Role of N-linked oligosaccharides attached to human renin expressed in COS cells.
One or both of two putative N-glycosylation sites (at asparagine-5 and -75) of human renin was eliminated by amino acid replacement of the asparagine residue with an alanine residue using site-directed mutagenesis. The three glycosylation-deficient renins (Asn-5, Asn-75, Asn-5 and -75 mutants) were expressed in COS cells and secreted into the conditioned media. The secreted amounts of the three mutants were different from one another, although the mutant and wild-type renins had practically the same specific activity. An Asn-5 and -75 mutant which did not contain any glycosylation sites was unstable in the medium, suggesting that the N-linked oligosaccharides play an important role in stabilization of human renin.
Hori
H
H
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
Yoshino
T
T
Ishizuka
Y
Y
Yamauchi
T
T
Murakami
K
K
D000595:Amino Acid Sequence; D001483:Base Sequence; D002460:Cell Line; D003470:Culture Media; D004247:DNA / Q000235:genetics; D004591:Electrophoresis, Polyacrylamide Gel; D006031:Glycosylation; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009154:Mutation; D009844:Oligosaccharides / Q000378:metabolism*; D010957:Plasmids; D012083:Renin / Q000235:genetics / Q000378:metabolism*; D013329:Structure-Activity Relationship; D014162:Transfection
D003470:Culture Media; D009844:Oligosaccharides; D004247:DNA; D012083:Renin