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)

Immunoglobulin- or multiple myeloma-associated amyloidosis has been distinguished by the tissue deposition of Congophilic, fibrillar protein consisting of light chains or light-chain fragments (AL amyloidosis). We now report the isolation and characterization of another form of immunoglobulin-associated amyloid obtained from a patient who had extensive systemic amyloidosis and in whom the amyloid deposits consisted not of light chains but rather of an unusual form of heavy chain. This component, isolated from splenic amyloid extracts, represented an internally deleted IgG1 heavy chain as evidenced by immunochemical, electrophoretic, and amino acid sequence analyses. A comparable immunoglobulin-related monoclonal protein, consisting only of IgG heavy chains, was present in the patient's urine. Based on serologic reactivity with a battery of anti-immunoglobulin antisera, these two immunoglobulin-related components were antigenically identical; however, when compared to normal IgG, both were deficient in Fc-associated gamma-chain determinants. The structural abnormality of the amyloid gamma-chain protein was further evidenced by SDS/PAGE and immuno-blotting analyses: An unusually low molecular mass of approximately 22 kDa was found for this material vs. the expected value of approximately 55 kDa for a normal gamma heavy chain. Despite the lack of certain Fc determinants, the amyloid and urinary heavy-chain proteins expressed the IgG1 subclass allotype marker G1m(a) located on the third constant region (CH3) domain of the internally deleted IgG1 heavy chains. That the amyloid protein contained an intact CH3 domain was established through amino acid sequence analyses of cyanogen bromide fragments and peptides generated by a lysine-specific protease. These studies also revealed that the gamma-chain amyloid protein contained the complete heavy-chain variable (VH) domain [including the diversity (DH) and joining (JH) segments] that was contiguous with the CH3 domain. The low molecular mass of the protein resulted from the total absence of the first (CH1), hinge, and second (CH2) heavy-chain constant regions. Such extensive CH deletions and the presence of a complete VH distinguish this amyloid-associated heavy chain from all other heretofore characterized gamma-heavy-chain disease proteins. This heavy-chain-related form of immunoglobulin-associated amyloidosis is tentatively designated AH amyloidosis.
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PMID:Immunoglobulin heavy-chain-associated amyloidosis. 211 50

Spleen cells of BALB/c mice immunized with human pulmonary adenocarcinoma cell LTEP-a2 were fused with murine myeloma cell SP 2/0, from which 4 hybridomas (2 A7, 2 E9, 4 F2 and 5 F11) were obtained. Indirect immunofluorescence test showed that these 4 monoclonal antibodies reacted with human lung cancer cells, but not with 2 BS or the lymphocytes and red blood cells in 4 different ABO groups of 10 persons. Using ABC immunoperoxidase stain technique, these 4 antibodies showed negative reaction with 9 tissue types from the normal subject and fetus but could react with 52-83% of the 29 human lung carcinomas and 64-92% of the 24 non-small cell lung cancers (non-SCLC). When 5 F11 was combined with 2 A7 or 2 E9, the percentage of positive stain was 100% in 24 non-SCLC. The results of indirect immunofluorescence stain showed that strong membrane stain by 5 F11 and membrane stain by 4 F2 were obtained, indicating that these antibodies could recognize antigens on cancer cell membrane. It is suggested that a mixture of 5 F11 and other antibodies be useful in the diagnosis and treatment of lung cancer. Molecular weight of the antigens recognized by the 4 antibodies was determined by SDS-PAGE and immunoblot technique to be 47 KD (2 A7), 67 KD (2E9), 40 KD (4F2) and 56 KD (5 F11).
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PMID:[Monoclonal antibody against human lung carcinoma]. 217 66

A case of acquired von Willebrand disease (AvWD) associated with an IgA lambda multiple myeloma is reported. No form of inhibitor could be detected. SDS-agarose gel electrophoresis patterns of von Willebrand factor (vWF) both in plasma and platelet lysates were normal but a decrease in all-sized multimers with a type IA pattern was seen. After 1-deamino-8-D arginine vasopressin (DDAVP) infusion, vWF multimers larger than those seen in the resting state appeared in patient plasma, which were progressively cleared. Indirect immunofluorescence studies with a monoclonal antibody to vWF showed that vWF was selectively absorbed into myelomatous cells. This is the first case of AvWD associated with multiple myeloma resulting from the selective absorption of vWF into abnormal plasma cells. This feature established a new pathophysiological mechanism of AvWD in multiple myeloma and probably in other lymphoproliferative diseases.
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PMID:Acquired von Willebrand disease in multiple myeloma secondary to absorption of von Willebrand factor by plasma cells. 220 95

