Abstract
Fluid obtained from chronic and acute wounds were examined for the presence of fibronectin, alpha 1-antitrypsin, and proteinases capable of degrading both proteins. Immunoblot analysis of fluids from ten chronic wounds revealed that fibronectin and alpha 1-antitrypsin were degraded in nine of ten samples. In contrast, both fibronectin and alpha 1-antitrypsin were intact in acute wound fluids. The degradation of the inhibitor and fibronectin occurred in the same wound fluids, and these two events correlated perfectly. Chronic or acute wound fluid proteins were coupled to benzamidine Sepharose 6B beads and incubated with fibronectin or alpha 1-antitrypsin. Chronic wound fluid proteins degraded fibronectin in the presence of ethylenediaminetetraacetate, leupeptin, cystatin, and pepstatin but not in the presence of phenylmethylsulfonyl fluoride. Acute wound fluids and normal human serum did not contain enzymes capable of degrading fibronectin. These data suggest that serine proteinases are responsible for fibronectin degradation in chronic wound fluids. Chronic wound fluids that contained degraded alpha 1-antitrypsin also contain proteinases capable of degrading alpha 1-antitrypsin from human serum. Acute wound fluids and normal human serum did not contain enzymes capable of degrading alpha 1-antitrypsin. The inhibitor from acute wound fluids bound to one of its targets, trypsin. In contrast, the fragment(s) of alpha 1-antitrypsin from chronic wound fluids did not bind trypsin. Chronic wounds associated with degraded fibronectin and the inhibitor contained ten- to forty-fold more elastase activity than acute wounds. The degradation of fibronectin by chronic wound fluid enzymes was inhibited by alpha 1-antitrypsin in a dose-dependent manner. Collectively, these results demonstrate that there are enzymes in chronic wounds that perturb the function of alpha 1-antitrypsin and allow fibronectin degradation by uninhibited serine proteinases.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.