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)

The usefulness of plasma ribonuclease assays was studied in (i) patients with possible protein deficiency, (ii) patients with myelomatosis, (iii) patients with carcinoma of the breast. In each group, the major factor associated with elevation of plasma ribonuclease was impairment of renal function. The assay was therefore of little value in the assessment of patients with myelomatosis or carcinoma of the breast. However, in the patients with possible protein deficiency and normal renal function, an elevation of plasma ribonuclease is, in general, associated with a decrease in serum albumin, transferrin and cholinesterase. Plasma ribonuclease may therefore be a useful parameter in the assessment of protein nutritional status.
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PMID:An assessment of the clinical usefulness of plasma ribonuclease assays. 97 78

Hybridomas secreting monoclonal antibodies to Nippostrongylus brasiliensis antigens were generated by hybridization of IR983F myeloma cells with spleen cells from Lou/M/Wol rats infected with living third-stage larvae. Antibodies specific either for larval or worm antigens were identified by enzyme-linked immunosorbent assays with Nippostrongylus brasiliensis fragments, homogenates and secretions as antigens. The results demonstrate that all antibodies which recognized larval antigens (38 antibodies) also reacted with worm surfaces. Ten antibodies were specific only for worm antigens. Ten antibodies reacted with worm homogenate, three antibodies recognized components of worm secretion and 17 antibodies combined with acetylcholinesterase. The epitope specificity was investigated by the capacity of various glycosides, aminoacids, N-acetylneuraminic acid and phosphorylcholine to inhibit the binding to worm fragments. The analysis revealed that alpha-methylglucoside, alpha-methylmannoside, N-acetylglucosamine, N-acetylgalactosamine, fucose and the amino acids leucine, phenylalanine, tyrosine, serine, tryptophan did not combine with the antigen-binding sites of the antibodies. Proline, arginine and histidine, however, displayed inhibitory effects. With N-acetylneuraminic acid as inhibitor three groups of antibodies could be discriminated. At a concentration of 10-20 mM, phosphorylcholine was a potent inhibitor for all antibodies.
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PMID:Characterization of antigens of the nematode Nippostrongylus brasiliensis by monoclonal antibodies. 241 42

Hybridomas secreting monoclonal antibodies to Nippostrongylus brasiliensis antigens were generated by fusion of NSI mouse myeloma cells with spleen cells from Balb/c mice which had been immunized either with killed third stage larvae or killed adult worms of N. brasiliensis. Enzyme-linked immunosorbent assays with worm or larvae fragments as antigens revealed that thirteen hybrids produced parasite-specific antibodies. The antibodies reacted with either both worms and larvae or exclusively recognized worm antigens. No antibody was found which solely reacted with larval antigens. Immunofluorescence studies demonstrated that most antibodies homogeneously stained the cuticle of 80-90% of the adult worms and 10-20% of the third stage larvae. The antibodies were further characterized by enzyme-linked immunosorbent assays specific for worm or larvae homogenates and secretions or for acetylcholinesterase from electric eel and bovine erythrocytes. Investigations of the epitope specificity by the inhibition of binding to worm fragments in the presence of various glycosides, N-acetylneuraminic acid and phosphorylcholine revealed that six antibodies reacted with N-acetylneuraminic acid. All antibodies displayed a low affinity to phosphorylcholine.
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PMID:Generation of monoclonal antibodies to characterize antigens of the nematode Nippostrongylus brasiliensis. 242 51

Five hybrid clones secreting antibodies to the neuropeptide substance P have been obtained by somatic cell fusion of mouse myeloma cells with splenocytes from immunized mice of the Biozzi strain. To perform rapid and sensitive screening tests as well as to study the fine specificities of each monoclonal antibody, we developed a new enzyme immunoassay of substance P using acetylcholinesterase as label. All five monoclonal antibodies were directed to the C-terminal pentapeptide of substance P, especially to the Phe7 residue. They cross-reacted with neurokinin A and to some extent with neurokinin B but not with other nontachykinin mammalian peptides. One monoclonal antibody (SP 14) was used for immunocytochemical experiments in the rat spinal cord and spinal ganglion, both at the light and electron microscopic levels. A strong specific neurokinin-like immunoreactivity was observed in cell bodies, nerve fibers, and terminals, with a very low background staining. Finally, the affinities of several analogues of substance P for SP 14 monoclonal antibody were shown to be correlated with their biological activities, as measured by their hypotensive effects in vivo. These findings suggested a strong structural resemblance between the combining site of the antibody and that of the physiological substance P receptor.
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PMID:Monoclonal antibodies to substance P: production, characterization of their fine specificities, and use in immunocytochemistry. 244 14

