PMID: 6066Jun 17, 1976

Phosphatidic acid phosphatase and phospholipdase A activities in plasma membranes from fusing muscle cells

Biochimica Et Biophysica Acta
C Kent, P R Vagelos

Abstract

Plasma membrane from fusing embryonic muscle cells were assayed for phospholipase A activity to determine if this enzyme plays a role in cell fusion. The membranes were assayed under a variety of conditions with phosphatidylcholine as the substrate and no phospholipase A activity was found. The plasma membranes did contain a phosphatidic acid phosphatase which was optimally active in the presence of Triton X-100 and glycerol. The enzyme activity was constant from pH 5.2 to 7.0, and did not require divalent cations. Over 97% of the phosphatidic acid phosphatase activity was in the particulate fraction. The subcellular distribution of the phosphatidic acid phosphatase was the same as the distributions of the plasma membrane markers, (Na+ + k+)-ATPase and the acetylcholine receptor, which indicates that this phosphatase is located exclusively in the plasma membranes. There was no detectable difference in the phosphatidic acid phosphatase activities of plasma membranes from fusing and non-fusing cells.

References

Jan 17, 1975·Nature·Q F AhkongJ A Lucy
Jul 7, 1965·Biochimica Et Biophysica Acta·B Sedgwick, G Hübscher
Nov 1, 1973·Proceedings of the National Academy of Sciences of the United States of America·S D SchimmelP R Vagelos
Aug 1, 1974·Proceedings of the National Academy of Sciences of the United States of America·J M Prives, B M Paterson
Aug 22, 1970·Nature·A R PooleJ A Lucy
Aug 1, 1961·Circulation·I R KONIGSBERG

Citations

May 1, 1981·The Histochemical Journal·J J TroutB A Schottelius
Jul 1, 1985·Developmental Biology·S J Kaufman, R F Foster

Related Concepts

DNA-dependent ATPase
Metazoa
kappa-Bungarotoxin
Calcium
Cell Fusion Procedure
Plasma Membrane
Chick Embryo
Enzyme Activation
Glycerin
Hydrogen-Ion Concentration

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