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)

In order to test the concepts that aminoacyl-tRNAs in plasmacytomas may on the one hand modulate the protein synthesized or on the other hand reflect the structure of the synthesized protein, the RPC-5 chromatographic profiles of aminoacyl-tRNAs for all 20 amino acids were studied in tRNA prepared from normal mouse liver and 11 plasmacytomas. The patterns of isoaccepting tRNA were compared with the structure of the myeloma protein being synthesized. The elution profiles of aminoacyl-tRNAs for nine of the amino acids were constant, i.e. they were the same for liver and all plasmacytomas. Significant variability was observed in the profiles of the other 11 families of aminoacyl-tRNAs: asparagine, serine and tryptophan, had peaks of isoaccepting tRNAs found in tumors and not in liver; glutamic acid, histidine and lysine, had different patterns of aminoacyl-tRNAs in plasmacytomas which could be distinguished from the elution profile of liver; and isoleucine, proline, threonine and tyrosine, showed pattern variability in only a few of the tumors. Valyl-tRNA uniquely had one isoacceptor present in liver but absent in the tumors. This variability is thought to be associated with different posttranscriptional modification of the tRNAs rather than regulation of individual tRNA genes in response to particular amino acid sequences in secreted myeloma proteins. Similarily, the lack of correlation of isoacceptors with sequence differences makes the modulation of protein fine structure by tRNA availability unlikely.
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PMID:Transfer ribonucleic acids from eleven immunoglobulin-secreting mouse plasmacytomas. Constant and variable chromatographic profiles compared with the myeloma protein sequences. 25 44

The low molecular weight RNAs in the nucleus and cytoplasm of mouse myeloma cells have been characterized. There are major nuclear species (other than 5-S and tRNA), four of which contain 'capped' 5' termini. There are three major small cytoplasmic RNAs none of which contain 'caps'. The biosynthesis of the nuclear species when studied using [3H]adenosine as an RNA precursor is characterized by a rapid, transient appearance in the cytoplasm, followed by fixation in the nucleus. Within 15 min, the amount in the cytoplasm has reached a steady-state level maintained for 60 min, while the accumulation in nuclei is linear after a short lag (less than 5 min). When biosynthesis is studied using [Me-3H]methionine as a precursor, much less labeled RNA is present in the cytoplasm, suggesting that methylation may immediately precede fixation into the nucleus.
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PMID:Biosynthesis of low molecular weight RNA in mouse myeloma cells. 73 84

The major valine acceptor tRNA1Val from rabbit liver was purified and its nucleotide sequence determined by in vitro [32P] - labeling with T4 phage induced polynucleotide kinase and finger-printing techniques. Its primary structure was found to be identical with the major valine tRNA from mouse myeloma cells. According to the wobble hypothesis this tRNA, which exclusively has an IAC anticodon, should decode the valine codons GUU, GUC and GUA only. However, this tRNA recognizes all four valine codons with a surprising preference for GUG. It is unknown whether this is due to the lack of A37 modification next to the 3' end of the anticodon IAC. The nature of the inosine-guanosine interaction remains to be clarified.
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PMID:Rabbit liver tRNA1Val:I. Primary structure and unusual codon recognition. 89 81

This paper describes the derivation of the primary structure of the major valine tRNA in the cytoplasm of mouse myeloma cells. Approximately 75% of the nucleotide sequence of this tRNA is also shared by the tRNA1-Val of yeast, this homology serving as a further indication of the extreme conservation of the structures of the tRNAs of different eukaryotic organisms. A novel feature of mouse myeloma tRNA1-Val is its loop IV sequence: -U-PSI-C-G-M1A-A-A-. This particular loop IV sequence has not previously been found in a tRNA structure. In addition, tRNA1-Val possesses some unusual nucleoside modifications. 5-Methyluridine (T) was not found to occur within loop IV of this tRNA, although this minor nucleoside is also absent from certain other mammalian tRNAs. Only one other tRNA, mammalian tRNAf-Met, has been found to possess 2-methylguanosine (m2G) in the position between the (b) and (c) stems of the cloverleaf. Numerous tRNAs have m2-2G in this location, and it would appear that the second methylation of this guanosine is characteristically absent from certain mammalian tRNA species.
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PMID:The primary structure of the major cytoplasmic valine tRNA of mouse myeloma cells. 109 87

The major form of methionine tRNA operational in the elongation of protein synthesis in mouse myeloma cells was purufied from these cells after they had been cultured in the presence of [32P]-phosphate. This [32P]tRNA4-Met species was then digested with T1 RNase or pancreatic RNase so as to obtain both complete and partial RNase digestion products. The nucleotide sequences of these fragments were analysed to enable the derivation of the complete primary structure of this tRNA. tRNA4-Met of mouse myeloma cells is 76 nucleotides in length and contains 15 modified nucleotides. It is the only tRNA yet sequenced which has been found to possess the minor nucleoside 2-methylguanosine (m2G) within the amino acid (a) stem, and also to have an anticodon (c) stem of only 4 and not 5 base-pairs. The loop IV sequence of eukaryotic initiator methionine tRNA (tRNAf-Met) species, -A-U-C-G-m1A-A-A-, IS NOT FOUND IN TRNA4-Met and is therefore absent from at least one of the methionine tRNAs functioning in polypeptide elongation in mammalian cells. This is consistent with the suggested importance of this loop structure in the initiator function of tRNAf-Met in eukaryotic organisms. Three distinct regions of the tRNA cloverleaf, the (b) stem, the anticodon loop (loop II), and loop III, are substantially conserved in structure between tRNAf-Met and tRNA4-Met of mouse myeloma cells. These regions of the structures of mammalian methionine tRNAs probably do not determine whether a certain tRNA-Met will function in the initiation or elongation of protein synthesis, although they might be important in tRNA-Met recognition if the different cytoplasmic tRNA-Met species of mammalian cells are aminoacylated by a single activating enzyme.
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PMID:The nucleotide sequence of a methionine tRNA which functions in protein elongation in mouse myeloma cells. 116 34

