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)

A routine blood analysis, using the Hitachi 717 analyser, of an asymptomatic patient with multiple myeloma revealed a phosphate concentration of 6.2 mmol/l (reference range 0.8-1.4 mmol/l). There was no clinical or biochemical evidence for secondary hyperphosphataemia. Two additional myeloma patients with a normal renal function were found to have serum phosphate concentrations of 5 and 4.7 mmol/l. Globulin-depleted sera of these patients were found to have phosphate levels within the normal range as assayed by a Hitachi 717. All these patients were found to have normal inorganic phosphate levels when a SMAC autoanalyser was used, thus indicating spurious readings by the Hitachi 717. The incidence of pseudohyperphosphataemia in 298 patients with normal renal function and hyperglobulinaemia was 8%. To test the direct effect of globulin on phosphate analysis by the Hitachi 717, globulin was precipitated from serum of myeloma and non-myeloma patients by ammonium sulphate. The analysed data showed a positive correlation between globulin concentration and the spurious phosphate levels. Furthermore, even when inorganic phosphate was completely removed from the tested samples, spurious phosphate readings were detected in the presence of globulins from either myeloma or non-myeloma patients by Hitachi 717. It can be concluded that the ammonium molybdate method for determining inorganic phosphate in the Hitachi 717 gives spuriously high phosphate levels in the presence of a high serum globulin concentration.
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PMID:Pseudohyperphosphataemia incidence in an automatic analyzer. 798 38

We report three cases of IgG kappa multiple myeloma with pseudohyperphosphatemia. The patients' serum calcium levels were normal, and the hyperphosphatemia was not related to impaired renal function. No hypoparathyroidism was found, and no exogenous phosphate preparation had been given. Since the hyperphosphatemia was of no obvious clinical or physiological significance, as evidenced by normal serum levels of 1,25 dihydroxy vitamin D3, it was diagnosed as spurious and was connected to interference of the paraprotein with the chromogenic assay. In two of the patients major fluctuations in serum phosphate levels were seen, induced by the changes in globulin and paraprotein levels that occurred during therapy and relapse.
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PMID:Hyperphosphatemia in multiple myeloma. 806 Nov 6

The authors report the case of an 82 year old woman hospitalized for hypercalcemia associated with low serum phosphate. Multiple myeloma was first diagnosed. However, despite chemotherapy, hypercalcemia persisted and she was subsequently diagnosed as primary hyperparathyroidism; eucalcemic state was then obtained after parathyroidectomy. Fifteen similar cases are reported in the literature and the mechanisms and implications of such an association are discussed.
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PMID:Coexisting kappa light chain multiple myeloma and primary hyperparathyroidism. 810 68

Six hybridoma clones (1M, 4M, 9M, 11M, 18M and 31G), secreting monoclonal antibodies (mAbs) against lipid A were obtained after fusion between cells of mouse myeloma line X63-Ag8.653 and spleen cells from BALB/c mice immunized with acid treated Salmonella minnesota bacteria coated with additional free lipid A. The specificity and cross-binding activity of the mAbs were characterized in ELISA by using synthetic lipid A analogs as well as different lipid A and lipopolysaccharides (LPS) extracted from R- and S-form bacteria. It was found that the antibodies recognize epitopes in which phosphate groups, especially those at the C4' position of the glucosamine backbone of lipid A, were present. These epitopes were accessible also for the antibodies in purified intact LPS. By using a set of core glycolipids with increasing completion of the core region of the molecule and S-LPSs it was shown that the mAbs cross-reacted with a variety of R- and S-form LPS. The binding activity decreased with increasing length of the polysaccharide chain. The mAb did not prevent ultimate lethality of mice challenged with Klebsiella pneumoniae B and Salmonella typhimurium C5. However a delay of mortality rate of mice pretreated with antibodies 18M and 31G and infected with K. pneumoniae was seen.
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PMID:Cross-binding activity and protective capacity of monoclonal antibodies to lipid A. 840 52

We have encountered two cases of bone tumors with high 18F-fluorodeoxyglucose (FDG) uptake and negative 99mTc-HMDP bone scintigraphy, including a patient with myeloma and a patient with a metastatic bone tumor from esophageal cancer. Bone scintigraphy with a 99mTc-phosphate complex reflects osteoblastic activity in the bone tissue surrounding the tumor, whereas the accumulation of FDG is associated with the metabolic activity of the tumor itself. An FDG-PET study can therefore be used as a complementary study for the detection and follow-up of bone tumors when a 99mTc-phosphate bone scintigram is negative.
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PMID:Fluorine-18-fluorodeoxyglucose positron emission tomography in technetium-99m-hydroxymethylenediphosphate negative bone tumors. 842 49

