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)

Monoclonal antibodies exhibiting various specificities for B6 vitamer forms have been prepared. The antigen preparation employed was a partially purified mixture of human placental proteins that had been derivatized by reaction with pyridoxal 5'-phosphate and sodium borohydride. Spleen cells obtained from mice immunized with the phosphopyridoxyl protein preparation were fused with the mouse myeloma cell line designated X63-Ag8.653. The resulting hybridomas were screened for production of antibodies to the haptenic phosphopyridoxyl group using an enzyme-linked immunosorbent assay. Clones producing such antibodies were isolated by limiting dilution methods. The monoclonal antibodies obtained in this fashion have been characterized with respect to their ability to interact with various forms of vitamin B6. In addition, these antibodies have been shown to be useful in the detection of cellular pyridoxal phosphate binding components using immunoblot techniques. Monoclonal antibodies to vitamin B6 derivatives are potentially powerful tools in the assessment of vitamin B6 nutritional status and in the study of the roles of pyridoxal phosphate binding components in relation to growth, differentiation, carcinogenesis, and steroid hormone action.
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PMID:Preparation, characterization, and use of monoclonal antibodies to vitamin B6. 682 78

Suspension of mouse myeloma cells in phosphate buffered saline (PBS) induced a significant amount of cell death. The lethal effects of PBS include an increase in cell lysis, a decreased ability of cells to exclude trypan blue, and a decrease in the colony-forming ability of these cells. Dead cells were also detected on a Coulter counter by the increase in the fraction of cells with a smaller electrical size distribution (ESD). Comparing mixtures of live and dead cells by ESD and trypan-blue exclusion showed a high correlation of electrical size with viability (correlation coefficient = 0.98). Sizing of PBS-treated cells by light microscopy suggested that the altered ESD of the PBS-treated cells was due to a downward shift in the volume distribution. Light-scattering experiments also suggested a decrease in the size of cells after PBS treatment. An increase in permeability of the cell membrane may also contribute to these results. We conclude that electrical sizing is an excellent indicator of physical changes that result from PBS-induced cell death, and is an effective method for distinguishing live and dead mouse myeloma cells after PBS treatment.
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PMID:Electrical determination of viability in saline-treated mouse myeloma cells. 710 49

L-Phenylalanine mustard (L-PAM), a bis-choroethylamine, is an important drug in the treatment of multiple myeloma and ovarian cancer. It undergoes rapid hydrolysis in vitro and in vivo, forming the mono-and dihydroxy degradation products. L-PAM's first-order disappearance rate in a phosphate-buffered solution did not differ statistically according to the presence or absence of activated rat liver microsomal enzymes. Furthermore, L-PAM's disappearance rate in a rat whole liver perfusion system was not greater than its hydrolysis rate in water. In vitro plasma recovery studies showed that up to 85% of the 14C L-PAM drug equivalents could be recovered as the parent compound and the mono- and dihydroxy degradation products. Thus, L-PAM in in vitro degradation was similar qualitatively and quantitatively to its reported in vivo degradation in animals and man. It is concluded that L-PAM does not undergo important, active in vivo metabolism.
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PMID:In vitro degradation of L-phenylalanine mustard (L-PAM). 710 81

Eighteen patients with multiple myeloma were studied using radiographs of the skeletal system, technetium phosphate bone scans, and gallium-67 scintigraphy. A total of 94 sites were used as the basis for comparison in these 18 patients. Radiographic sensitivity on a patient basis was 94%, and was 82% on a site basis. Bone scans were positive in 78% of patients and in 46% of sites. Gallium scans were positive in 56% of patients and 40% of sites. In five of the 18 patients, gallium scans showed activity in abnormal sites with a greater lesion-to-nonlesion ratio than did the bone scan. In this subgroup of patients, the disease was fulminant, and all died within 3 mo of their study. The finding of high gallium uptake in osseous sites that are normal or only slightly abnormal on bone scan has served to identify a subgroup of patients with rapidly progressive disease who may benefit from alternative treatment modalities such as radiation therapy.
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PMID:Radiographic and radionuclide imaging in multiple myeloma: the role of gallium scintigraphy: concise communication. 720 66

