Primary Structure and Functional Activity of a Phosphatidylinositol-Glycan-Specific Phospholipase D
1991; American Association for the Advancement of Science; Volume: 252; Issue: 5004 Linguagem: Inglês
10.1126/science.2017684
ISSN1095-9203
AutoresBernard J. Scallon, Wen-Jian Fung, T. Chris Tsang, Shirley Xin Li, Helen Kado‐Fong, Kuo‐Sen Huang, Jarema Kochan,
Tópico(s)Animal Genetics and Reproduction
ResumoA 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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