Literature DB >> 2017684

Primary structure and functional activity of a phosphatidylinositol-glycan-specific phospholipase D.

B J Scallon1, W J Fung, T C Tsang, S Li, H Kado-Fong, K S Huang, J P Kochan.   

Abstract

A phosphatidylinositol-glycan-specific phospholipase D (PI-G PLD) that specifically hydrolyzes the inositol phosphate linkage in proteins anchored by phosphatidylinositol-glycans (PI-Gs) has recently been purified from human and bovine sera. The primary structure of bovine PI-G PLD has now been determined and the functional activity of the enzyme has been studied. Expression of PI-G PLD complementary DNA in COS cells produced a protein that specifically hydrolyzed the inositol phosphate linkage of the PI-G anchor. Cotransfection of PI-G PLD with a PI-G-anchored protein resulted in the secretion of the PI-G-anchored protein. The results suggest that the expression of PI-G PLD may influence the expression and location of PI-G-anchored proteins.

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Year:  1991        PMID： 2017684     DOI： 10.1126/science.2017684

Source DB:  PubMed          Journal:  Science        ISSN： 0036-8075            Impact factor:   47.728


  31 in total

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Authors: 
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Journal:  Biochem J       Date:  2002-01-01       Impact factor: 3.857

8.  Effects of membrane cholesterol depletion and GPI-anchored protein reduction on osteoblastic mechanotransduction.

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9.  Phospholipases of mineralization competent cells and matrix vesicles: roles in physiological and pathological mineralizations.

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10.  Augmentation of carcinoembryonic antigen release from intact, viable tumor cells by a factor in human serum.

Authors:  T J Yeatman; C Duan; W Mao; R C Karl; J Y Djeu
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