Monoclonal antibodies (mAbs) of IgG1 class produced by hybridomas raised with NS-1 myelomas, which were purified homogeneously by anion-exchange high-performance liquid chromatography (HPLC), contained two types of immunoglobulin light (kappa) chain. Since NS-1 myeloma synthesizes the light (kappa) chain, the mAb was presumed to be the mixture of hybrid mAbs formed by the random association of heavy (gamma l) and light chains from antigen-immunized spleen cells and light chain from NS-1 cells. Hydrophobic interaction HPLC using TSKgel Phenyl-5PW was applicable to separate 3 species of hybrid mAb from mAb fractions obtained by anion-exchange HPLC. mAbs in the fractions were adsorbed onto the gel equilibrated with phosphate-buffered saline containing 1 M ammonium sulfate and eluted by reducing the concentration to 0 M. The hybrid mAbs were purified separately. The hydrophobic interaction HPLC could discriminate a small difference in hydrophobicity between kappa chains from spleen and NS-1 cells. The immunoreactivities of hybrid mAb bearing light chains only from spleen cells and that bearing those from both spleen and NS-1 cells were almost the same, and hybrid mAb bearing light chains derived only from NS-1 cells showed a relatively lower immunoreactivity than the others. The method described here could be useful for purification of hybrid mAbs.
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PMID:Purification of monoclonal antibodies with light-chain heterogeneity produced by mouse hybridomas raised with NS-1 myelomas: application of hydrophobic interaction high-performance liquid chromatography. 750 10

Primary cultures of cells derived from the rat proximal tubule were exposed to up to 200 microM lambda- or kappa-light chain obtained from myeloma patients. Light chains inhibited the uptake of both phosphate and glucose by the cells while albumin had no effect. The half-maximal inhibitory concentration (IC50) of both the lambda- and kappa-light chains on phosphate transport were similar, 34 and 35 microM respectively. The IC50 of the kappa-light chain on glucose transport was 360 microM. The inhibitory effect of light chains was dose-dependent (r = 0.90, p < 0.01 for the lambda-light chain and r = 0.93, p < 0.001 for the kappa-light chain, on phosphate transport; and r = 0.93, p < 0.001 for glucose transport). Dixon and Line-weaver-Burk plot analyses were characteristic for noncompetitive inhibition. The inhibition constant 89 microM for phosphate uptake derived from the Dixon plot was similar to the IC50 calculated from the dose-response curves. These findings indicate that light chains, at concentrations found in the tubule fluid of a typical myeloma patient, are potent inhibitors of phosphate and glucose transport in proximal tubular cells, and that direct cell toxicity is a major mechanism of light chain nephrotoxicity.
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PMID:Effect of myeloma light chains on phosphate and glucose transport in renal proximal tubule cells. 753 8

A murine monoclonal antibody, MAHI 3 (immunoglobulin G2b), that is broadly reactive with Haemophilus influenzae lipopolysaccharides (LPSs) but nonreactive with all enterobacterial LPSs tested was generated by fusing mouse myeloma cells with spleen cells of BALB/c mice immunized with azide-killed H. influenzae RM.7004. MAHI 3 bound to all H. influenzae, all other human Haemophilus spp., all Bordetella pertussis and Bordetella parapertussis, and all Aeromonas spp. tested but not to any Neisseria or Moraxella catarrhalis strains, as determined by enzyme immunoassay, colony dot immunoblotting, and immunoblotting. In an inhibition enzyme immunoassay, MAHI 3 reacted with all 45 H. influenzae LPSs tested but not with the LPS from the rough mutant I69 Rd-/b+, which has only 3-deoxy-D-manno-octulosonic acid (P) [Kdo(P)] and lipid A. The antibody was not inhibited by H. influenzae lipid A or lipid-free polysaccharide isolated after mild acid hydrolysis. Only native LPSs show positive inhibitory activity, indicating that part of lipid A is involved in the binding of MAHI 3. From the results, it is indicated that the structural element recognized by MAHI 3 is Hep alpha 1-->2Hep alpha 1-->3Hep alpha 1-->Kdo together with part of lipid A, including the phosphate.
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PMID:The tetrasaccharide L-alpha-D-heptose1-->2-L-alpha-D-heptose1--> 3-L-alpha-D-heptose1-->(3-deoxy-D-manno-octulosonic acid) and phosphate in lipid A define the conserved epitope in Haemophilus lipopolysaccharides recognized by a monoclonal antibody. 754 87

