A heparin-binding synthetic peptide of heparin/heparan sulfate-interacting protein modulates blood coagulation activities

Shouchun Liu, Fanyu Zhou, Magnus Höök, Daniel D. Carson

Research output: Contribution to journalArticle

63 Scopus citations

Abstract

We have previously identified and characterized a heparin-binding cell surface protein (heparin/heparan sulfate-interacting protein, or HIP) present on epithelial and endothelial cells. A synthetic peptide mimicking a heparin- binding domain of HIP is now shown to hind a small subset of heparin molecules with high affinity and, therefore, presumably recognizes a specific structural motif in the heparin molecule. Further analyses revealed that the heparin molecules exhibiting a high affinity for the HIP peptide also show an extremely high affinity for antithrombin III (AT-III), a cofactor required for heparin's anticoagulant activity. The HIP peptide was shown to compete with AT-III for binding to heparin and to neutralize the auticoagulant activity of heparin in blood plasma assays. Furthermore, the heparin subfraction that binds to the HIP peptide with high affinity exhibits an extremely high anticoagulant activity. We conclude that although the HIP peptide shows no sequence similarity with AT-III, the two proteins recognize the same or similar structural motifs in heparin.

Original languageEnglish (US)
Pages (from-to)1739-1744
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume94
Issue number5
DOIs
StatePublished - Mar 4 1997

ASJC Scopus subject areas

  • General

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