Secretion and localization of cathepsin D in synovial tissues removed from rheumatoid and traumatized joints. An immunohistochemical study.
The proteinase cathepsin D which degrades proteoglycan was never demonstrated in extracellular sites in tissues from patients with traumatized meniscoid cartilage, either before or after culture with an antiserum to human cathepsin D. In contrast, in synovia (but not usually cartilage) from the knees of 6 of 11 rheumatoid patients, extracellular cathepsin D was commonly detected by culturing tissues with an antiserum to this enzyme.
D000818:Animals; D001172:Arthritis, Rheumatoid / Q000201:enzymology*; D001345:Autoradiography; D002358:Cartilage, Articular / Q000201:enzymology / Q000473:pathology; D002403:Cathepsins / Q000378:metabolism*; D006801:Humans; D007596:Joints / Q000293:injuries*; D010539:Permeability; D013462:Sulfur Radioisotopes; D013582:Synovial Fluid / Q000201:enzymology; D013583:Synovial Membrane / Q000473:pathology; D000070600:Tibial Meniscus Injuries
D013462:Sulfur Radioisotopes; D002403:Cathepsins