Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.4.24.3 (collagenase)
 18,340 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A series of hydrolytic enzymes were compared with lysolecithin, glycerol monooleate, and inactivated Sendai virus for their ability to bring about the fusion of several human and mouse lymphoid cell lines. The agents were tried alone and in various combinations, and a variety of incubation conditions were tested to determine those optimal for fusion. Sendai virus was found to produce the best results with the mouse lymphoid cells; lysolecithin plus glycerol monooleate was slightly superior with the human lymphoid cells. A mixture of hyaluronidase plus collagenase produced low (2 to 6%), but significant, fusion of the human lymphoid cells; both the human and mouse lymphoid cell lines were found to contain relatively high amounts of prolyl hydroxylase, the enzyme which forms collagen from protocollagen. The maximum fusion obtained with the human cells was 16%; with a mouse plasmacytoma line, the maximum was 7.5%; and with a mouse leukemic line derived from L5178Y, the maximum was 60%.
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PMID:Optimal conditions for the fusion of lymphoid cell lines. 24 Jul 76

Using monoclonal antibodies, we examined the display of rabbit Ia by articular chondrocytes. We found that 29 to 46% of chondrocytes displayed Ia antigen compared with 46 to 60% of spleen cells. Ia antigen expression was not likely to be the result of enzyme treatment. To investigate antigen presenting activity of enzyme dissociated normal articular chondrocytes, adult rabbits were immunized in the front foot pads with ovalbumin (OVA) in complete Freund's adjuvant. Four to six weeks later, draining popliteal lymph node cells (LNC) were obtained. Articular chondrocytes were obtained by overnight collagenase, DNase, and hyaluronidase digestion of cartilage from both ends of femurs and proximal end of tibias. Antigen-presenting cells from spleen were used as positive controls. LNC and nylon wool-purified T cells were cultured with OVA pulsed and mitomycin C-treated chondrocytes or spleen cells, and lymphocyte proliferation was measured by 3H-TdR uptake. Both chondrocytes and spleen cells showed antigen presenting activity, and stimulation of lymphocyte proliferation was inhibited by murine monoclonal anti-rabbit Ia antibody (2C4), whereas control plasmacytoma cell supernatants had no effect. When T cells were purified first by Sephadex G-10 and later by nylon wool columns, these cells were dependent on antigen-presenting cells for immunogen (OVA)-induced lymphocyte proliferation. Again, chondrocytes under these strict experimental conditions presented antigen to T cells. Chondrocytes also stimulated autologous and allogeneic normal lymphocytes. Thus, normal chondrocytes have Ia antigens on their surface and can function as antigen-presenting cells. These results are significant for the understanding of local cellular interaction in the pathogenesis of rheumatoid arthritis.
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PMID:Class II histocompatibility antigen-mediated immunologic function of normal articular chondrocytes. 293 76

Hepatocyte-stimulating factor, interferon-beta 2, B-cell stimulation factor 2, and hybridoma/plasmacytoma growth factor are identical proteins presently referred to as interleukin 6 (IL-6). Through the use of synthetic oligonucleotide technology, we have constructed a biologically active recombinant IL-6 (rIL-6) gene based on the sequence of a human IL-6 cDNA. The synthetic gene encodes a cysteine-free, bioengineered rIL-6 protein that is expressed at high levels in Escherichia coli as a tripartite fusion protein. Cleavage of the fusion protein with collagenase releases a 23-kDa rIL-6 protein that can be easily purified to homogeneity. We show that the rIL-6 protein displays a range of biological activities similar to those of natural human IL-6, as demonstrated by its ability to (i) protect cells from viral infection, (ii) stimulate the synthesis of fibrinogen in rat FAZA 967 cells, and (iii) induce the terminal differentiation of B cells, resulting in elevated secretion of immunoglobulin.
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PMID:High-level expression of a bioengineered, cysteine-free hepatocyte-stimulating factor (interleukin 6)-like protein. 305 47