Prothymosin alpha is post-translationally modified. When human myeloma cells were metabolically labeled with [32P]orthophosphoric acid, they synthesized [32P]prothymosin alpha. The incorporated radioactivity was resistant to DNase and RNases A, T1, and T2, but could be completely removed by alkaline phosphatase. No evidence was found for an RNA adduct as postulated by Vartapetian et al. [Vartapetian, A., Makarova, T., Koonin, E. V., Agol, V. I., & Bogdanov, A. (1988) FEBS Lett. 232, 35-38]. Thin-layer electrophoresis of partially hydrolyzed [32P]prothymosin alpha indicated that serine residues were phosphorylated. Analysis of peptides derived from bovine prothymosin alpha and human [32P]prothymosin alpha by treatment with endoproteinase Lys-C revealed that the amino-terminal 14-mer, with serine residues at positions 1, 8, and 9, was phosphorylated at a single position. Approximately 2% of the peptide in each case contained phosphate. Further digestion of the phosphopeptide with Asp-N followed by C18 reversed-phase column chromatography produced two peptides: a phosphate-free 9-mer containing amino acids 6-14 and a labeled peptide migrating slightly faster than the N-terminal 5-mer derived from the unmodified 14-mer. Positive identification of the phosphorylated amino acid was obtained by colliding the 14-residue phosphopeptide with helium in the mass spectrometer and finding phosphate only in a nested set of phosphorylated fragments composed of the first three, four, and five amino acids. The results prove that prothymosin alpha contains N-terminal acetylserine phosphate. In a synchronized population of human myeloma cells, phosphorylation occurred throughout the cell cycle. Furthermore, prothymosin alpha appeared to be stable, with a half-life slightly shorter than the generation time. Although prothymosin alpha is known to be essential for cell division, the constancy of both the amount of the protein and the degree of its phosphorylation suggests that prothymosin alpha does not directly govern mitosis.
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PMID:Phosphorylation of human and bovine prothymosin alpha in vivo. 848 35

Glomerular extracapillary cellular proliferation with crescent formation initially presenting as rapidly progressive glomerulonephritis is a rare clinical manifestation of multiple myeloma. We report here a case of a 58 year old female who initially presented with haematuria, loss of weight and appetite and history of febrile episodes and was diagnosed following renal biopsy as rapidly progressive glomerulonephritis. Haemodialysis was carried out a month later because of uremic symptoms and maintained with monitoring of serum, calcium, phosphate, alkaline phosphatase, albumin and iPTH levels. After 6 months, she complained of bone pains over anterior chest wall which persisted even with low calcium haemodialysis. Serum protein electrophoresis and bone marrow aspiration revealed multiple myeloma. On starting chemotherapy, bone pain subsided but the patient expired within 15 days of therapy.
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PMID:Multiple myeloma presenting as proliferative (crescentic) glomerulonephritis. 873 63

The molecular mechanism underlying the interaction between myeloma cells and stromal cells was investigated by using a human myeloma cell line (OPM-2) and human umbilical vein endothelial cells (HUVECs). Adhesion of OPM-2 cells to HUVECs was found to be significantly augmented with treatment of OPM-2 cells with an alpha-glycosidase inhibitor, castanospermine (CSP). The treatment of OPM-2 cells with CSP resulted in alteration of oligosaccharide structures of cell surface glycoproteins particularly at molecular weight of 220 kD (GP220). To determine if GP220 was involved in the adhesion of OPM-2 cells to HUVECs, cell surface glycoproteins of HUVECs were labeled by biotin and were incubated with the PVDF membrane to which cell surface glycoproteins of OPM-2 cells were blotted. The biotinylated glycoproteins at the plasma membrane of HUVECs specifically bound to GP220 of OPM-2 cells. Purification and partial amino acid sequencing of GP220 revealed that GP220 had a structure homologous to cation-independent mannose 6-phosphate/insulin-like growth factor-II (CIM6P/IGF-II) receptor. Furthermore, an antibody against CIM6P/IGF-II receptor was reactive with GP220, indicating that GP220 was a CIM6P/IGF-II receptor. The adhesion of OPM-2 cells to HUVECs was inhibited by mannose 6-phosphate. Moreover, M6P was found to suppress the adhesion of human myeloma cell lines, OPM-2 and RPMI 8226, to bone marrow stromal cells that was established from the patients with multiple myeloma. In addition, proliferation of OPM-2 was stimulated in response to IGF-II. These results suggest that CIM6P/IGF-II receptor may be functional in terms of supporting cell adhesion and proliferation of myeloma cells.
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PMID:Functional role of cation-independent mannose 6-phosphate/insulin-like growth factor II receptor in cell adhesion and proliferation of a human myeloma cell line OPM-2. 889 22

