Degradation of soluble collagen by ozone or hydroxyl radicals.
Collagen exposed to ozone or hydroxyl radicals was degraded in a time- and dose-dependent manner. This degradation was inhibited by free radical scavengers. Furthermore, lower levels of these oxidants did not degrade the molecule, but caused it to become susceptible to proteolytic degradation. We suggest an alternative mechanism by which oxygen-derived free radicals participate in the destruction of extracellular matrix observed during acute lung injury by oxidant gas, in addition to the commonly accepted proteinase-antiproteinase theory of lung injury.
D000818:Animals; D002642:Chick Embryo; D003094:Collagen / Q000378:metabolism*; D004305:Dose-Response Relationship, Drug; D004591:Electrophoresis, Polyacrylamide Gel; D005609:Free Radicals; D006878:Hydroxides / Q000494:pharmacology*; D017665:Hydroxyl Radical; D010126:Ozone / Q000494:pharmacology*; D010446:Peptide Fragments / Q000378:metabolism; D010447:Peptide Hydrolases / Q000494:pharmacology; D011347:Procollagen / Q000378:metabolism
D005609:Free Radicals; D006878:Hydroxides; D010446:Peptide Fragments; D011347:Procollagen; D017665:Hydroxyl Radical; D010126:Ozone; D003094:Collagen; D010447:Peptide Hydrolases