CD89: the human myeloid IgA Fc receptor.
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Experimental and clinical studies have been carried out to investigate the application of a number of monoclonal antibodies which recognise human lymphocytes in clinical organ transplantation. Where possible, preliminary studies have been carried out using a primate renal allograft model before proceeding to clinical pilot studies. The Campath-1 antigen (CDW52) appears to be a good target for antilymphocytic therapy; a powerful immunosuppressive effect has been demonstrated using both IgM and IgG2b antibodies which recognise this antigen. An IgG2b antibody which recognises the IL-2 receptor was shown to be immunosuppressive in the primate model but clinical studies have, as yet not demonstrated a significant, beneficial effect in preventing rejection. Patients who receive antilymphocyte monoclonal antibodies require monitoring of the expression of the target antigen, the level of free antibody in serum and the development of an antiglobulin response. The current issues in the use of antilymphocyte monoclonal antibodies in clinical immunosuppression include identification of the optimum target, interaction of the antibody with recipient effector mechanisms and methods to avoid or suppress the antiglobulin response.
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Experimental and clinical studies have been carried out to investigate the application of a number of monoclonal antibodies which recognise human lymphocytes in clinical organ transplantation. Where possible, preliminary studies have been carried out using a primate renal allograft model before proceeding to clinical pilot studies. The Campath-1 antigen (CDW52) appears to be a good target for antilymphocytic therapy; a powerful immunosuppressive effect has been demonstrated using both IgM and IgG2b antibodies which recognise this antigen. An IgG2b antibody which recognises the IL-2 receptor was shown to be immunosuppressive in the primate model but clinical studies have, as yet not demonstrated a significant, beneficial effect in preventing rejection. Patients who receive antilymphocyte monoclonal antibodies require monitoring of the expression of the target antigen, the level of free antibody in serum and the development of an antiglobulin response. The current issues in the use of antilymphocyte monoclonal antibodies in clinical immunosuppression include identification of the optimum target, interaction of the antibody with recipient effector mechanisms and methods to avoid or suppress the antiglobulin response.
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Antigenic determinants of the human transferrin molecule on the sublobe and lobe levels were localized for 7 monoclonal antibodies. Antibodies used have different effects on the interaction of the transferrin with its receptor. It was concluded that transferrin-receptor recognition was determined by NH2-lobe, the N2-sublobe playing major part. Dimerization of the transferrin molecules in solution was detected. Using the panel of monoclonal antibodies it was shown that dimerization accomplished by means of the COOH-lobes of transferrin molecules, the sites of interaction of the NH2-lobe with receptor being exposed. A model of the transferrin - receptor complex is proposed.
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We describe a family of six rat monoclonal antibodies which appear to recognize identical or closely related determinants present on virtually all mature human lymphocytes and monocytes, but absent from other blood cells including myeloid and erythroid colony-forming cells. Four IgM antibodies and one IgG2a fix human complement; one IgG2c antibody does so only poorly. All of the antibodies react with lymphocytes from baboons, rhesus and cynomolgus monkeys. However, in all baboons and rhesus monkeys tested, and some cynomolgus monkeys, they also recognize red cells. Nevertheless, in other cynomolgus monkeys reactivity is with lymphocytes only, so these animals will be suitable models for testing the effects of the antibodies in vivo. The antibodies described here could be useful for in vitro removal of lymphocytes from allogeneic marrow grafts (to prevent graft-versus-host disease) or malignant lymphoid cells from autologous grafts (for treatment of leukaemia) and may also find application as general immunosuppressants and for immunotherapy of leukaemia.
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The culture supernates from a variety of mouse hybridomas which were known to secrete antibodies to antigens unrelated to steroid hormone receptors were examined for routine use as experimental controls for monoclonal anti-oestrogen receptor (ER) antibodies. During this process, we made an observation which is important for all investigations on monoclonal anti-receptor antibodies. Our results indicated that the phenol red dye present in these hybridoma culture fluids by binding to the immunoglobulins (Ig) secreted by the hybridoma cells, may impart to the Ig-dye complex, a capacity to interact with ER/progesterone receptors(PR) which are present in the cytosols or in the sections of ER+ tumors. The Ig-dye may thus mimic anti-receptor antibody activity. Growth media containing phenol red and Ig-free bovine calf serum supplement or culture fluids from a non-Ig secreting hybridoma failed to show similar binding to ER+ tissues. This observation documents the need for Ig-dye complex formation to obtain such ER-Ig interaction. Complete dialysis of phenol red from the Ig positive supernates removed the observed interference of the dye. In this report we describe the nature of this interference and the results obtained before and after the removal of the dye from Ig+ culture fluids. In addition, we suggest some remedial measures that should be considered, while screening and testing the specificity of any hybridoma culture product for anti-receptor antibody activity (particularly, anti-ER or anti-PR antibodies).
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The effect of monoclonal antibodies to the human transferrin receptor on transferrin and iron uptake by rat and rabbit reticulocytes has been examined.The antibodies used were as follows: T5811.4,B3/25.4,42/6.3, T56114.3.1, and 43/31.The effects were the same, irrespective of the antibody.Transferrin and iron uptake were stimulated in both rat and rabbit reticulocytes.The stimulation was not due to an increase in the number or affinity of the receptors, but rather to an increase in the rate of turnover of the receptors.Electron microscopy suggested that the antibody acted by facilitating the formation of coated pits containing the transferrin-receptor complex.
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Do monoclonal antibodies Tü15 and Tü67 detect heterogeneity of human transferrin receptor molecules?
The possible molecular heterogeneity of human transferrin receptors was analyzed using two murine monoclonal antibodies, Tü15 and Tü67. Both reagents precipitated from lysates of 125I-labeled HL-60 cells a major component of 88 kDa which could be identified as the transferrin receptor by comparison with the proteins detected by monoclonal antibody OKT9. Although sequential immunoprecipitations appeared to demonstrate molecular heterogeneity of transferrin receptors, since the Tü15-reactive species were fully included in the Tü67-positive population, but not vice versa, the possible association of Tü15-reactive molecules with transferrin receptor is also discussed.
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