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)

Mouse myeloma immunoglobulin IgM heavy chains were cleaved with cyanogen bromide into nine peptide fragments, four of which contain asparagine-linked glycosylation. Three glycopeptides contain a single site, including Asn 171, 402, and 563 in the intact heavy chain. Another glycopeptide contains two sites at Asn 332 and 364. The carbohydrate containing fragments were treated with Pronase and fractionated by elution through Bio-Gel P-6. The major glycopeptides from each site were analyzed by 500 MHz 1H-NMR and the carbohydrate compositions determined by gas-liquid chromatography. The oligosaccharide located at Asn 171 is a biantennary complex and is highly sialylated. The amount of sialic acid varies, and some oligosaccharides contain alpha 1,3-galactose linked to the terminal beta 1,4-galactose. The oligosaccharides at Asn 332, Asn 364, an Asn 402 are all triantennary and are nearly completely sialylated on two branches and partially sialylated on the triantennary branch linked beta 1,4 to the core mannose. The latter is sialylated about 40% of the time for all three glycosylation sites. The major oligosaccharide located at Asn 563 is of the high mannose type. The 1H-NMR determination of structures at Asn 563 suggests that the high mannose oligosaccharide contains only three mannose residues.
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PMID:Major carbohydrate structures at five glycosylation sites on murine IgM determined by high resolution 1H-NMR spectroscopy. 408 5

Gel filtration analysis of the urinary proteins of some patients with myeloma has shown the presence of "fragments" of Bence Jones proteins which correspond to the variable half of these proteins. Experiments have been carried out to establish the origin of a "fragment" observed in a patient who excreted a large amount of this protein. Labeled homologous Bence Jones protein has been injected into this and other control patients. Excretion of labeled "fragment" has been observed in all. Analysis by peptide mapping and radio-autography of this labeled "fragment" isolated from the urine showed that the invariable half of the Bence Jones protein was not excreted; it seemed thus likely that the invariable half was metabolized to small peptides and free amino acids. A labeled Bence Jones protein which was excreted without any accompanying "fragment" was injected into the patient who excreted large amounts of "fragment." No excretion of labeled "fragment" was observed. It was thus concluded that the property of being degraded to "fragment" is characteristic of some "fragile" Bence Jones proteins and is not determined by the patient. Incubation with serum or urine of the "fragile" Bence Jones protein failed to produce any "fragment." "Fragments" of Bence Jones proteins are thus most likely formed during excretion of these proteins through the kidney and are products of the catabolism of Bence Jones proteins.
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PMID:Catabolic origin of a Bence Jones protein fragment. 566 62

Hybridomas have been prepared by fusing mouse myeloma (P3 X 63 Ag8) cells with spleen cells of mice immunized with a yeast fraction enriched with respect to non-ribosomal translational components. Cloned hybridoma lines were grown in the form of ascites tumors, and the monoclonal antibodies produced were purified from the ascites fluid by chromatography on DEAE-Affi-Gel Blue. One of the antibodies, from a hybridoma cell line designated as PSH-1, inhibited the translation of natural mRNA and poly(U) and polysomal chain elongation in a cell-free protein-synthesizing system from yeast. Resolution and partial purification of the elongation factors indicated that the monoclonal antibody from PSH-1 did not interact with EF-1 or EF-2 but reacted with and inactivated EF-3, the 125 000 molecular weight additional elongation factor specifically required with yeast ribosomes. The EF-3 purified from the cytosol by immunoaffinity chromatography was comparable to that prepared by ion-exchange chromatography. Evidence was obtained which indicated that EF-3 was essential for the translation of natural mRNA as well as poly(U), was associated with polysomes but not ribosomal subunits, and was required for every cycle in the elongation phase of protein synthesis.
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PMID:Monoclonal antibody specific for yeast elongation factor 3. 638 May 81