Several methods of preparing low molecular weight RNA from chick embryo chromatin have been examined. Traditional methods for dissociating chromatin utilizing high concentrations of salt (greater than 2 M) followed by high-speed centrifugation resulted in very low yields of RNA. Increased yields of RNA were obtained by treating chromatin at lower salt concentration (0.2-0.5 M). By using low salt extraction and sodium dodecyl sulfate-phenol deproteinization, six to eight low molecular weight homogeneous RNA species were isolated from chick embryo chromatin and mouse myeloma chromatin. In the myeloma system, all these RNAs are metabolically stable. Each component is homogeneous as examined by gel electrophoresis and hybridizes with mouse DNA at a rate consistent with a single species. There are multiple gene copies for these RNA species in the mouse genome, varying from 100 to 2000 copies for the different species. One of these RNAs is identical with 5S rRNA. In addition, the redundancy of genes for 18S, 28S, and 5S rRNA and tRNA was determined. Approximately 300 copies for 18 and 28S rTRNA and 500 copies for 5S rRNA were found. tRNAs were on an average 110-fold redundant with about 55 different species measured.
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PMID:Low molecular weight RNA species from chromatin. 117 46

A rapid and efficient procedure for isolating homogeneous beef liver phenylalanyl-tRNA synthetase (EC.6.1.1) was developed that enables to purify the enzyme 5000 fold and to achieve the activity of 8 e.a.u. per mg of protein. The molecular mass of the native enzyme was estimated to be 260 kDa, for alpha subunit - 59 kDa, and for beta - 72 kDa. Two cellular clones were derived by means of hybridization of immunised splenocytes with myeloma cells. They secrete monoclonal antibodies, designated P6 and P1 2, that bind to human placental and bovine liver phenylalanyl-tRNA synthetases but not to the same enzymes from E. coli and T. thermophilus. P6 and P1 2 antibodies do not affect the aminoacylation capacity of human or bovine phenylalanyl-tRNA synthetases. By immunoblotting, it was shown that P6 antibodies recognize the alpha subunit of the enzyme.
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PMID:[Express method of isolation of mammalian phenylalanine-tRNA-synthetase and preparation of monoclonal antibodies against this enzyme]. 220 92

Synthesis of alpha- and beta-globin RNA in DMSO-induced Friend's erythroleukemia cells and synthesis of immunoglobulin gamma- and kappa-chain RNA, total RNA, 5S RNA, and tRNA in mouse myeloma cells (MPC-11) was inhibited by gamma-irradiation. For all RNA species, synthesis decreased nearly exponentially as a function of radiation dose, whereas RNA size distributions, turnover rates, and specific activities of radioactively labeled RNA were affected only insignificantly. D37 values for the loss of synthesis of various RNA species correspond to target sizes ranging from 21,000 to 53,000 kd, or 30-80 kbp of DNA. These target sizes are several-fold larger than the structural genes in question; however, they correspond well with the size of DNA loops, or "domains" constrained by the nuclear matrix. The data suggest that the eukaryotic transcription unit is the torsionally constrained chromatin loop, transcription of which may be inactivated, or significantly reduced by a DNA single-strand break.
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PMID:Structure of transcriptionally active chromatin: radiological evidence for requirement of torsionally constrained DNA. 247 70

Methoxyamine reacts selectively with tRNA molecules at certain exposed cytosine residues usually located in non base-paired regions of the two dimensional clover leaf structure. Here methoxyamine is used for the first time in a study of a mammalian tRNA structure. One of the sequence abnormalities of myeloma initiator tRNA is a cytosine instead of the usual uracil immediately preceding the anticodon. A study of the reaction of the cytosine residues with methoxyamine indicates that the accessibility of bases to chemical reagents in the anticodon loop of this mammalian initiator tRNA is very similar to that observed for the bacterial initiator tRNA.
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PMID:The selective reaction of methoxyamine with cytidine residues in mammalian initiator transfer ribonucleic acid. 1079 58

This paper describes an attempt to find a difference between the patterns of methylation of E. coli tRNA by extracts of two mouse tissues. Two samples of tRNAs, methylated in two separate experiments with extracts of myeloma and of liver in presence of either 14C or 3H S-Adenosyl-L-Methionine, were pooled and fractionated together on a RPC column. The results show a difference in the specificities of the two extracts. Chromatography on DEAE Sephadex suggests that the tRNA Met is methylated by the enzymes on the myeloma, while enzymes from liver react very little, if at all, with that particular tRNA species. Studies have been undertaken in order to find out whether similar differences can also be demonstrated in homologous systems.
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PMID:??? 1194 21


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