Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0026764 (multiple myeloma)
 36,148 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Hybridoma cells were produced by fusing P3X63Ag8.653 mouse myeloma cells with spleen cells from BALB/c mice immunized with Japanese encephalitis (JE) virus, Nakayama-RFVL strain. The resulting 26 clones produced hemagglutination inhibition antibodies against the homologous strain. The hemagglutination inhibition reactivity of each clone was tested against six flaviviruses: JE, Murray Valley encephalitis (MVE), Egypt 101 strain of West Nile (WN), St. Louis encephalitis (SLE), Russian spring summer encephalitis, and dengue type 1. The 26 monoclonal antibodies fell into four groups: 14 JE species-specific antibodies, 6 antibodies reactive to JE and MVE viruses, 3 antibodies to three or four viruses in the JE-MVE-WN-SLE subgroup, and 3 antibodies to all six flaviviruses. Furthermore, antigenic comparison of 27 strains of JE virus was carried out by using five JE species-specific monoclonal antibodies. Of these, 24 strains were isolated in various parts of Japan, and 3 strains came from Southeast Asia. In reactivity, the 27 strains were classified into at least four antigenic groups. The results showed that the Nakayama-Yakken strain is a mutant strain which lacks the Nakayama strain-specific antigen and that the recently isolated strains are immunologically different from Nakayama and JaGAr 01 strains. One clone (NARMA 13) produced a JE species-specific antibody which showed almost the same titer against 26 JE virus strains, whereas one clone (NARMA 5) produced a Nakayama strain-specific antibody which reacted only to the Nakayama-RFVL and Nakayama-Yoken strains.
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PMID:Antigenic analysis of Japanese encephalitis virus by using monoclonal antibodies. 620 Apr 38

Macrophages have been obtained from the peritoneal cavities of C57BL/6 mice following treatment with C. parvum, MVE-2, mineral oil, or thioglycollate. Cell populations were primarily composed of mononuclear phagocytes as determined by a latex bead uptake assay. Macrophages obtained from C. parvum or MVE-2 were activated as judged by enhanced cytostatic activity against two tumor cell target lines. Thioglycollate-elicited macrophages demonstrated much lower cytostatic ability. Rats were immunized with activated MVE-2 macrophages. Hybridomas were prepared by fusion with a non-secreting myeloma cell line followed by cloning. Cell supernates were selected on the basis of binding to activated but not elicited macrophages. The monoclonal antibody produced has been characterized by flow cytometry. The antibody does not react with syngeneic erythrocytes, thymocytes, or spleen cells. Reaction with thioglycollate macrophages is very low. Alternatively, intense binding is found on activated macrophages. This antigen which accompanies macrophage activation for tumor cell cytostasis is designated as macrophage activation antigen-1 (MAA-1). Several important physiological changes accompany the process of macrophage activation. For example, activated macrophages demonstrate enhanced microbicidal, phagocytic, secretory, and tumoricidal activity (for reviews see refs. 1,2). Concommitant alterations in cell surface properties have been observed. These include: (a) changes in surface morphology and spreading (3-5), (b) altered lipid and protein content (6,7), (c) decreases in 5'-nucleotidase activity and alkaline phosphodiesterase (8), increases in leucine aminopeptidase (8), decreases in mannose receptors (11,12), and antigen F4/80 (11), (d) increases in Ia antigens (11,12), and (e) increased tumor cell binding (13). These structural and functional modifications indicate that activated macrophages represent a unique class of functionally differentiated cells (9). Antigenic modifications accompanying macrophage differentiation are of special interest. Markers for specific macrophage classes might be useful in defining differentiation pathways, dissecting type-specific functional activities such as tumor cytotoxicity, and providing a means to identify macrophage subsets in heterogeneous cell populations. In the present work we have taken the first step in this direction by defining a cell surface macrophage activation antigen.
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PMID:Characterization of a monoclonal antibody defining a macrophage activation-specific cell surface antigen. 674 39