcellular distribution of the endoplasmic reticulum marker, NADH dehydrogenase. These data indicate the acetyltransferase in the remodeling pathway of PAF synthesis is located at the same cellular site as the acyltransferase(s) that catalyze the transfer of long-chain acyl moieties from acyl-CoAs to lyso-phospholipids. Also the acetyltransferase in undifferentiated HL-60 cells appears to have a similar intracellular distribution as reported for human neutrophils.
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Medical Sciences Division, Oak Ridge Associated Universities, TN 37831-0117.
Snyder
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D000123:Acetyltransferases / Q000378:metabolism*; D002454:Cell Differentiation; D004721:Endoplasmic Reticulum / Q000201:enzymology; D006801:Humans; D007938:Leukemia / Q000378:metabolism / Q000473:pathology; D009245:NADH Dehydrogenase / Q000378:metabolism; D010972:Platelet Activating Factor / Q000096:biosynthesis*; D014407:Tumor Cells, Cultured / Q000378:metabolism* / Q000473:pathology
D010972:Platelet Activating Factor; D009245:NADH Dehydrogenase; D000123:Acetyltransferases; C046035:1-alkylglycerophosphocholine acetyltransferase