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)

Bone marrow mononuclear cell populations were studied in 35 patients without myeloma, 39 patients with multiple myeloma, and 15 patients with benign monoclonal gammopathy. Bone marrow mononuclear cell receptors, responses to mitogens or allogeneic stimuli, and suppressive effects on in vitro peripheral blood lymphocyte (PBL) function were studied. In bone marrow cell populations from patients with untreated multiple myeloma, the percent of complement receptor-bearing cells and the pokeweed mitogen- and concanavalin A-stimulated responses were significantly greater than were those in bone marrow cell populations from patients without myeloma. Sheep red blood cell receptor-bearing cells were significantly greater in marrow populations from treated multiple myeloma patients compared to those from untreated multiple myeloma patients. Sheep red blood cell receptor-bearing cells from the bone marrow of multiple myeloma patients suppressed responses of the multiple myeloma patients' PBL's to autologous mitomycin C-treated bone marrow plasma cells and to allogeneic stimuli in one-way mixed leukocyte culture. Complement receptor-bearing cells suppressed the response to pokeweed mitogen. The presence of lymphocytes in the marrow compartment that are capable of suppressing the response of myeloma patients' PBL's to plasma cell antigens may be significant in the pathogenesis of multiple myeloma.
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PMID:Multiple myeloma: an immunologic profile. II. Bone marrow studies. 15 51

A monoclonal mouse antibody (3A1) that specifically bound to 65% of human peripheral blood (PB) thymus-derived (T) cells but did not bind to complement receptor-positive PB bone marrow-derived (B) cells, polymorphonuclear leukocytes, or human erythrocytes has been produced. The 3AI antibody was synthesized by a stable cloned lymphocyte hybrid cell line. This lymphocyte hybrid line (3AI) was derived from fusion of P3 X 63/Ag8 myeloma cells and spleen cells from BALB/c mice immunized with HSB-2 cells, a human T cell line. The 3A1 lymphocyte hybrid line produced mouse ascites fluid containing 3A1 antibody in saturating titers of up to 1:25,600. Purified PB T cells that carried the 3A1 antigen incorporated tritiated thymidine maximally in response to phytohemagglutinin and concanavalin A stimulation, whereas purified PB T cells that lacked the 3A1 antigen responded suboptimally to phytohemagglutinin and minimally to concanavalin A. Thus, the 3A1 antibody can be easily used to study the role of 3A1-positive and negative T cell subsets in the regulation of normal and abnormal human immune responses.
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PMID:Human lymphocyte antigens: production of a monoclonal antibody that defines functional thymus-derived lymphocyte subsets. 31 38

A monoclonal antibody, anti-Z-1, was established by fusion of spleen cells from mice immunized with guinea pig thioglycollate-induced peritoneal macrophages (TGC-M phi s) with mouse myeloma cells, P3-X63-Ag8-6.5.3. The Fab' fragments of anti-Z-1 bound to almost all of the TGC-M phi s with a high association constant (6.0 +/- 0.8) X 10(8) M-1, and effectively inhibited phagocytic activities of the cells for unopsonized zymosan and serum-treated zymosan. On the contrary, neither the phagocytic activity for rabbit IgG antibody-sensitized sheep erythrocytes nor that for periodate-treated sheep erythrocytes was inhibited by anti-Z-1. Immunoprecipitation analysis revealed that the antigen recognized by anti-Z-1, which was named Z-1 antigen, consists of a polypeptide chain with a molecular weight of 140,000 (alpha chain) noncovalently associated with a polypeptide chain of 95,000 (beta chain). The epitope with which anti-Z-1 reacts was found to be on the alpha chain by Western blotting. Furthermore, it was found that Z-1 antigen solubilized from the cells with nonionic detergent was capable of binding to unopsonized zymosan, suggesting that Z-1 antigen may function as a receptor for zymosan. These findings show the structural and functional similarities of Z-1 molecules on guinea pig peritoneal macrophages to the third complement receptor on human and mouse leukocytes.
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PMID:Characterization of a monoclonal antibody to guinea pig peritoneal macrophages that inhibits phagocytosis of unopsonized zymosan: structural and functional similarities of the antigen to human and mouse CR3. 246 9

In the majority of 188 non-Hodgkin lymphomas (NHL) investigated in this study, we found a simultaneous expression of the receptors for c3b and c3d (CR1 & CR2; cccorr = 0.69, P less than 0.0005). An analysis of the different histological entities of the Kiel classification revealed that this coexpression was most pronounced for germinal centre-derived (cccorr = 0.63, P = 0.0004) and immunocytic NHL (cccorr = 0.86, P = 0.0024), whereas in chronic lymphocytic leukaemias there tended to be a more heterogeneous pattern of complement receptor (CR) expression (cccorr = 0.29, P greater than 0.10). In contrast to these NHL of mid B cell stage, most of the NHL of early (i.e. acute lymphocytic leukaemia, lymphoblastic NHL) and late B cell stage (i.e. hairy cell leukaemia, immunoblastic NHL, multiple myeloma) did not express either of these receptors. CR positive NHL often showed a follicular arrangement of the neoplastic cells and had higher numbers of T helper/inducer (T4) lymphocytes (PCR1 less than 0.00005, PCR2 less than 0.05). Some cases of mid B cell NHL and all cases of hairy cell leukaemia reacted with antibodies against CR3 (i.e. the ic3b receptor).
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PMID:Receptors for the third component of complement: their association with maturation stage in non-Hodgkin lymphomas (NHL) and their possible implication with the development of follicular structures. 294 42

