Syndecan-4 as antithrombin receptor of human neutrophils.

Abstract:

:Antithrombin inhibits chemokine-induced migration of neutrophils by activating heparan sulfate proteoglycan-dependent signaling. Mechanisms of antithrombin's effects on neutrophils were, therefore, studied by testing function and expression of heparan sulfate proteoglycans in RT-PCR or flow cytometry and cell migration assays, respectively. In vitro effects of antithrombin on human neutrophil migration in modified Boyden chambers were abolished by pretreating cells with heparinase-1, chondroitinase, sodium chlorate, and anti-syndecan-4 antibodies. Expression of syndecan-4 mRNA and protein in neutrophils was demonstrated in RT-PCR and anti-syndecan-4 immunoreactivity assay, respectively. In the presence of pentasaccharide, antithrombin lost its activity on the cells. Data suggest that antithrombin regulates neutrophil migration via effects of its heparin-binding site on cell surface syndecan-4.

authors

Kaneider NC,Egger P,Dunzendorfer S,Wiedermann CJ

doi

10.1006/bbrc.2001.5534

subject

Has Abstract

pub_date

2001-09-14 00:00:00

pages

42-6

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(01)95534-2

journal_volume

287

pub_type

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