Biomedical subjects
Publications and source records attributed to E Gurr.
Connective tissue from specimens of Dupuytren's disease showed higher contents and altered distribution patterns of glycosaminoglycans. Increasing chondroitin sulphate concentrations as well as increasing proportions of 6-sulphated galactosamines were found to be the characteristic changes.
A method has been established for analysing the glycosaminoglycan distribution pattern in small specimens from intervertebral discs and other connective tissue materials. The procedure is based on the consecutive digestion by the specific enzymes hyaluronate lyase, chondroitin sulfate lyase AC and ABC. The quantitative determination of the resulting disaccharides was achieved by high performance liquid chromatography with a detection limit of less than 0.1 nmmol. The undigested heparan- and keratansulfate were separated from each other by thin layer chromatography and quantified by the colorimetric determination of uronic acid and hexosamine, respectively. Correlation of distribution patterns obtained by this method with those obtained by ion exchange chromatography (Dowex 1 X 2) is not possible without the additional enzymatic characterization of the ion exchange chromatographic fractions. The method was applied to 9 discs of one human spine (anulus fibrosus and nucleus pulposus separately) with the following results: 1) there were no systematic changes to be seen in the distribution patterns with respect to the location of the discs in the spine, and 2) the galactosaminoglycan/keratansulfate ratio was higher in the anulus fibrosus than in the nucleus pulposus.
Rheumatic joint destruction usually starts with the destabilisation of cartilage. Lysosomal elastase is a candidate effector of this process, since this enzyme is found at the site of cartilage erosion by rheumatoid synovial tissue. In order to prove this hypothesis we assessed the mechanical stability of cartilage during treatment by this enzyme in vitro. An indentation apparatus was used for this purpose and biochemical as well as microscopic techniques were used to supplement the results thus obtained. Our findings show that elastase irreversibly impairs the stability of cartilage by lysis of matrix proteoglycans without the help of additive enzymes. Collagen fragmentation played no significant role during elastase-induced destabilisation, while specific collagenase attacked the collagen network within the matrix only subsequent to the removal of proteoglycans. These findings suggest that elastase is a leading enzyme during proteolytic cartilage degradation. In addition polysulfonated glycosaminoglycan was found to reduce the mechanical effect of elastase on normal cartilage. It is therefore concluded that local inhibition of elastase promises therapeutic benefit during rheumatic cartilage degradation. Upon treatment of cartilage with elastase we observed this enzyme not only within the matrix under destruction but also bound to chondrocytes. These findings support the hypothesis that elastase plays a role on the matrix not only by direct degradation, but also by an indirect effect mediated through living chondrocytes.
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