From a panel of IgG1 myeloma proteins, only one was found to interact with human monocyte FcR in a manner similar to that of polyclonal IgG. This protein was used in binding studies involving human macrophage Fc receptors. A monomeric fraction depleted of dimeric and polymeric IgG1 was crosslinked with bis-diazonium benzidine, and a fraction highly enriched in cross linked IgG1 dimers was radiolabeled. Labeled monomeric and dimeric IgG were allowed to interact with monocytes that had matured to macrophages in vitro. The association with macrophages at 4 degrees C, in the presence of cytochalasin B, reached a plateau after 6 hr. The dissociation induced by excess unlabeled IgG followed similar kinetics as the association, but 20-30% of the bound IgG could not be dissociated. Under equilibrium conditions, evidence for a single FcR population binding monomeric IgG was obtained, the Kd being in the range of 12-42 nM. In contrast, the binding of dimeric IgG was more consistent with a model assuming two populations of binding sites when appropriate curve-fitting calculations were applied. The high-affinity FcR population had a Kd in the range of 0.8-3.5 nM, whereas the Kd of the low-affinity FcR population was in the range of 28-85 nM. When macrophages had been pre-treated with recombinant interferon-gamma, the expression of high-affinity sites was increased by a factor of 1.5-3, but the number of low-affinity sites was not augmented. Cytofluorographic analyses confirmed the increased expression of high-affinity FcR, binding fluoresceinating murine IgG2a. The expression of CD16, a low-affinity FcR expressed on neutrophils, NK cells and macrophages, as well as the expression of the complement receptor type III was little influenced by the rIFN-gamma pretreatment.
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PMID:Monomeric and dimeric IgG1 as probes for assessing high-affinity and low-affinity receptors for IgG on human monocyte-derived macrophages and on activated macrophages. 297 17

A cDNA clone encoding human thymosin-beta 4 was isolated from a cDNA library prepared from peripheral blood leukocytes of a patient with acute lymphocytic leukemia. This clone contained the entire coding sequence of 43 amino acid residues of thymosin-beta 4 and had an initiation codon and two termination codons. The amino acid and nucleotide sequences in the coding region were well conserved between rat and human. Nine of 132 nucleotides were different in the coding sequences (93% homology), but the deduced amino acid sequences were identical. No signal peptide was found in the deduced protein sequence. Human thymosin-beta 4 mRNA, approximately 830 nucleotides in length, was about 30 nucleotides larger than rat thymosin-beta 4 mRNA. Expression of the human thymosin-beta 4 gene in various primary myeloid and lymphoid malignant cells and in a few human hemopoietic cell lines was studied. Northern blot analyses of different neoplastic B lymphocytes revealed that steady state levels of thymosin-beta 4 mRNA varied as a function of differentiation stage. Thymosin-beta 4 mRNA levels were decreased in myeloma cells as are class II human leukocyte antigen, Fc receptor, and complement receptor, suggesting a relationship between thymosin-beta 4 and the immune response. Thymosin-beta 4 mRNA was more highly expressed in mature granulocytes than in immature blastic cells. Treatment of THP-1 cells, a human monocytic cell line, with recombinant human interferon-lambda reduced the levels of thymosin-beta 4 mRNA. Its level decreased after differentiation of THP-1 cells into Ia+ macrophages, but increased after differentiation of HL-60 cells into Ia- macrophages. The pattern of thymosin-beta 4 gene expression suggests that it may play a fundamental role in the host defense mechanism.
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PMID:Differential expression of the human thymosin-beta 4 gene in lymphocytes, macrophages, and granulocytes. 350 Feb 30

A comparison was made between the binding sites of two receptors that are believed to be closely associated on human B lymphocytes: complement receptor type two (CR2) that is specific for C3d fragments, and the receptor (EBVR) for Epstein Barr virus (EBV). Isolated fluid-phase CR2 bound to C3d on erythrocytes (EC3d) and inhibited both B cell-EC3d rosettes and the agglutination of EC3d by anti-C3d, it failed to inhibit either the binding or superinfection of B cells by EBV. By contrast, isolated fluid-phase EBVR inhibited EBV B cell binding activity and superinfection but had no CR2 activity. In addition, radiolabeled CR2 bound to EC3d and anti-CR2-Sepharose, whereas radiolabeled EBVR did not. Purified fluid-phase C3d fragments inhibited EC3d rosette formation with CR2+/EBVR+ cells but did not inhibit EBV binding. However, EBV binding to B cells did inhibit EC3d rosette formation. Clones of human/mouse somatic cell hybrids made from CR2+/EBVR+ human B lymphoblastoid cell and CR2-/EBVR- mouse myeloma cell parents expressed either EBVR or CR2 but only rarely expressed both EBVR and CR2. This suggested that the genes for EBVR and CR2 were located on two different human chromosomes. Thus it was concluded that CR2 is probably not the binding site for EBV.
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PMID:Studies of the Epstein Barr virus receptor found on Raji cells. II. A comparison of lymphocyte binding sites for Epstein Barr virus and C3d. 621 5