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)

Nephrotoxicity due to injection of uro-angiographic water soluble contrast media is a wellknown hazard in patients with renal failure, diabetes mellitus, cardiovascular disease, multiple myeloma and old age. Cases of nephrotoxicity in other patient populations are extremely rare. In order to document the influence of water soluble contrast media in patient undergoing intravenous urography diuresis, osmolar changes, creatinine clearance, absolute urinary creatinine excretion and uric acid metabolism were evaluated before and after contrast medium injection. No adverse reaction could be evidenced as far as the renal function is concerned, as creatinine clearance and absolute urinary creatinine output values showed no significant differences. The significant raise (p less than or equal to 0.001) of uric acid excretion (absolute urinary uric acid excretion values before and after contrast injection were respectively 5.22 micrograms/min.kg (IR: 3.24) and 10.68 micrograms/min.kg (IR: 4.03] can be co-responsible for adverse reactions when the renal function is not normal.
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PMID:Evaluation of renal function before and after intravenous injection of uroangiographic water soluble contrast media in men. 263 82

Spin-label 14C-TEMPO-dichlorotriazine distribution in Fab- and Fc-fragments of monoclonal myeloma immunoglobulin IgG (lambda) 1 Bel, in their heavy and light chains, and tryptic fragments of chains was investigated. Radio-active spin label in proteolytic Fab- and Fc-fragments, in heavy and light chains, and in separate peptides was detected. 3 cm and 2 mm band ESR spectra of spin-labeled IgG in water solutions was studied. It was shown that the models of highly anisotropic motion, isotropic motion and slow isotropic motion of spin label around globule or the description of experimental ESR spectra of TEMPO-dichlorotriazine spin-labeled immunoglobulins do not work.
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PMID:[Distribution of the tempo-dichlorotriazine spin label in the immunoglobulin molecule]. 283 41

While in carps kept in warm water (28 degrees C) and immunized with a human myeloma protein a challenge leads to an increase, the antibody titres in carps kept in cold water (14 degrees C) are changed only unsignificantly. Antibody titres of carps immunized once respectively three times and kept in cold water are not markedly different. In testing the specificity of the antisera taken from each of the three groups no differences could be recognized. With carp anti-IgGZei sera using the passive hemagglutination inhibition test a paraprotein characterizing determinant (s) is just as well demonstrable as by using a rabbit antiserum.
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PMID:[Specificity of carp antihuman myeloma protein sera depending on the holding temperature]. 293 21

To investigate the direct toxicity of human Bence Jones protein (BJP), individual nephrons of male Sprague-Dawley rats were perfused in vivo at 20 nl/min with an artificial tubule fluid (ATF) that contained no protein, a human kappa BJP (5 g/dl), or bovine serum albumin (5 g/dl), and proximal convoluted tubule function and morphology were examined. Perfusion with BJP perfusate for less than or equal to 5 minutes produced no changes (P = NS) in absorption of water, Jv, (1.09 +/- 0.20 vs. 1.50 +/- 0.25 nl/min/mm), chloride, JCl, (95 +/- 47 vs. 123 +/- 41 pEq/min/mm), and glucose, JG, (39 +/- 3 vs. 40 +/- 5 pmol/min/mm) compared to perfusions with only ATF. However, perfusion for at least 20 minutes with the same BJP perfusate produced decreased (P less than 0.025) in Jv (0.58 +/- 0.12 vs. 1.15 +/- 0.14 nl/min/mm) and JG (27 +/- 3 vs. 38 +/- 3 pmol/min/mm) compared to perfusions with ATF alone; the decrease in JCl (64 +/- 47 vs. 119 +/- 27 pEq/min/mm) did not reach statistical significance. Perfusion for 20 minutes with ATF containing albumin resulted in no changes in Jv (1.22 +/- 0.21 vs. 1.15 +/- 0.14 nl/min/mm), JCl (207 +/- 29 vs. 119 +/- 27 pEq/min/mm), and JG (31 +/- 1 vs. 38 +/- 3 pmol/min/mm), when compared to the ATF perfusions. Immunocytochemistry, immunofluorescence and immunoelectron microscopy of the BJP-perfused tubules demonstrated the kappa light-chain protein in endosomes and activated lysosomes. In addition, cellular desquamation and fragmentation, prominent cytoplasmic vacuolation, and focal loss of the microvillus border were found in the BJP-perfused tubules, but not in the albumin-perfused tubules. In conclusion, these functional and morphologic data show that a human kappa light-chain is toxic to the proximal convoluted tubule of the rat. This toxicity occurred in a time-dependent fashion when the lysosomal system was markedly activated. Direct damage of the tubule epithelium by BJP's may be involved in the development of the tubulointerstitial nephropathy associated with multiple myeloma.
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PMID:Human Bence Jones protein toxicity in rat proximal tubule epithelium in vivo. 312 60

