Production of chemotactic peptides by neutrophil degradation of heparin cofactor II.

Journal Article (Journal Article)

This study investigated the reaction of heparin cofactor II (HCII) with stimulated polymorphonuclear leukocytes (PMN). We have expanded upon previous studies showing that HCII can be degraded by stimulated PMN (Sie, P., Dupouy, D., Dol, F., and Boneu, B., Thromb. Res. 47, 657-664, 1987), and that chemotactic activity is produced when HCII is partially proteolyzed with purified leukocyte elastase or cathepsin G (Hoffman, M., Pratt, C.W., Brown, R.L., and Church, F.C., Blood, 73, 1682-1695, 1989). We found that HCII was proteolyzed by stimulated PMN, generating peptides with chemotactic activity. Both proteolysis and generation of chemotactic activity were inhibited by a specific leukocyte elastase inhibitor and by more general proteinase inhibitors. Leukocyte elastase activity was lost upon addition of either inhibitor. Heparin and dermatan sulfate altered the pattern of proteolysis. Our results suggest that HCII may be involved not only in functions related to thrombin inhibition but also in regulating acute inflammation.

Full Text

Duke Authors

Cited Authors

  • Corbin, LW; Church, FC; Hoffman, M

Published Date

  • January 1, 1990

Published In

Volume / Issue

  • 57 / 1

Start / End Page

  • 77 - 85

PubMed ID

  • 2300926

International Standard Serial Number (ISSN)

  • 0049-3848

Digital Object Identifier (DOI)

  • 10.1016/0049-3848(90)90196-j


  • eng

Conference Location

  • United States