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.
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Authors | A Pardo, R Ramirez, L Gutierrez-Kobeh, F Mendoza, E Bauer, M Selman |
Journal | Connective tissue research
(Connect Tissue Res)
Vol. 26
Issue 4
Pg. 259-69
( 1991)
ISSN: 0300-8207 [Print] England |
PMID | 1660801
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Enzyme Precursors
- Collagen
- Collagenases
- Metalloendopeptidases
- procollagenase
- Matrix Metalloproteinase 3
- Microbial Collagenase
- Zinc
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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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