Subcellular localization of phospholipids and enzymes involved in PAF-acether metabolism

Journal of Cellular Biochemistry
M RecordH Chap

Abstract

The biosynthesis of platelet-activating factor (PAF-acether or 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine) through the remodeling pathway was investigated at the subcellular level in two different cell lines. In human neutrophils, plasma membrane was isolated not only from granules, but also from internal membranes related to endoplasmic reticulum. Interestingly, the latter exhibited enhanced acetyltransferase upon neutrophil stimulation with ionophore A23187. A similar study was undertaken on the tumor strain Krebs-II cells. The enzyme acetyltransferase was found to be located only on an endoplasmic reticulum subfraction, whereas most alkylacyl-GPC, the source of PAF-precursor alkyl-lyso-GPC, was located in the plasma membrane inner leaflet. The topographical separation of enzyme and precursor emphasizes the central role of the intracellular phospholipase A2 in providing lyso-PAF to the acetyltransferase to form PAF-acether.

References

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Citations

Dec 1, 1991·Lipids·E Ninio, F Joly
Aug 4, 1999·Molecular and Cellular Endocrinology·A M StrandH S Hansen
Jul 21, 2001·The Biochemical Journal·R J RaggersG van Meer
Aug 1, 1991·Annals of Neurology·P J LindsbergG Feuerstein
Jan 5, 1996·Biochimica Et Biophysica Acta·F H ChiltonJ D Winkler

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