A novel myeloma paraprotein has been isolated from a horse with a lymphoid tumor. The protein was a euglobulin and consequently was readily isolated from serum in pure form and high yield by simple dilution in distilled water. The purified intact protein had a molecular weight of 150,000 and was composed of heavy and light chains, both of which had blocked amino-termini and were thus not susceptible to amino-terminal sequence analysis. The amino acid compositions of these respective chains corresponded to those of comparable chains from immunoglobulins of other species. Peptide maps of paraprotein light chains prepared by high pressure liquid chromatography corresponded in part to those of normal pooled equine light chains. The identification of this paraprotein as an equine AI (aggregating immunoglobulin) protein was confirmed by serological analysis using a specific antiserum. The relationship of this particular protein to other members of the immunoglobulin family was further demonstrated by the production of an anti-idiotypic antiserum individually specific for this molecule.
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PMID:Characterization of a homogeneous paraprotein from a horse with spontaneous multiple myeloma syndrome. 312 40

We have established a monoclonal antibody (MoAb) AM34 (IgG1) which was prepared by a hybridoma constructed from fusion between murine myeloma cells and murine splenocytes. Crude amyloid proteins which were used as immunogen, were extracted from the kidney of a patient with rheumatoid arthritis by the distilled water method. This antibody strongly reacted with all 8 cases of secondary amyloidosis, but did not react or very weakly reacted with 17 tissue sections of primary or myeloma-associated amyloidosis. Other amyloid tissues did not give any positive reaction. Interestingly, 6 brain tissues of Alzheimer's disease clearly showed positive staining with this antibody, whereas two apparently normal brain tissues exhibited negative staining. Senile plaque cores, neurofibrillary tangles (weakly stained) and cerebrovascular amyloid in Alzheimer's disease were stained. Absorption of the MoAb AM34 with the crude amyloid proteins abolished the immunoreactivity of the MoAb AM34 not only with the kidney tissue section of the secondary amyloidosis, but also with the above mentioned portions of the brain in the case of Alzheimer's disease. Therefore, these immunohistological data suggest that the MoAb AM34 recognizes common epitope which exists in amyloid deposits of both secondary amyloidosis and Alzheimer's disease. An inhibition test on the kidney section showed that the reactivity of MoAb AM34 was not at all inhibited by the pretreatment of the section with 10 times higher concentration of anti-human amyloid A (AA) MoAb KM268 which was prepared against synthetic peptides of AA protein, suggesting that MoAb AM34 might react with amyloid-related protein other than AA protein. In addition, MoAb KM268 did not react with any lesions in Alzheimer's disease.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Detection of novel proteins associated with secondary amyloidosis and Alzheimer's disease by monoclonal antibody. 320 35

