THE EFFECT OF PEPTIDE DELETIONS ON THE GLYCOSYLATION OF MURINE IMMUNOGLOBULIN-M HEAVY-CHAINS

被引:2
作者
FINLEY, EM
REBBE, NF
HICKMAN, S
机构
[1] VET AFFAIRS MED CTR,RES SERV 151JC,915 N GRAND,ST LOUIS,MO 63106
[2] WASHINGTON UNIV,VET AFFAIRS MED CTR,MED SERV,JOHN COCHRAN DIV,ST LOUIS,MO 63106
关键词
D O I
10.1016/0003-9861(90)90507-U
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The glycosylation and processing of the asparagine-linked oligosaccharides at individual glycosylation sites on the μ-chain of murine immunoglobulin M were investigated using variant cell lines that synthesize and secrete IgM heavy chains with known peptide deletions. Normal murine IgM has five N-linked oligosaccharides in the constant region of each heavy or μ-chain. Each μ-chain has four complex-type oligosaccharides as well as a single high mannose-type oligosaccharide near the carboxyl terminus of the molecule. The peptide deletion of the Cμ1 constant region domain in the heavy chains synthesized by one variant cell line did not prevent subsequent glycosylation at more distal glycosylation sites. In fact, the presence of this deletion resulted in more complete glycosylation at the C-terminal glycosylation site. Evaluation of glycopeptides containing individual glycosylation sites by Concanavalin A-Sepharose indicated that this deletion had no significant effect on the processing of structures from high mannose-type to complex-type oligosaccharide chains. In contrast, a deletion of the C-terminal peptide region of the heavy chain of IgM synthesized by a second variant cell line resulted in intracellular processing to more highly branched oligosaccharide structures at several of the glycosylation sites not involved in the deletion. © 1990.
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页码:395 / 401
页数:7
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