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Purification of a procollagenase-activator present in medium of cultured guinea pig carrageenin granuloma.

Abstract
Activation of procollagenase constitutes a crucial event in collagenolytic activity regulation. In this study we have purified by DEAE-cellulose, Ultrogel AcA-44, and zinc chelate sepharose chromatographies, a procollagenase-activator from the culture medium of the guinea pig carrageenin granuloma model. On SDS-PAGE, the activator migrates as a principal band of Mr approximately 44,000. The molecule activates procollagenase from human lung fibroblasts in a concentration dependent manner and an enhancement of collagenase activity of trypsin-treated crude culture medium was observed. A loss of about 50% of its activity occurs after heating. In addition, this activator degrades gelatin and casein. All these data suggest that this procollagenase-activator might be stromelysin. The activator was found in both phases of the granuloma, at 7 days when collagen is actively deposited and an important proportion of the collagenolytic activity remains in latent form; and at 14 days, when this enzymatic activity is fully expressed.
AuthorsA Pardo, R Ramirez, L Gutierrez-Kobeh, F Mendoza, E Bauer, M Selman
JournalConnective tissue research (Connect Tissue Res) Vol. 26 Issue 4 Pg. 259-69 ( 1991) ISSN: 0300-8207 [Print] England
PMID1660801 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Enzyme Precursors
  • Collagen
  • Collagenases
  • Metalloendopeptidases
  • procollagenase
  • Matrix Metalloproteinase 3
  • Microbial Collagenase
  • Zinc
Topics
  • Animals
  • Chromatography, Affinity
  • Chromatography, Ion Exchange
  • Collagen (metabolism)
  • Collagenases
  • Enzyme Activation
  • Enzyme Precursors (metabolism)
  • Granuloma (chemically induced, enzymology)
  • Guinea Pigs
  • Matrix Metalloproteinase 3
  • Metalloendopeptidases (isolation & purification)
  • Microbial Collagenase (metabolism)
  • Skin (enzymology)
  • Zinc

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