Protein Metabolism of Necrotic Wounds.
Abstract
The collagen losses in necrotic woulds are associated with an apparent collagenolysis due to the activation of a collagenolytic enzyme. This enzyme is normally complexed with a protein inhibitor which is more sensitive to tryptic digestion than is the collagenolytic enzyme itself. This enzyme releases a wide variety of molecular weight products from purified soluble native collagen ranging from 1,000 to 30,000 daltons in molecular weight. All of these products have been shown to be capable of aggregating platelets of both human and rats in vitro. This suggests that the breakdown products released during collagenolysis in vivo within the wound space can stimulate platelet aggregation and the chemotactic response of polymorphonuclear (PMN) leukocytes along with other more well established mediators, particularly, complement. The inhibition of the synthesis of collagenolytic activity by actidione, cycloheximide and actinomycin D suggests that peptide bond and messenger RNA synthesis is necessary and that in fact this is a de-repression of an operon being demonstrated for the first time in diploid human cells.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jun 22, 1971
- Accession Number
- AD0745003
Entities
People
- John C. Houck