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)

To determine whether the ligand-binding site of the BALB/c myeloma protein 315 is essential for the anti-idiotypic response in syngeneic animals, 17 BALB/c mice were immunized with M315 that had been affinity-labeled with bromo-acetyl-DNP-L-lysine (BADL). Essentially all the active sites of M315 were blocked by the affinity label. Fourteen mice produced antibodies that reacted with an idiotypic determinant localized in the Fv fragment of M315, but this idiotype was not part of the DNP-lysine-binding site, and it was absent from L315 and H315 chains. Two groups of BALB/c mice were immunized with nonaffinity-labeled M315, to determine whether the same idiotype was recognized with this immunogen. All animals in the group that received the most prolonged immunization produced antibodies that could be divided in two populations: about 75% were directed against the site-associated idiotype, and the rest reacted with the nonsite idiotype. The other group produced antibodies exclusively specific for the site. Thus, the site-associated idiotype of M315 is not essential for the antibody response of BALB/c mice against M315, and M315 carries at least two different idiotypes that can be recognized by B cells of syngeneic animals.
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PMID:Production of BALB/c anti-idiotypic antibodies against the BALB/c myeloma protein 315 does not require an intact ligand-binding site. 6 35

Normal adult BALB/c mice are virtually unresponsive to the idiotype of myeloma protein T15 when immunized with purified T15. However, antibodies to the T15 idiotype can be elicited by T15 in BALB/c mice that are reared in a germ-free environment or injected as newborns with an alloantiserum to the idiotype. Some germ-free and neonatally suppressed mice also produce helper cells (presumably T helpers) that enhance B-cell production of anti-DNP antibodies in response to DNP-T15. Taken together with previous studies, the present results mean that so far there are no exceptions to the rule that BALB/c mice have B and T cells that can respond to idiotypes of myeloma proteins of BALB/c origin. There appears to be a reciprocal relation between the natural prevalence of an immunoglobulin's idiotype and its immunogenicity in isologous individuals. The findings support proposals for an immune network of idiotypes and anti-idiotypes. Besides binding one or more extrinsic antigens, it is likely that each immunoglobulin also binds the idiotype of some other immunoglobulin. An immune network therefore implies multispecificity of antibodies.
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PMID:Immune responses of BALB/c mice to the idiotype of T15 and of other myeloma proteins of BALB/c origin: implications for an immune network and antibody multispecificity. 7 Mar 7

The idiotype-specific myeloma transplantation resistance induced in BALB/c mice by immunization with the DNP-binding IgAlambda2 protein produced by plasmacytoma MOPC-315 is ablated by post-immunization thymectomy. Sham-thymectomy has no effect. The ablative effect of thymectomy is observed is observed in mice challenged subcutaneously with MOPC-315 cells either 3 days after thymectomy, or after a rest period of 44 days after thymectomy. These observations suggest that short-lived, thymic-dependent suppressive factors may play a role in the idiotype-specific myeloma graft resistance.
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PMID:Idiotype-specific transplantation resistance to MOPC-315: abrogation by post-immunization thymectomy. 7 76

Normal BALB/c spleen cells are unresponsive in vitro to the phosphorylcholine (PC) determinant in the presence of anti-idiotype antibodies specific for the TEPC-15 myeloma protein (T15) which carries an idiotypic determinant indistinguishable from that of most anti-PC antibodies in BALB/c mice. The possibility that idiotype-specific suppressor cells may be generated during the culture period was examined by coculturing the cells with untreated syngeneic spleen cells. Cells that had been preincubated with anti-T15 idiotype (anti-T15id) antibodies and a PC-containing antigen, R36a for 3 d, were capable of specifically suppressing the anti-PC response of fresh normal spleen cells, indicating that idiotype-specific suppressor cells were generated during the culture period. The presence of specific antigen also appeared to be necessary because anti-T15id antibodies and a control antigen, DNP-Lys-Ficoll, were not capable of generating such suppressor cells. Suppressor cells were induced only in the population of spleen cells nonadherent to nylon wool and the suppressive activity was abrogated by treatment with anti-Thy 1.2 serum and complement. These results indicate that anti-idiotype antibodies and specific antigen can generate idiotype-specific suppressor T cells in vitro. These in vitro results may reflect in vivo mechanisms of idiotype suppression.
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PMID:Mechanisms of idiotype suppression. I. In vitro generation of idiotype-specific suppressor T cells by anti-idiotype antibodies and specific antigen. 8 88

The structure of the combining site of the DNP binding IgA mouse myeloma protein MOPC 315 has been determined by a combination of high resolution nuclear magnetic resonance, electron spin resonance, model building and chemical modifications. This approach yields that general dimensions of the site, its polarity and asymmetry features, the assignment of the DNP-contact residues and their three-dimensional coordinates.
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PMID:Structure of an antibody combining site by magnetic resonance. 19 May 43

