Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Phospholipase D specific for the phosphatidylinositol anchor of cell-surface proteins is abundant in plasma

Journal Article · · Proc. Natl. Acad. Sci. U.S.A.; (United States)
An enzyme activity capable of degrading the glycosyl-phosphatidylinositol membrane anchor of cell-surface proteins has previously been reported in a number of mammalian tissues. The experiments reported here demonstrate that this anchor-degrading activity is also abundant in mammalian plasma. The activity was inhibited by EGTA or 1,10-phenanthroline. It was capable of removing the anchor from alkaline phosphatase, 5'-nucleotidase, and variant surface glycoprotein but had little or no activity toward phosphatidylinositol or phosphatidylcholine. Phosphatidic acid was the only /sup 3/H-labeled product when this enzyme hydrolyzed (/sup 3/H)myristate-labeled variant surface glycoprotein. It could be distinguished from the Ca/sup 2/=-dependent inositol phospholipid-specific phospholipase C activity in several rat tissues on the basis of its molecular size and its sensitivity to 1,10-phenanthroline. The data therefore suggest that this activity is due to a phospholipase D with specificity for glycosylphosphatidylinositol structures. Although the precise physiological function of this anchor-specific phospholipase D remains to be determined, these findings indicate that it could play an important role in regulating the expression and release of cell-surface proteins in vivo.
Research Organization:
Oklahoma Medical Research Foundation, Oklahoma City (USA)
OSTI ID:
6659453
Journal Information:
Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 85:4; ISSN PNASA
Country of Publication:
United States
Language:
English