Degradation of collagen by a human granulocyte collagenolytic system.

Journal Article (Journal Article)

This report suggests a mechanism for collagen degradation mediated by human granulocytic leukocytes. A specific collagenase, which is extractable from human granulocytes, has been partially purified by DEAE chromatography. This collagenolytic enzyme is operative at physiological pH and is inhibited by EDTA, cysteine, and reduced glutathione but not by human serum. The enzyme cleaves the collagen molecule into two specific products, without loss of helical conformation. Electron micrographs of segment long spacing aggregates indicate that the cleavage occurs one-quarter of the length from the carboxy terminal end of the molecule. Experiments with crude extracts from granulocytes suggest that the specific products of granulocyte collagenase activity are then degraded by other proteases present in the human granulocyte.

Full Text

Duke Authors

Cited Authors

  • Lazarus, GS; Daniels, JR; Brown, RS; Bladen, HA; Fullmer, HM

Published Date

  • December 1, 1968

Published In

Volume / Issue

  • 47 / 12

Start / End Page

  • 2622 - 2629

PubMed ID

  • 4302177

Pubmed Central ID

  • PMC297433

International Standard Serial Number (ISSN)

  • 0021-9738

Digital Object Identifier (DOI)

  • 10.1172/JCI105945


  • eng

Conference Location

  • United States