Biochemical studies on the collagen of the palmar aponeurosis affected with Dupuytren's disease.

The palmar aponeurosis of patients affected with Dupuytren's disease was examined for collagen characteristics with regard to extractability, polymorphism, and posttranslational modifications, and the results were compared with those from normal subjects. The increased proportion of type III collagen relative to type I collagen in the affected tissue confirmed the previous findings in this disease. A slight but significant increase in a ratio of glucosylgalactosylhydroxylysine to galactosylhydroxylysine in the Dupuytren's tissue may be interpreted by the increase in the content of type III collagen. The affected tissue contained increased amounts of dihydroxylysinonorleucine as the reducible cross-link of collagen. These data support the view that Dupuytren's tissue contains collagen resembling that in granulation and embryonic tissues. Pyridinoline was shown to occur in normal and affected aponeurosis. No change in its content suggests that this cross-link is not involved in the pathogenesis of contracture in this disease.