Primary structure and functional activity of a phosphatidylinositol-glycan-specific phospholipase D.
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.
Scallon
B J
BJ
Department of Molecular/Cellular Biology and Biochemistry, Hoffmann-La Roche, Inc., Nutley, NJ 07110.
Fung
W J
WJ
Tsang
T C
TC
Li
S
S
Kado-Fong
H
H
Huang
K S
KS
Kochan
J P
JP
D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D002460:Cell Line; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D015870:Gene Expression; D017261:Glycosylphosphatidylinositols; D006801:Humans; D006868:Hydrolysis; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry; D010716:Phosphatidylinositols / Q000378:metabolism; D010739:Phospholipase D / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011134:Polysaccharides / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid; D014162:Transfection; D014357:Trypsin
D017261:Glycosylphosphatidylinositols; D010446:Peptide Fragments; D010716:Phosphatidylinositols; D011134:Polysaccharides; D004247:DNA; D010739:Phospholipase D; C065017:glycoprotein phospholipase D; D014357:Trypsin