A 55-year-old man presented with nerve compression and examination of tissue removed by laminectomy, and bone marrow aspiration was diagnostic of multiple myeloma. Protein studies showed a total serum protein of 5.7 g/dL, with a M-component in the fast beta region. The abnormal protein reacted only with anti-lambda antisera but not with antisera from multiple sources in four different laboratories, against known heavy chain and kappa-chain determinants. A marked difference in potency of commercial anti-lambda antisera was noted. The reaction was primarily demonstrable in serum and present only in 100-times concentrated urine. Gel filtration disclosed a molecular weight of 84,000. The patient has been followed for the past four years and has not demonstrated significant proteinuria. The English and Japanese literature records seven cases of tetrameric Bence Jones multiple myeloma or plasma cell dyscrasia. This case appears to be the eighth recorded cases of tetrameric Bence Jones proteinemia, the fifth case without proteinuria, and the fifth case involving lambda light chains.
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PMID:Polymeric (presumed tetrameric) lambda Bence Jones proteinemia without proteinuria in a patient with multiple myeloma. 643 10

Major controversies exist in the literature on the presence of blood group antigens on the endothelial and stromal layers of the cornea, and the importance of major histocompatibility typing for keratoplasty. Antibodies were raised in BALB/C mice against water soluble proteins of corneal epithelium. Following fusion of spleen cells with myeloma cells (Sp2/0-Ag14) hybrid colonies were maintained in HAT selective medium. The supernates of each colony were measured and screened for antibody production by radioimmunoassay. Gel electrophoresis of the antigen showed nine major bands. The antibodies were partially characterized by cross reaction against other soluble corneal fractions.
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PMID:Production of hybridomas secreting antibodies to the cornea. 729 1

Comparative studies of the N-linked carbohydrate chains of human myeloma proteins of the IgA1 and IgA2 subclasses were performed. The N-linked carbohydrate chains were released by hydrazinolysis from the polypeptide backbone, converted to radioactive oligosaccharides by sodium borotritide reduction after N-acetylation and separated into one neutral and two acidic fractions by paper electrophoresis. The acidic oligosaccharides were completely converted to neutral oligosaccharides by sialidase treatment, indicating that they were sialyl derivatives. The neutral and sialidase-treated acidic oligosaccharides were further fractionated by Bio-Gel P-4 column chromatography. Structural studies of each oligosaccharide by sequential exoglycosidase digestion and methylation analysis revealed that human myeloma IgA proteins contained significant amounts of biantennary complex-type carbohydrate chains in addition to a small amount of the high mannose-type. The results indicated that the oligosaccharide structures of human IgA1 and IgA2 display a high degree of heterogeneity not only in the number of carbohydrate chains, but also in their composition.
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PMID:Carbohydrate heterogeneity of human myeloma proteins of the IgA1 and IgA2 subclasses. 782 67

This study characterized the N-glycans of a humanized immunoglobulin G4 (IgG4) expressed in NS/O mouse myeloma cells and directed against the CD18 family of adhesion-promoting receptors on leukocytes. The N-glycans were released from the purified recombinant IgG by N-glycanase treatment, purified by Sephadex G50 chromatography, and fractionated by Bio-Gel P-4 chromatography into three oligosaccharide pools. Each pool was analyzed individually by glycosyl composition analysis, high-pH anion-exchange chromatography with pulsed amperometric detection (HPAEC-PAD), 600-MHz 1H-NMR spectroscopy, and electrospray-ionization mass spectrometry. In addition, each of the three pools was subfractionated by HPAEC and the isolated subfractions that contained sufficient material were hydrolyzed and analyzed for glycosyl composition by HPAEC-PAD. The overall results indicate the presence of five oligomannoside-type structures (containing 5 to 8 Man residues) which are not usually found in IgG, and the presence of eight diantennary (mostly truncated) N-acetyllactosamine-type structures which are typical of mouse and human IgGs. The N-acetyllactosamine-type structures were heterogeneous with regard to alpha(1-->6) fucosylation of the linkage GlcNAc, and the presence or absence of GlcNAc and/or Gal beta(1-->4)GlcNAc extending the core pentasaccharide (Man3GlcNAc2). No evidence was found for the presence of sialic acid or bisecting GlcNAc residues on the N-acetyllactosamine-type chains. The latter finding suggests that the N-glycans of this humanized IgG are of the mouse type.
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PMID:Structural characterization of the N-glycans of a humanized anti-CD18 murine immunoglobulin G. 790 4

