Degradation of articular cartilage by copper and hydrogen peroxide.
When porcine articular cartilage particles were incubated in the presence of Cu2+ and H2O2 at pH 7.4, solubilization of collagen and proteoglycan was observed. Both agents were necessary and the rate of solubilization was concentration dependent. Other transition metal ions showed much lower catalytic activity. The solubilized polypeptides were polydispersed in size and the hydroxyproline content of the larger fragments was 13% by weight. Further incubation of the released material with Cu2+ and H2O2 resulted in further degradation and partial destruction of hydroxyproline residues. Competitive studies with scavengers of OH X and 1O2 as well as the effect of D2O excluded these two species as major mediators in this system.
D000818:Animals; D002358:Cartilage, Articular / Q000187:drug effects* / Q000378:metabolism; D002417:Cattle; D002614:Chelating Agents / Q000494:pharmacology; D003300:Copper / Q000494:pharmacology*; D006595:Hexosamines / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D008670:Metals / Q000494:pharmacology; D008970:Molecular Weight; D010455:Peptides / Q000378:metabolism; D011509:Proteoglycans / Q000378:metabolism
D002614:Chelating Agents; D006595:Hexosamines; D008670:Metals; D010455:Peptides; D011509:Proteoglycans; D003300:Copper; D006861:Hydrogen Peroxide