Legionellae are widely spread in natural and man-made habitats. In many instances contaminated tap water has been linked to sporadic or endemic cases of human pulmonary infections, but it is not known why, in spite of frequent occurrence, legionellae only rarely cause disease. Monoclonal antibodies against Legionella pneumophila serogroup 1 (Philadelphia 1) were prepared in order to distinguish between subtypes of this serogroup. Balb/c mice were immunized i.v. three times with heat inactivated bacteria. Antibody formation was detected by an enzyme-linked immunosorbent assay (ELISA) technique using peroxidase-conjugated antimouse IgG. Spleen cells were then fused with NS-1 myeloma cells and cloned by limiting dilution. Four monoclonal antibodies were studied in detail. The study included 47 strains of L. pneumophila: 19 strains were of human origin and 28 were isolated from different environmental sources. Most were from tap water, but none from natural habitats. All strains belonged to serogroup 1 as defined by direct immunofluorescence (DFA) using monospecific FITC-labelled polyclonal antisera from rabbits. The strains were further characterized by beta-lactamase production, activity of catalase, oxidase and proteases, analysis of ubiquinones, and demonstration of membrane protein patterns by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. A strong homogenicity between all the strains could be revealed by these methods independent of their origin. One of the monoclonal antibodies (B-1) was able to distinguish between human and environmental isolates. Eighteen of the 19 human strains reacted very strongly in DFA using antimouse immunoglobulin. No reaction, however, was seen with all of the environmental strains. Immunoblots were performed for characterization of the distinguishing feature using membrane complexes of all strains on nitrocellulose strips. The blots were incubated with antibody B-1, and immune complexes were detected by 125I-protein A. Broad intense blackening was seen between 22 and 70 kilodalton. This result suggests that no single protein, but rather a smaller component such as an oligosaccharide attached to constituents of different molecular weights, might be responsible for the discriminating reaction.
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PMID:Discrimination between clinical and environmental strains of Legionella pneumophila by a monoclonal antibody. 353 65

In order to standardize a radioimmunoassay of milk progesterone as a routine method for confirmation of oestrus and diagnosis of pregnancy in water buffalo, monoclonal antibodies against progesterone were produced. Hybridomas were prepared by fusing spleen cells from a Balb/c mouse immunized with progesterone 11 alpha-hemisuccinate-bovine serum albumin conjugate with the mouse myeloma cell line NS-1. Thirty wells out of 94 secreted anti-progesterone antibodies. Of the ten independent hybridomas derived, one (AF65) was suitable for the quantification of milk progesterone by radioimmunoassay. The tracer used in the assay was progesterone-11 alpha-hemisuccinate [( 2-125I]iodohistamine). The sensitivity of the assay was 50 pg/tube. The mean progesterone concentration at oestrus was 0.8 +/- 0.2 ng/ml increasing to 8.5 +/- 0.8 ng/ml 24 d later in pregnant animals.
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PMID:Use of monoclonal antibodies for radioimmunoassay of water buffalo milk progesterone. 369 28

Cerebrospinal fluid (CSF) involvement in myeloma is rarely seen. Recently we experienced a case with this lesion. A 70-year-old man developed consciousness level disorder during the course of bronchopneumonia. Neurological examination revealed stuporous consciousness, neck stiffness and Kernig's sign. Immunoelectrophoresis showed monoclonal IgG in serum. CSF which was obtained through lumbar puncture was clear and its pressure was 155 mm H2O. It contained 207 white cells/3 mm3; glucose, 54 mg/dl; and protein, 33 mg/dl. The differential count of the CSF was (in %) monocytes, 48.0; plasma cells, 25.5; neutrocytes, 15.5; and lymphocytes, 11.0. Cytoplasm and nucleus of the plasma cells were in various sizes. Some irregular multiple nuclei, flaming cells and grape cells were also observed in them. The cytoplasm of the plasma cells fluoresced with antisera against lambda chains IgG. The value of immunofluorescent technique in identifying plasma cells in the CSF is emphasized.
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PMID:[Abnormal cerebrospinal fluid plasma cells in a case of myeloma]. 371 84

Molecules of normal mouse IgG are oriented horizontally in monolayers at air-water interface unlike the molecules of mouse IgG1 kappa secreted by MOPC-21 myeloma which have vertical orientation. Sodium desoxycholate processing of both preparations at concentrations below the critical micelle concentration resulted in abnormal IgG1 kappa preservation and normal IgG acquisition of vertical orientation in monolayers. When sodium desoxycholate was used for IgG modification at concentration higher than the critical micelle concentration both normal and abnormal IgG had horizontal orientation in monolayers.
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PMID:[Changes in the orientation of mouse myeloma immunoglobulin G in monolayers after treatment with sodium deoxycholate]. 381 42


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