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Query: UMLS:C0009443 (cold)
 92,137 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The vibration exposure dose dependency of clinical stage, examination results and symptoms are valuable for evaluation of exposure effect in vibration syndrome. The 1973 national survey of 461 chain saw operators in private forests was reexamined with respect to vibration exposure dose (VD) and clinical stage (Stockholm Workshop scales: CIRP-0 to 3 and SN-0 to 3 stages). VD was calculated by the formula "ahw(eq.4h) x D (days) x Y (years)". Vibration exposure dose index (VDI) was calculated according to the VD level. Subjects were divided into five VDI, four CIRP stage and four SN stage groups, respectively. Ratio of four CIRP and SN in VDI, examination results and prevalences of symptoms were compared between VDI-1 and the other VDI groups. Vibration dose dependency was observed in Stockholm Workshop scales (CIRP and SN stage) and examination results (prevalence of CIRP, vibrotactile perception threshold, prevalence of numbness in hands, and fingertip pinch strength). Higher VDI (VDI-5) was associated with higher prevalence of hypersensitivity to cold, muscle weakness and deterioration of finger function. Which formula is more useful to evaluate cumulative vibration effects is still controversial.
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PMID:Vibration exposure dose dependency of clinical stage, examination results and symptoms in vibration syndrome. 899 29

In response to low ambient temperature, mammalian cells as well as microorganisms change various physiological functions, but the molecular mechanisms underlying these adaptations are just beginning to be understood. We report here the isolation of a mouse cold-inducible RNA-binding protein (cirp) cDNA and investigation of its role in cold-stress response of mammalian cells. The cirp cDNA encoded an 18-kD protein consisting of an amino-terminal RNAbinding domain and a carboxyl-terminal glycine-rich domain and exhibited structural similarity to a class of stress-induced RNA-binding proteins found in plants. Immunofluorescence microscopy showed that CIRP was localized in the nucleoplasm of BALB/3T3 mouse fibroblasts. When the culture temperature was lowered from 37 to 32 degrees C, expression of CIRP was induced and growth of BALB/3T3 cells was impaired as compared with that at 37 degrees C. By suppressing the induction of CIRP with antisense oligodeoxynucleotides, this impairment was alleviated, while overexpression of CIRP resulted in impaired growth at 37 degrees C with prolongation of G1 phase of the cell cycle. These results indicate that CIRP plays an essential role in cold-induced growth suppression of mouse fibroblasts. Identification of CIRP may provide a clue to the regulatory mechanisms of cold responses in mammalian cells.
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PMID:A glycine-rich RNA-binding protein mediating cold-inducible suppression of mammalian cell growth. 915 92

Although the cold-shock responses of microorganisms have been extensively investigated, those of mammalian cells are just beginning to be understood. Recently, CIRP, a member of the glycine-rich RNA-binding protein (GRP) family, has been identified as the first cold-shock protein in mammalian cells. Here, we report that RBM3, another member of the GRP family, is induced in human cells in response to cold stress (32 degrees C). RBM3 transcripts were constitutively expressed in all cell lines examined including K562, HepG2, NC65, HeLa, and T24 cells. In all of them, the transcript levels of RBM3 were increased at 24 h after the 37 to 32 degrees C temperature down-shift. In NC65 cells, the kinetics of RBM3 induction was different from that of CIRP. Protein synthesis inhibitors cycloheximide and puromycin induced RBM3 transcripts, but cadmium chloride, H2O2, ethanol, and osmotic shock had no effect. Combined with the different tissue distribution of expression, these results suggest that RBM3 and CIRP play distinct roles in cold responses of human cells.
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PMID:Increased transcript level of RBM3, a member of the glycine-rich RNA-binding protein family, in human cells in response to cold stress. 924 37

Cold stress induces in microorganisms the synthesis of several proteins that are involved in various cellular processes such as transcription, translation and recombination. Recently, the cold-inducible RNA-binding protein (Cirp) was found to be induced in rodent cells by mild cold stress (32 degrees C). Cirp consists of an N-terminal RNA-binding domain and a C-terminal Gly-rich domain, and plays an essential role in cold-induced suppression of cell proliferation. We report here the cloning of a cDNA encoding an 18-kDa protein with 95.3% identity in an amino-acid sequence to that of mouse Cirp. The human CIRP gene has been mapped to the chromosomal locus 19p13.3 by fluorescence in-situ hybridization. CIRP mRNA is constitutively expressed in all cell lines examined, including K562, HepG2, NC65, HeLa, T24, and NEC8 cells. In all of them, the levels of CIRP mRNA and protein were increased within 12 h after a temperature down-shift from 37 degrees C to 32 degrees C. These results demonstrated that CIRP is a cold-shock protein in human cells. Identification of CIRP may provide a clue to the regulatory mechanisms of cold responses in human cells.
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PMID:Cloning and characterization of human CIRP (cold-inducible RNA-binding protein) cDNA and chromosomal assignment of the gene. 943 72

