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Biochem J. 1998 Aug 1;333 ( Pt 3):749-56.

Glycosylation pattern of human inter-alpha-inhibitor heavy chains.

Author information

1
Laboratoire de Biochimie, Faculté de Pharmacie, Université de Lille II, Avenue du Professeur Laguesse, B.P. 83, F-59006 Lille, France.

Abstract

Human inter-alpha-inhibitor (IalphaI) is a plasma serine-proteinase inhibitor. It consists of three polypeptide chains covalently linked by a glycosaminoglycan chain: a light chain named bikunin carrying the anti-proteinase activity and two heavy chains, H1 and H2, which exhibit specific properties, e.g. they interact with hyaluronan thus stabilizing the extracellular matrix. In this study, using matrix-assisted laser desorption ionization-time-of-flight MS and amino acid sequencing of tryptic peptides, we provide a detailed analysis of the glycosylation pattern of both heavy chains. H1 carries two complex-type N-glycans of predominantly biantennary structure linked to asparagine residues at positions 256 and 559 respectively. In contrast, the oligosaccharides attached to H2 are a complex-type N-glycan in the N-terminal region of the protein (Asn64) and three to four type-1 core-structure O-glycans mono- or di-sialylated, clustered in the C-terminal region. We propose that these O-glycans might function as a recognition signal for the H2 heavy chain. The biological implications of this hypothesis, notably for the biosynthetic pathway of IalphaI, are discussed.

PMID:
9677337
PMCID:
PMC1219641
DOI:
10.1042/bj3330749
[Indexed for MEDLINE]
Free PMC Article

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