Small unilamellar lipid vesicles bearing the DNP-hapten on their surfaces and containing the water-soluble fluorescent dye carboxyfluorescein were formed by sonication. These vesicles were incubated with cells from the murine myeloma tumor MOPC 315, which secrete and also bear on the cell surface an immunoglobulin with affinity for the nitrophenyl hapten. At 0 degrees C the cells bound an average of several thousand vesicles at saturation. This binding was specific for the nitrophenyl hapten on the vesicle since it was abolished by an excess of soluble nitrophenyl derivative, by omission of the hapten from the vesicle, or by substitution for MOPC 315 of a tumor lacking receptors for the nitrophenyl hapten. Specific binding of vesicles was greater when cells were incubated at 37 degrees C. The study suggests that ligand-bearing vesicles can be a useful marker for cell surface immunoglobulin. However, in spite of the ability to "target" vesicles to cell surface determinants, binding did not result in increased delivery of vesicle contents to the cytoplasm.
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PMID:Binding of antigen-bearing fluorescent liposomes to the murine myeloma tumor MOPC 315. 36 42

Six hundred and twelve mouse plasmacytomas were screened for hapten binding by using eleven different bacteriophage-hapten conjugates (phage T4 conjugated with haptens NP, NIP, DIP, DNP,BOC-ABA-Tyr, ABA-NP, ABA-MIP, ABS-HOP, PAB-HOP, penicillin G, cloxacillin). Fifteen ascites fluids (2.4%) inactivated at least one of the phage conjugates at a high dilution indicating binding. The specificity of these reactions was studied by titrating one ascites fluid with phage conjugates carring unrelated haptens, and by inhibiting the phage inactivation with free haptens. Of the 15 myeloma proteins, 10 had high titers (at least 30 times higher than the ascites fluid background) with the NIP-cap phage or the NP-cap phage or both. Four had high titers with the DNP-cap phage and one with the ABA-MIP phage. Thirteen of the 15 myeloma proteins were IgA, one was IgM and one IgG2b.
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PMID:A search for hapten-binding mouse plasmacytoma proteins. 43 27

Hosts of plasma cell tumors have a depressed primary antibody response. We have investigated the ability of cell homogenates and culture fluids from short-term cultures of spleen cells and tumor cells of mice bearing the MOPC-315 plasmacytoma to suppress the in vivo primary antibody response to sheep red blood cells. The homogenates and culture fluids of both MOPC-315 spleen cells and tumor cells suppress the antibody response in a dose-dependent manner. Culture fluids of spleen cells from tumor-bearing mice contain a 10,000- to 20,000-dalton immunosuppressive factor. Culture fluids of non-adherent tumor cells contain a high m.w. suppressor. Injection of the high m.w. tumor suppressive factor into normal mice induces the expression or appearance of host cells that secrete the 10,000- to 20,000-dalton immunosuppressor. The tumor suppressive factor, but not the spleen factor, causes an alteration of lymphocyte membranes such that the anti-DNP activity of the MOPC-315 myeloma protein can be detected on the circulating lymphocytes of injected mice.
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PMID:Myeloma-induced immunosuppression: a multistep mechanism. 70 1

We have devised a rapid method for obtaining large amounts of J chain from IgA in the ascitic fluid of mice bearing the MOPC 315 tumor. The J chain was released by reduction from the MOPC 315 IgA adsorbed onto a DNP-lysyl-Sepharose column, and was further purified by DEAE Sephadex chromatography. The mouse J chain was characterized as to its electrophoretic mobility, amino acid composition, apparent size, presence in different immunoglobulin classes, and reactivity with an antiserum containing anti-J chain activity. Variant cell lines have been selected from the IgA-producing mouse myeloma cell line MOPC 315. The variants did not synthesize detectable quantities of alpha heavy chains but continued to synthesize and secrete light chains. J chain was synthesized by both parent and variant cell lines but only secreted by the parent cells. It is postulated that J chain synthesis is not dependent on alpha heavy chain synthesis, but that secretion of J chain by MOPC 315 cells occurs only because of its attachment to the Ig1 molecule.
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PMID:Synthesis but not secretion of J chain by variant mouse myeloma cells which lose alpha-chain-synthesizing ability. 80 9

The complement (C) system can solubilize immune precipitates prepared with antibodies of the IgG class, and apparently also of the IgM class. This paper shows that C can also solubilize immune precipitates prepared with two different antigen-binding IgA myeloma proteins. Immune precipitates were prepared with a) mouse myeloma protein TEPC 15 and PC-KLH, and b) mouse myeloma protein MOPC 315 and DNP-BSA. The precipitates could be solubilized by fresh mouse serum, but not by zymosan- or heat-inactivated serum. The rate of solubilization was not affected by the removal of of Ca++ ions. These results verify that the C-mediated solubilization effect can proceed entirely via the alternative C pathway, and lend increased support to the view that the effect is a general phenomenon, not restricted to a particular antibody class or type of antigen.
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PMID:Solubilization of IgA immune precipitates by complement. 97 53


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