Monoclonal antibodies against purified urease (EC 3.5.1.5) from Canavalia ensiformis were raised by hybridoma technology using Sp2/0 myeloma cells as a fusion partner. All culture wells exhibited hybrid growth and 25% of these (ie 45 culture wells) contained anti-urease activity. Two positive hybrid cells were cloned twice by the limiting dilution method and three hybridoma clones (B6F, C4F and B18) secreting monoclonal antibodies were selected at random for purification and characterisation purposes. All three cell lines secreted monoclonal antibodies of IgM class which were purified by gel filtration chromatography on Sephacryl S-200 column with a final recovery of 85% and a purification factor of about 18. The purified preparations were apparently homogeneous on native PAGE running with a M(r) of 920,000 Da. mAbs were highly specific for jack bean urease as determined by Western blotting. The affinity constants (K) for these mAbs ranged from 10(8) to 10(9) l mol-1. mAb B6F inhibited about 65% of urease activity whereas C4F and B18 stimulated the enzyme activity slightly by 20%. The presence of 2-mercaptoethanol in incubation mixtures protected urease from inactivation by B6F. Urease inactivation by B6F could be reversed by addition of 2-mercaptoethanol which reactivated most of the partially inactive enzyme. Gel filtration chromatography of purified urease exhibited two protein peaks with M(r) values of 290,000 and 90,000 Da which revealed antibody activity. This result suggests that the mAb B6F recognizes the trimeric as well as the monomeric forms of urease.
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PMID:Monoclonal antibodies against urease from Canavalia ensiformis. 812 99

Agarose Gel Serum Electrophoresis is a simple, rapid and sensitive technique routinely used for diagnosis of Multiple Myeloma. Its effectiveness as a screening tool for detecting infraclinical cases of Multiple Myeloma is brought out in this study. 29 out of the 219 patients presenting with unexplained osteoporosis and pain are found to be positive for M proteins. These patients were earlier adjudged organic disease free after preliminary investigation and examination.
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PMID:A simple screening procedure for detection of infraclinical cases of multiple myeloma. 815 15

1. In order to explore the significance of brain natriuretic peptide (BNP), a cardiac hormone secreted from the ventricle, in mice, we prepared a monoclonal antibody against mouse BNP (mBNP) and established a specific radioimmunoassay (RIA) for mBNP. 2. A monoclonal antibody, KY-mBNP-I, was prepared by the fusion of mouse myeloma cells X63-Ag8.653 with spleen cells of the BALB/c mouse immunized with synthetic mBNP[108-121] conjugated to bovine thyroglobulin. KY-mBNP-I belonged to an IgG2a subclass and showed a high affinity for mBNP (Ka = 1.8 x 10(11) mol/L-1). 3. The RIA established that using KY-mBNP-I was highly sensitive and specific for mBNP, with an IC50 value of 3 fmol/tube and cross-reactivities of less than 0.003% with related natriuretic peptides. mBNP-like immunoreactivity (mBNP-LI) was detected in the mouse atrium (0.35 +/- 0.02 nmol/g), ventricle (20.5 +/- 0.5 pmol/g) and kidney (0.50 +/- 0.05 pmol/g), but not in other tissues including brain. 4. Gel filtration analysis revealed that the major component of tissue mBNP-LI was co-eluted with synthetic mBNP[77-121], a 45-amino acid mature peptide. 5. The monoclonal antibody and RIA for mBNP established here will provide useful tools to investigate the functional significance of BNP in mice, coupled with the genetic engineering approach.
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PMID:Preparation of a monoclonal antibody against mouse brain natriuretic peptide (BNP) and tissue distribution of BNP in mice. 907 48


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