Format

Send to

Choose Destination
Glycobiology. 1994 Apr;4(2):221-5.

Human protein C inhibits selectin-mediated cell adhesion: role of unique fucosylated oligosaccharide.

Author information

1
Cardiovascular Research, Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, IN 46285-1543.

Abstract

The human anticoagulant factor, Protein C, is a plasma glycoprotein that has reported anti-ischaemic and anti-inflammatory properties. To explore potential mechanisms for these reported activities, we examined the effect of Protein C on the process of cell adhesion to vascular endothelial cells, which plays a critical role during inflammatory responses. We show that both human plasma-derived and human cell-produced recombinant Protein C inhibit E-selectin-mediated cell adhesion. This effect was not mediated through the serine protease activity of Protein C, but through its carbohydrates. Using oligosaccharides isolated from human cell-produced Protein C, we have defined a polylactosamine structural determinant that inhibits adhesion. This uncharged determinant appears to be a more potent ligand for E-selectin than the sialylated Lewis X antigen. Our data suggest a potential mechanism for the reported anti-inflammatory effects of Protein C and describe a new ligand for selectin-mediated adhesion.

PMID:
7519910
DOI:
10.1093/glycob/4.2.221
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Silverchair Information Systems
Loading ...
Support Center