Rearrangements of immunoglobulin genes are mediated by highly conserved heptamer and nonamer recombinational signal sequence. Using a protein-blotting procedure, a heptamer and nonamer recombinational signal sequence-specific DNA-binding protein(s) was examined in the nuclear extracts from lymphoid and nonlymphoid cell lines. Nuclear extracts were subjected to SDS-polyacrylamide gel electrophoresis, and transferred by electroblotting to nitrocellulose filters. Then the filters were hybridized to 32P-labelled synthetic double-stranded heptamer-23bp-nonamer or nonamer-12bp-heptamer recombinational signal sequence probes. A relatively large amount of a DNA-binding protein(s) of Mr 115,000 for both probes was detected in the nuclear extracts from immature B and immature T cell lines. No DNA-binding proteins were detected in a myeloma cell line. Interestingly, this DNA-binding protein(s) might be able to recognize both heptamer and nonamer. Recombinational signal sequence-specific DNA-binding activity of the protein(s) and the presence of the protein(s) in a stage-specific manner strongly suggest that the protein(s) of Mr 115,000 detected here may play an important role in the recombination of Ig and TCR genes.
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PMID:Identification of a recombinational signal sequence-specific DNA-binding protein(s) of Mr 115,000 in the nuclear extracts from immature lymphoid cell lines. 221 1

Guinea pig polymorphonuclear leukocytes (PMNs) possess two distinct types of Fc gamma receptor (Fc gamma R): Fc gamma 1/gamma 2R for both IgG1 and IgG2, and Fc gamma 2R for IgG2 alone. The Fc gamma 2R was previously shown to differ antigenically from homologous macrophage (M phi) Fc gamma 2R by the use of a monoclonal antibody to M phi Fc gamma 2R (VIIAI IgG1), though the Fc gamma 1/gamma 2R cross-reacts with a monoclonal antibody to homologous M phi Fc gamma 1/gamma 2R (VIA2 IgG1). Recently, we obtained a monoclonal antibody (MP-2) secreted by a hybridoma prepared by fusion of the splenic cells of mice immunized with guinea pig PMNs with a myeloma cell line. This antibody completely inhibited both the Fc gamma 2R-mediated rosette formation of PMNs with IgG2 antibody-sensitized sheep erythrocytes and the Fc gamma 2R-mediated binding of ovalbumin (OA)-complexed IgG2 antibody to PMNs. When the antigen of MP-2 was isolated by affinity chromatography with the antibody-Sepharose, it gave a single band with a molecular weight of 120,000 on SDS-PAGE. The number of antigen molecules per PMN was estimated to be 9 X 10(4) by measuring the binding of 125I-MP-2 Fab. This value was essentially the same as that obtained by measuring the binding of OA-complexed IgG2 antibody to the PMNs treated with the Fab' of VIA2 IgG1. These results strongly suggest that MP-2 is a monoclonal antibody to PMN Fc gamma 2R.
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PMID:Characterization of the Fc receptor for IgG2 on guinea pig polymorphonuclear leukocytes by the use of a monoclonal antibody. 222 13

Production of porcine monoclonal antibodies for use in research and immunotherapy has been hampered by the lack of suitable fusion partners which promote high efficiencies of hybridoma out-growth and immunoglobulin synthesis. To overcome these obstacles, five heteromyeloma fusion partners (HM-1,2,3,4 and 5) were constructed by successively fusing porcine lymphocytes with murine myeloma cells or murine x bovine heteromyeloma cells. Following section of hypoxanthine/aminopterin/thymidine (HAT)-sensitive mutants, karyotypes, growth rates and surface phenotypes of the heteromyelomas were determined. Karyotyping revealed an increase in the mean number of chromosomes present in HM-1,4 and 5 cells. Peak doubling times of the parental and HM cells ranged between 12.2 and 17.4 h. Uisng flow microfluorimetry and monoclonal antibodies specific for class I/II major histocompatability antigens, it was determined that the surface phenotype of HM-1,2,3,4 and 5 resembled that of the parental murine X63 myeloma cells. HM 1,2,3,4 and 5 were evaluated for their abilities to serve as fusion partners. Highest percentages of hybrid outgrowth (37%) and immunoglobulin synthesis (52%) were observed when HM-1 was fused with procine lymphocytes. When cloned, percentage of outgrowth and immunoglobulin synthesis increased if HM-1 and HM-2 were used as fusion partners. Cryopreservation of HM-1 and HM-2 did not adversely affect their abilities to promote hybrid outgrowth or immunoglobulin synthesis. During the first week following fusion of porcine lymphocytes with heteromyelomas, murine thymocytes were found to be essential for survival of the nascent hybrids. To confirm that immunoglobulin secreted by hybridomas was of porcine and not murine or bovine origin, culture supernates were subjected to SDS gel electrophoresis, electroblotted and identified. using species-specific isotyping reagents. Two of four cell lines tested secreted porcine light chains and one of four cell lines secreted whole IgM molecules. This paper is the first to describe porcine heteromyelomas for use as fusion partners. Similar to findings of human and bovine studies, our data suggest that heteromyeloma fusion partners perform better than rodent myelomas for creating hybridomas synthesizing porcine immunoglobulin.
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PMID:Characterization of heteromyeloma fusion partners which promote the outgrowth of porcine hybridomas. 226 87

