Heparin cofactor II-proteinase reaction products exhibit neutrophil chemoattractant activity.

Published

Journal Article

The physiologic function of the plasma glycoprotein heparin cofactor II (HCII) is not well understood. An in vivo role for thrombin (IIa) inhibition by HCII in the presence of certain glycosaminoglycans (dermatan sulfate and heparin) can be proposed. Many proteins, such as complement components, can be proteolyzed to generate secondary bioactive molecules. HCII is a substrate for the human neutrophil (PMN) proteinases cathepsin G (CG) and elastase (LE). We found that degradation of HCII by CG or LE generated products with potent PMN chemotactic activity, which did not stimulate the PMN oxidative burst. Our results suggest that HCII may be a physiologic regulator of the acute inflammatory response.

Full Text

Duke Authors

Cited Authors

  • Hoffman, M; Pratt, CW; Brown, RL; Church, FC

Published Date

  • May 1, 1989

Published In

Volume / Issue

  • 73 / 6

Start / End Page

  • 1682 - 1685

PubMed ID

  • 2713501

Pubmed Central ID

  • 2713501

International Standard Serial Number (ISSN)

  • 0006-4971

Language

  • eng

Conference Location

  • United States