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Clinical Chemistry 38: 2510-2516, 1992;
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Clinical Chemistry, Vol 38, 2510-2516, Copyright © 1992 by American Association for Clinical Chemistry

Placental alkaline phosphatase: a model for studying COOH-terminal processing of phosphatidylinositol-glycan-anchored membrane proteins

R Amthauer, K Kodukula and S Udenfriend
Department of Neurosciences, Roche Institute of Molecular Biology, Roche Research Center, Nutley, NJ 07110.

Placental alkaline phosphatase (PLAP) has been used as a model for studying the biosynthesis of the phosphatidylinositol-glycan (PI-G)- protein linkage in intact cells and in cell-free systems. However, for the study of processing in cell-free systems, a small protein devoid of glycosylation sites is preferable. A PLAP-derived cDNA was engineered that codes for a nascent protein (mini-PLAP) of 28 kDa in which the NH2- and COOH-termini are retained but most of the interior of PLAP is deleted. In vitro translation of mini-PLAP mRNA in the presence of rough microsomal membranes yields mature PI-G-tailed mini-PLAP. Processing of nascent mutant proteins occurs only when a small amino acid is located at the site of cleavage and PI-G attachment (omega site). Mutations adjacent and COOH-terminal to the omega site have revealed that the omega + 1 site is promiscuous in its requirements but that only glycine and alanine are effective at the omega + 2 site. Rough microsomal membranes from T cells deficient in PI-G biosynthesis do not support processing of mini-PLAP; addition of exogenous PI-G restores activity. Translocation of the proprotein, most likely requiring ATP and GTP, precedes COOH-terminal processing.


The following articles in journals at HighWire Press have cited this article:


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 J. Biol. Chem.Home page
G.ör. Sipos, A. Puoti, and A. Conzelmann
Biosynthesis of the Side Chain of Yeast Glycosylphosphatidylinositol Anchors Is Operated by Novel Mannosyltransferases Located in the Endoplasmic Reticulum and the Golgi Apparatus
J. Biol. Chem., August 25, 1995; 270(34): 19709 - 19715.
[Abstract] [Full Text] [PDF]


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Copyright © 1992 by the American Association for Clinical Chemistry.