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Science 2 October 1987:
Vol. 238. no. 4823, pp. 81 - 84
DOI: 10.1126/science.2443973
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Articles

Science, Vol 238, Issue 4823, 81-84
Copyright © 1987 by American Association for the Advancement of Science

articles

A glycan-phosphatidylinositol-specific phospholipase D in human serum

MA Davitz, D Hereld, S Shak, J Krakow, PT Englund, and V Nussenzweig

Department of Pathology, New York University School of Medicine, NY 10016.

A group of proteins anchored to the cell by phosphatidylinositol (PI) has recently been identified. The significance of this new class of membrane anchor is unknown; one possibility is that it facilitates release of the molecule by phospholipases. In fact, phospholipase C enzymes specific for the complex carboxyl-terminal glycolipids of these proteins have been isolated from African trypanosomes and from hepatocyte plasma membranes. This study reports the discovery of a glycan-PI-specific phospholipase D in human serum that cleaves both the membrane form of the variant surface glycoprotein of African trypanosomes and its glycolipid precursor, but not phosphatidylethanolamine, phosphatidylcholine, or phosphatidylinositol. Decay-accelerating factor, another PI-anchored molecule, is also cleaved by the enzyme and converted from a hydrophobic to a soluble protein. The enzyme is Ca2+-dependent, heat labile, and not affected by the inhibitor of serine proteases, phenylmethylsulfonylfluoride. Its function is not known, but the present findings indicate that it participates in the metabolism of glycolipid-anchored membrane proteins.


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