| pubmed-article:8037839 | pubmed:abstractText | Five monoclonal antibodies (HuMC1, HuMC2, HuMC3, HuMC4 and HuMC5) raised against intact human articular chondrocytes were tested with chondrocyte samples from arthritic and non-arthritic patients by surface immunofluorescence and by immunoperoxidase labeling of fixed cells. All acetone-fixed samples reacted strongly with the monoclonal antibodies but some variation in the percentages of intact chondrocytes positive by immunofluorescence was noted. Under culturing conditions which induced de-differentiation, epitopes recognized by HuMC1, HuMC3 and HuMC4 disappeared with time in culture. In contrast, reactivities to HuMC2 and HuMC5 either persisted or increased as the culture became more fibroblastic and these antibodies bound to antigens on human fibroblast cell lines. HuMC1, HuMC3 and HuMC4 reacted with purified adult and fetal proteoglycan. HuMC2 and HuMC5 exhibited only slight or no reactivity to either proteoglycan. All five monoclonal antibodies reacted with chondrocytes in frozen articular cartilage but HuMC2 and HuMC5 failed to react to chondrocytes in paraffin-embedded cartilage sections. Only HuMC1, HuMC3 and HuMC4 recognized matrix components in both frozen and paraffin-embedded cartilage. When tested against 29 different non-cartilaginous tissues, each of the monoclonal antibodies had distinctive reactivity patterns, suggesting that each reacted to different epitopes. HuMC3 reacted with neurons in the cerebral cortex and cerebellum, indicating that it may recognize epitopes shared on the S-100 protein. HuMC1 showed the greatest specificity for chondrosarcomas. These antibodies are useful for identifying differentiated chondrocytes, providing information on the distribution of chondrocyte antigens shared by other human tissue, assessing the extent of chondrocyte heterogeneity in a population and aiding in the classification of chondrosarcomas. | lld:pubmed |
