hydroxylysine and Dupuytren-Contracture

In inflammatory granuloma, synovial sclerosis or inflammation and in Dupuytren's contracture, the neocollagen contains chains and/or transverse links that are characteristic of rapidly growing immature tissues. In arthrosis, a conversion of collagen synthesis towards a cutaneous type may occur. The destruction of cartilage in rheumatoid arthritis is brought about by a specific collagenase that originates from the inflamed synovial membrane. Finally, certain forms of osteoporosis may be due to alterations of the osseous collagen which impair the mechanism of calcification.

Topics: Animals; Arthritis, Rheumatoid; Bone Diseases; Cartilage, Articular; Collagen; Collagen Diseases; Dupuytren Contracture; Fibroblasts; Granulation Tissue; Granuloma; Humans; Hydroxylysine; Microbial Collagenase; Osteitis Deformans; Osteoarthritis; Osteoporosis; Protein Conformation; Rheumatic Diseases; Sclerosis; Synovial Membrane; Synovitis

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.

Topics: Amino Acids; Collagen; Dipeptides; Dupuytren Contracture; Hand; Humans; Hydroxylysine; Male; Polymorphism, Genetic; Solubility; Tendons

The palmar fascial tissues of more than 400 patients with Dupuytren's disease were studied biochemically and compared with normal tissue obtained from more than 100 patients who were undergoing hand surgery for other reasons. No alterations of the molecular structure or the state of macromolecular aggregation of the collagen in Dupuytren's disease were detected by wide or low-angle x-ray diffraction studies or by transmission electron microscopy. Major biochemical changes in the palmar fascia affected by Dupuytren's disease included increased collagen and hexosamine contents and the presence of galactosamine in the most severely involved tissue. Type-III collagen, which is virtually absent from normal adult palmar fascia, was abundant in the tissue of patients with Dupuytren's disease. Post-translational modifications included a very elevated hydroxylysine content, an increase in the total number of reducible cross-links, and the appearance of hydroxylysinohydroxynorleucine (virtually absent from normal palmar fascia) as the major reducible cross-link. Even palmar fascia from patients with Dupuytren's disease that appeared grossly and histologically normal showed the same biochemical changes, albeit to a lesser extent. All of these biochemical changes are similar to those that occur during the active stages of connective-tissue wound repair. This includes the rapid synthesis and turnover of collagen which leads to newly synthesized, immature collagen being more abundant in the involved tissue than in normal tissue. There is no evidence that the gross, macroscopic contracture of the palmar fascia in Dupuytren's disease is due to shortening, plication, or contraction of the collagen fibrils or fibers present in the tissue at the onset of the disease or synthesized during its development. Instead, we propose that the gross contracture (shortening) of the palmar fascia in Dupuytren's disease is due to an active cellular process that progressively draws the distal extremities of the affected tissue closer together at the same time that the original tissue is being replaced. The result of these two processes is simply a shorter, smaller piece of tissue fabric containing collagen molecules, fibrils, and fibers of normal length and organization, but with pretranslational and posttranslational modifications similar to those observed in collagens during the active stages of connective-tissue repair in general.

Topics: Adult; Aged; Collagen; Dupuytren Contracture; Fascia; Female; Hand; Hexosamines; Histocytochemistry; Humans; Hydroxylysine; Hydroxyproline; Male; Middle Aged; Solubility; X-Ray Diffraction