N-linked glycosylation of the C5a receptor.
The recent cloning of the cDNA encoding the human C5a receptor reveals a single potential site for N-linked glycosylation. Previous studies have suggested the presence of at least one carbohydrate moiety in the C5a receptor. Enzymatic digestion with Endoglycosidase F confirmed this presence and a point mutation at the predicted site of glycosylation was sufficient to lower the apparent molecular weight of the receptor as determined by SDS-PAGE. Removal of the carbohydrate moiety failed to abolish expression of the receptor and brought about only a slight reduction in the dissociation constant of the C5a receptor suggesting that the role of glycosylation in the binding of C5a by its receptor is limited.
Pease
J E
JE
Krebs Institute, Department of Molecular Biology and Biotechnology, University of Sheffield, U.K.
Barker
M D
MD
D000818:Animals; D001483:Base Sequence; D016466:CHO Cells; D015936:Complement C5a / Q000378:metabolism*; D006224:Cricetinae; D003412:Cricetulus; D018076:DNA, Complementary / Q000302:isolation & purification; D006031:Glycosylation; D006801:Humans; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011233:Precipitin Tests; D044087:Receptor, Anaphylatoxin C5a; D011951:Receptors, Complement / Q000737:chemistry* / Q000378:metabolism; D014170:Transformation, Genetic
D018076:DNA, Complementary; D044087:Receptor, Anaphylatoxin C5a; D011951:Receptors, Complement; D015936:Complement C5a; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase