A glycan-phosphatidylinositol-specific phospholipase D in human serum

Michael A. Davitz, Dale Hereld, Steve Shak, Jessica Krakow, Paul T. Englund, Victor Nussenzweig

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)81-84
Number of pages4
JournalScience
Volume238
Issue number4823
DOIs
StatePublished - Jan 1 1987

ASJC Scopus subject areas

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    Davitz, M. A., Hereld, D., Shak, S., Krakow, J., Englund, P. T., & Nussenzweig, V. (1987). A glycan-phosphatidylinositol-specific phospholipase D in human serum. Science, 238(4823), 81-84. https://doi.org/10.1126/science.2443973