The trimannosyl cores of N-glycans are important for the procoagulant protease-inhibitory activity of urinary protein C inhibitor.

Abstract:

:We investigated the relationship between the procoagulant protease-inhibitory activity and the N-glycan structures in urinary protein C inhibitor (uPCI) by sequential exoglycosidase digestions based on the N-glycan structures elucidated in this report. uPCI was glycosylated on the three potential N-glycosylation sites, asparagines 230, 243 and 319 (N230, N243 and N319) in the molecule and had four biantennary complex type sugar chains. The inhibitory activities of uPCI toward thrombin and plasma kallikrein were little changed by the sequential removal of N-acetylneuraminic acid and galactose residues from the termini and N-acetylglucosamine residues from the branches of the N-glycans. However, the inhibitory activities were markedly decreased by further removing alpha-mannose residues from the trimannosyl cores of the N-glycans. These results suggest that the trimannosyl cores of N-glycans are important for uPCI to inhibit the procoagulant protease.

journal_name

Thromb Res

journal_title

Thrombosis research

authors

Izutani W,Fujita M,Nishizawa K,Koga J

doi

10.1016/s0049-3848(01)00342-5

subject

Has Abstract

pub_date

2001-10-01 00:00:00

pages

65-74

issue

1

eissn

0049-3848

issn

1879-2472

pii

S0049-3848(01)00342-5

journal_volume

104

pub_type

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