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Degradation of human collagen isoforms by Clostridium collagenase and the effects of degradation products on cell migration
Author(s) -
Shi Lei,
Ermis Ryan,
Garcia Anastacia,
Telgenhoff Dale,
Aust Duncan
Publication year - 2010
Publication title -
international wound journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.867
H-Index - 63
eISSN - 1742-481X
pISSN - 1742-4801
DOI - 10.1111/j.1742-481x.2010.00659.x
Subject(s) - collagenase , fibroblast , wound healing , cell migration , type i collagen , extracellular matrix , microbial collagenase , cell , cell culture , clostridium , in vitro , biochemistry , chemistry , microbiology and biotechnology , medicine , biology , immunology , pathology , enzyme , bacteria , genetics
Clostridium collagenase has been widely used in biomedical research to dissociate tissues and isolate cells; and, since 1965, as a therapeutic drug for the removal of necrotic wound tissues. Previous studies found that purified collagenase‐treated extracellular matrix stimulated cellular response to injury and increased cell proliferation and migration. This article presents an in vitro study investigating the digestive ability of Clostridium collagenase on human collagen types I, III, IV, V and VI. Our results showed that Clostridium collagenase displays proteolytic power to digest all these types of human collagen, except type VI. The degradation products derived were tested in cell migration assays using human keratinocytes (gold surface migration assay) and fibroblasts (chemotaxis cell migration assay). Clostridium collagenase itself and the degradation products of type I and III collagens showed an increase in keratinocyte and fibroblast migration, type IV‐induced fibroblast migration only, and the remainder showed no effects compared with the control. The data indicate that Clostridium collagenase can effectively digest collagen isoforms that are present in necrotic wound tissues and suggest that collagenase treatment provides several mechanisms to enhance cell migration: collagenase itself and collagen degradation products.

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