The clinical usefulness of alkaline phosphatase (ALP) and lactate dehydrogenase (LDH) levels in serum and pathogenetic mechanism of hypoalbuminemia and hypocholesterolemia in multiple myeloma (MM) were investigated. In cases of MM with a history of pathological fracture, the level of serum ALP was significantly higher than normal. Thus, elevated ALP in MM patients may be an indicator of the occurrence of a pathological fracture within the past 2 months. The levels of serum LDH in about 80% of the MM patients were within normal limits despite the presence of a malignant tumor. These patients showed a normal pattern of isoenzymes and more mature types according to the Greipp classification. In contrasts, the patients with elevated serum levels of LDH showed the tumor pattern of the isoenzymes and the plasmablastic type. The total cholesterol concentration was correlated with the total protein levels and the serum cholinesterase. These findings were the same as those in patients with nephrotic syndrome and polyclonal hypergammaglobulinemia without liver dysfunction. These results suggest that the decreased cholesterol in MM is due to a reduction in the synthesis of albumin in the liver.
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PMID:Some problems in the laboratory findings in multiple myeloma. 269 42

Human erythrocyte acetylcholinesterase was used to immunize mice, and hybridomas were generated by fusion of mouse spleen cells with cells of the Sp 2/0 myeloma cell line. Five independently derived hybridoma clones produced antibodies that bound to purified erythrocyte acetylcholinesterase. All of these antibodies crossreacted with human and monkey neuromuscular junctions; immunocytochemical staining patterns corresponded to the distribution of junctional acetylcholinesterase. The monoclonal antibodies fell into at least four categories based on differences in crossreactivity with neuromuscular acetylcholinesterase of rabbit, dog, calf, and guinea pig, and competition tests indicated that the antibodies defined five different antigenic sites on the acetylcholinesterase molecule. It is concluded that there is a high level of homology between the acetylcholinesterases of erythrocytes and neuromuscular junctions.
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PMID:Acetylcholinesterase of human erythrocytes and neuromuscular junctions: homologies revealed by monoclonal antibodies. 617 61

Butyrylcholinesterase purified from human plasma and acetylcholinesterase purified from human red blood cells were used to immunize separate groups of BALB/c mice. A solid-phase immunoadsorbance assay was developed to screen and characterize antibodies specific for the cholinesterases. Immunized spleen cells were fused with a non-immunoglobulin-secreting myeloma cell line (FO). After two subcultures at limiting dilution, several clones secreting antibodies to acetylcholinesterase or butyrylcholinesterase were obtained. Selected clones were expanded as ascites tumors in immunosuppressed BALB/c mice. All tested immunoglobulins consisted of kappa light chains and either G1 or G2b heavy chains. Two-dimensional gel electrophoresis confirmed the monoclonal nature of each isolated antibody. None of the antibodies to acetylcholinesterase cross-reacted with butyrylcholinesterase, and vice versa. All tested antibodies exhibited high avidity for human enzyme, independent of the tissue source (apparent dissociation constants: 1-3 nM for acetylcholinesterase antibodies; 2-13 nM for butyrylcholinesterase antibodies). Treatment of enzymes with monoclonal antibodies increased the sedimentation coefficients (from 6.5 S to 12 S for acetylcholinesterase, from 11 S to 18 S or 20 S for butyrylcholinesterase). All of the monoclonal antibodies displayed marked species specificity. Several antibodies reacted only with human enzyme; others reacted with enzyme from nonhuman primates as well. A few of the butyrylcholinesterase antibodies cross-reacted weakly with enzyme from dog, cat, and horse, but none reacted with the enzyme from rat, guinea pig, and chicken. One acetylcholinesterase antibody cross-reacted with acetylcholinesterase of rabbit and guinea pig. The avidity, species selectivity, and other properties of these antibody reagents will be useful in future studies on the regulation and disposition of cholinesterases.
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PMID:Production and characterization of separate monoclonal antibodies to human acetylcholinesterase and butyrylcholinesterase. 619 17

The study included 82 patients with multiple myeloma (MM) to evaluate the diagnostic and prognostic significance of correlation between of levels of ceruloplasmin (CP), acetylcholinesterase (ACE) and total proteolytic activity (TPA) in blood serum and immunochemical pattern, tumor mass and response to chemotherapy. It was shown that CP, ACE and TPA determination may be used as additional markers to confirm therapeutic benefits, to timely detect relapse and to verify resistance to chemotherapy. It was also demonstrated that resultant decrease in CP and TPA and increase in ACE levels are reliable indicators of changes developing in MM course and remission fulfillment. High values for CP and low ones for ACE point to pathological activity. Both diagnostic and prognostic significance of the indices has been shown. The highest levels of CP and TPA in blood serum were identified in cases of A-myeloma and myeloma of Bence Jones while ACE concentrations in those patients were lower than in G-myeloma which correlated with median survival. Application of said assays might improve diagnosis, management and prognosis of MM.
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PMID:[Diagnostic and prognostic significance of blood-serum ceruloplasmin, acetylcholinesterase and total proteolytic activity in patients with multiple myeloma]. 1053 99