Mouse monoclonal antibodies MAHI 4 and MAHI 10 reactive with Haemophilus influenzae lipopolysaccharide (LPS), were generated by fusing mouse myeloma cells with spleen cells of mice immunized with H. influenzae strain RM.7004-XP-1. The antibody MAHI 4 reacted in whole-cell enzyme immunoassay (EIA) and colony-dot-immunoblotting with 20 of 123 H. influenzae strains and to a few other human Haemophilus spp. and Neisseria spp., but not to any Bordetella pertussis, B. parapertussis, Aeromonas spp. or Moraxella catarrhalis strains tested. This suggests a specific epitope accessible to recognition in just a few strains. This conclusion was supported by the data on binding of MAHI 4 to only three of 18 H. influenzae LPSs tested, but not to any Haemophilus ducreyi or enterobacterial LPSs. The antibody MAHI 10 bound to 80 of 123 strains of H. influenzae and to a few strains of Neisseria spp. and M. catarrhalis as evaluated by EIA and colony-dot-immunoblotting, which suggests an epitope accessible to recognition in 65% of the H. influenzae strains tested. The antibody MAHI 10 reacted with 10 of 18 H. influenzae LPSs as determined by EIA. By using polysaccharides, obtained after both mild acidic hydrolysis, strong alkali treatment, and dephosphorylation, as inhibitors of the antibodies binding to H. influenzae LPS antigens it was shown that phosphate groups were essential for the binding of MAHI 10 to LPS but they did not affect antigenic recognition by MAHI 4. None of the monoclonal antibodies bound to isolated lipid A, but the aggregation caused by the fatty acids of lipid A was essential for optimum epitope recognition. Enzymatic treatment of homologous LPSs with galactose-oxidase led to products which were between 20 to 30 times less effective as inhibitors of the binding of the MAHI 4 than the native LPSs. Taken together the results indicate that MAHI 4 has the following pentasaccharide as the epitope Gal beta 1-->2 Hep alpha 1-->2Hep alpha 1-->3Hep alpha 1--> Kdo(P). These results emphasize the importance of the terminal beta-Gal residue in the definition of the MAHI 4 specificity, and of the terminal phosphorylated saccharide residues of some of the Haemophilus LPSs for the MAHI 10 specificity.
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PMID:Monoclonal antibodies against Haemophilus influenzae lipopolysaccharides: clone MAHI 4 binding to a pentasaccharide containing terminal beta-Gal residues and clone MAHI 10 recognizing terminal phosphorylated saccharide residues. 893 39

The overall objective of this series of experiments is to generate immunological markers that may elucidate bull sperm surface changes in vitro. Here we report the initial experiments of the study, involving the production and characterization of monoclonal antibodies (mAbs) again bull sperm. BALB/c mice were immunized with phosphate-buffered saline (PBS)-washed whole bull sperm, and their spleen cells were fused with NS-1 myeloma cells in two separate cell fusion experiments, resulting in the generation of 15 mAbs. The mAbs were specific to antigens of either the posterior tail or the head regions of bull sperm and detected five major domains of antigen localization in the bull sperm (apical crescent, equatorial band, principal acrosomal, whole head, and posterior tail). Eleven of the 13 head-specific mAbs recognized intra-acrosomal antigens, whereas 2 mAbs recognized antigens that were localized in the plasma membrane. One mAb specific to the tail region was of the IgM class; the remaining 14 mAbs were of the IgG class. They were all sperm specific, with no cross-reactivity to bovine oocytes or to any of the 12 bovine somatic tissues tested. The mAbs were not species specific, however, because 11, 10, 2, and 1 of the 15 mAbs cross-reacted with sheep, pig, mouse, and human sperm, respectively. None of the mAbs cross-reacted with rooster sperm. The cognate antigens of the 11 tested mAbs were of testicular origin, but several of them showed enhanced binding to epididymal sperm. In western blot analysis, 3 of the 13 mAbs tested identified more than one protein band (40-200 kDa). Seven others recognized proteins of > or = 200 kDa, whereas three mAbs recognized no proteins.
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PMID:Anti-bull sperm monoclonal antibodies: I. Identification of major antigenic domains of bull sperm and manifestation of interspecies cross-reactivity. 895 1


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