Growth cartilage (GC) cells of young rabbits were cultured in vitro and their homogenates were injected into mice. Hybridomas were prepared by the cell fusion technique between the myeloma cells and the spleen cells of the immunized mice. Monoclonal antibodies (MoAbs) were produced by the hybridomas in the peritoneal cavities of the mice, and some of these, temporarily named MoAbs A, B, D, N, P, and S, were studied. The localization of the antigens of each of the MoAbs in the GC or adjacent resting cartilage (RC) was examined by indirect fluorescent antibody staining. The molecular weight of the antigens was examined by immunoblot staining after SDS-polyacrylamide gel electrophoresis. MoAb A and MoAb N stained RC cells and GC cells, except calcified GC. MoAb B stained the hypertrophic and calcified GC, and matrices in the RC and proliferating GC. MoAb D stained the calcified GC. MoAb P and MoAb S stained the RC cells and the matrices in the GC, intensively in the hypertrophic GC and perichondrium. The molecular weights of the antigens of MoAbs A, P, and S were 40-70 KD, 35-40 KD and 30 KD, respectively.
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PMID:Production and characterization of monoclonal antibodies against rabbit growth cartilage. 227 43

A rapid and simple affinity chromatography method for purifying IgM from myeloma serum and ascites fluid is described. Complement protein C1q is coupled to Sepharose with an efficiency of 35%, giving 1.7 mg of C1q bound/ml of gel. This C1q-Sepharose selectively binds IgM from crude samples at 5 degrees C, with a capacity of 0.4 mg of IgM/ml of gel. The bound IgM may be eluted simply and isocratically by bringing the gel to room temperature for 2 h, or by washing with buffer containing 0.5 M KI. The eluted IgM is highly pure by SDS-PAGE and double immunodiffusion analysis, although IgG may be a potential contaminant. The C1q-Sepharose is stable for at least 18 months.
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PMID:Single-step purification of immunoglobulin M on C1q-Sepharose. 230 24

The polyclonal antibodies to juveniles of Paragoniums westermani (PwJ-PcAbs) from sera of Wistar rats infected with Paragoniums westermani (P.w.) were purified by Sephadex G 200 chromatography. Next the shared serological antigens of P.w. metacercaria and juveniles (PwMJ-SAg) from the crude antigens of the metacercariae (M-NS-Ag) were purified with immuno-affinity chromatography on cyanogen bromide-activated cross-linked Sepharose 4B beads coupled with PwJ-PcAbs. PwMJ-SAg, a group of glycoprotein molecules shown by the staining test, were specific serological antigens of P.w. metacercariae and juveniles, identified by the immunoabsorb test and immunoelectrophoresis. By SDS-PAGE, PwMJ-SAg were fractionated to seven bands, including major bands A (27.5 K) and Bi (19.5 K), the two major serological antigen molecules. 20 sera samples from the patients with the nonpulmonary type of P. w. paragonimiasis were detected using PwMJ-SAg and M-NS-Ag by Dot-ELISA, and the difference of sensitivity between two antigens was highly statistically significant (P less than 0.001). BALB/c mice, in the early stage of infection with P. w. metacercaria, were immunized with PwMJ-SAg. The spleen cells of the mice were isolated and fused with SP2/o, a murine myeloma cell line. After three subclonal cultures, eight cell lines secreting monoclonal antibodies (McAbs) to PwMJ-SAg were prepared from 384 wells of hybridoma cells. All McAbs were IgG1 subclass.
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PMID:Studies on specific serological antigens in metacercariae and juveniles of Paragoniums westermani and its monoclonal antibodies. 234 88

Two monoclonal antibodies (AD-1 and AD-2) were prepared by fusion of mouse myeloma cells and lymph node cells of mice immunized with porcine adipocyte plasma membranes. Immunoprecipitation of iodinated adipocyte plasma membrane proteins followed by SDS-PAGE and autoradiography yielded protein antigens for each antibody. The AD-1 and AD-2 antigens were detected on mature adipocytes and a proportion of non-lipid-containing cells in stromal-vascular cultures. Adipocytes and associated capillary networks in subcutaneous adipose tissues as well as capillaries between the underlying muscle fiber bundles bound each antibody, whereas the AD-2 monoclonal antibody also reacted with vessels but not capillaries in liver tissues. In stromal-vascular cell cultures prepared from newborn pig subcutaneous tissue, the AD-1 and AD-2 antibodies exhibited reactivity towards 45 percent and 10 percent respectively, of cells 24 hours after seeding. On the other hand, only 4 percent and 1 percent of the cells in cultures prepared from 60 day fetal subcutaneous tissues expressed detectable amounts of the AD-1 and AD-2 antigens, respectively. In conclusion, cells along the adipogenic lineage possess cell surface antigens which may not be unique to adipogenic cells, but do exhibit differential expression among cell populations within adipose tissues. A temporal relationship between adipogenesis and angiogenesis was also demonstrated.
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PMID:Monoclonal antibodies against cell surface antigens expressed during porcine adipocyte differentiation. 238 93


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