Hybridoma cells producing antibody reactive with poly(A) were isolated following fusion of spleen cells from a BALB/c mouse immunized with poly(A).poly(dT) and myeloma cells. The antibody was purified from ascitic fluid by the formation of immune complexes with poly(A). The antibody reacted with poly(A) and some homopolymers (poly(dT), poly(I) and poly(dC)) which was most probably due to its reaction with the ribose-phosphate part of the molecules, but not with cellular RNAs and DNA. Poly(A) tailed 5 S rRNA (about 20 nucleotides) and tobacco mosaic virus RNA (1060 nucleotides) were precipitated quantitatively by the antibody. Dot hybridization and in vitro translation confirmed that the RNA precipitated by the antibody from mouse spleen total RNA contained biologically active mRNA.
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PMID:Production of a monoclonal antibody reactive with poly(A) and its application in the isolation of poly(A)+ RNA. 768 20

Mouse monoclonal antibodies (MAbs) DP8 [immunoglobulin G1(kappa)] and DH24 [immunoglobulin M(kappa)], which are specific for Haemophilus ducreyi lipopolysaccharide (LPS), were generated by fusing mouse myeloma NS0 cells with spleen cells of BALB/c mice immunized with a total membrane preparation of H. ducreyi. MAb DP8 reacted in whole-cell enzyme immunoassay (EIA) and colony dot immunoblotting with all 50 strains of H. ducreyi but not with any other bacteria tested, which suggests an exposed and species-specific epitope on the H. ducreyi cell surface. This conclusion was supported by the finding that DP8 bound to all six H. ducreyi LPSs tested but not to any of the Haemophilus influenzae or enterobacterial LPSs or synthetic glycoconjugates. The MAb DH24 bound to 43 of 50 strains of H. ducreyi and to few strains of H. influenzae, Neisseria gonorrhoeae, and Neisseria meningitidis, as evaluated by whole-cell EIA and colony dot immunoblotting. The MAb DH24 reacted with five of the six H. ducreyi LPSs tested and with the lacto-N-neotetraose (Gal beta 1-->4GlcNAc beta 1-->3Gal beta 1-->4Glc) series of synthetic glycoconjugates, as determined by EIA. By using polysaccharides obtained after both mild acidic hydrolysis and strong alkali treatment and dephosphorylated samples as inhibitors of the MAbs binding to H. ducreyi LPS antigens, it could be shown that phosphate groups were essential for the binding of DP8 to LPS but that they did not affect antigenic recognition by DH24. None of the MAbs bound to isolated lipid A, but aggregation caused by the fatty acids of lipid A was essential for epitope recognition.
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PMID:Monoclonal antibodies against Haemophilus lipopolysaccharides: clone DP8 specific for Haemophilus ducreyi and clone DH24 binding to lacto-N-neotetraose. 779 83

Polyclonal antibodies catalyzing the hydrolysis of carbonate ester were generated by immunizing a rabbit with hapten(4-nitrophenyl phosphate II) conjugated to keyhole limpet hemocyanin. The hydrolytic activity of IgG purified from antisera exhibited plateu one month later than the simple hapten-binding. The affinity of IgG with substrate increased even after the hapten-binding reached plateu. These suggest a strategy to generate good polyclonal catalytic antibodies and the day to fuse spleen cell with myeloma cell to get good monoclonal catalytic antibodies.
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PMID:Delayed appearance of the catalytic activity by immunization of a rabbit compared with the hapten binding. 784 22


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