A presumably full-length cDNA encoding a putative glycine-rich RNA binding protein was isolated from a lambdaZAP cDNA library prepared from mRNAs extracted from needles of 2year old white spruce seedlings, which had been either wounded or jasmonate-treated. The cDNA, designated PgRNP (Picea glauca RNP protein), presents a 468bp open reading frame encoding a 155 amino acid protein. This polypeptide possesses an RNA binding domain (RNP-CS) and a glycine-rich domain. Comparative alignment reveals extensive homologies to glycine-rich RNA binding proteins containing an RNP-CS found in other angiosperm species. Genomic hybridization experiments suggest that the PgRNP gene is part of a small multigene family with at least four members. RNA blot analysis revealed that the PgRNP transcript is expressed in all tissues from non-stressed plants. Constitutive mRNA level was found in needle tissue from control as well as methyl-jasmonate treated plants. Wounding had no clear induction effect. Jasmonic acid treatment and systemic wound response had a positive effect on transcript accumulation. Transcript accumulation was slightly induced by cold in needles, and repressed by drought stress in both needle and root tissues of 2year old plants. Finally, the level of PgRNP accumulation was induced by wounding and repressed in 2week old dark-grown seedlings upon jasmonate treatments.
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PMID:Isolation and characterization of a cDNA clone encoding a putative white spruce glycine-rich RNA binding protein. 1058 Jan 58

Expression of CIRP (cold-inducible RNA-binding protein) is inducible at 32 degrees C in cultured fibroblasts. Because ischemia is known to induce expression of heat shock proteins, its effect on the CIRP expression was examined using the rat transient forebrain ischemia model. The isolated rat CIRP cDNA encoded amino acids 100% identical in its sequence to mouse CIRP. Northern blot analysis revealed that the CIRP transcripts were ubiquitously expressed in various tissues. In situ hybridization histochemistry of normal rat brain revealed the expression of CIRP in neurons in the hippocampus and the cerebral cortex among others. In the hippocampus of postischemic rats, CIRP mRNA level decreased from 3-6 h after the onset of reperfusion, while it did not change in the cerebral cortex. When PC12 pheochromocytoma cells were cultured at 32 degrees C, the CIRP mRNA level was increased. The presence of H2O2 in the culture media inhibited dose dependently this induction as well as constitutive expression, suggesting that the effect of brain ischemia on CIRP expression is related to generation of reactive oxygen species. Further studies are necessary to clarify the roles played by cold shock proteins in the hypothermic therapy of brain damages.
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PMID:Effects of ischemia and H2O2 on the cold stress protein CIRP expression in rat neuronal cells. 1064 16

We have cloned a putative ascidian glycine-rich RNA binding protein gene, CiGRP1. Its maternal transcript and protein are stored in the unfertilized egg. They are gradually decreased during the first few rounds of cleavage. The CiGRP1 zygotic transcript and protein start to accumulate at the gastrula stage. The CiGRP1 transcript is expressed in the brain precursor and mesenchyme precursor cells of the gastrula and the neurula stage, and the brain and mesenchyme cells of the tailbud stage embryo. The CiGRP1 protein is found in all nuclei and in the cytoplasm of brain and mesenchyme cells. Although many glycine-rich RNA binding protein homologs of plants and vertebrates are cold-inducible, CiGRP1 cannot be induced by cold shock or heat shock at the transcriptional and translational levels during embryogenesis. The temporal expression pattern and the tissue-restricted expression pattern of CiGRP1 suggest that it has important roles in the very early stage of development and in the brain and the mesenchyme tissue specification.
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PMID:An ascidian glycine-rich RNA binding protein is not induced by temperature stress but is expressed under a genetic program during embryogenesis. 1067 29

Gene expression of cold inducible RNA-binding protein (CIRP) was examined in the frog. In Xenopus laevis, expression of CIRP (XCIRP) was observed in both brain and liver at 24 degrees C. Circadian expression of XCIRP was observed in brain. Expression of XCIRP in brain was induced by cold treatment and gradually decreased to the control level at 24 degrees C, but no significant changes were observed in liver. Employing the sequence of murine CIRP, bullfrog (Rana catesbeiana) CIRP gene was cloned. The bullfrog CIRP gene, designated BFCIRP, was 706 bp in length and encoded a putative protein of 164 amino acid residues. The deduced protein contained one consensus sequence of RNA-binding domain (CS-RBD) and a glycine rich domain (GRD). The amino acid sequence of BFCIRP was 78.4% identical to XCIRP. Expression of BFCIRP in brain was stronger in winter than that in summer. These findings suggest that BFCIRP expression in brain may link to hibernation.
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PMID:Cloning and characterization of amphibian cold inducible RNA-binding protein. 1081 11

Compared to bacteria and plants, the cold shock response has attracted little attention in mammals except in some areas such as adaptive thermogenesis, cold tolerance, storage of cells and organs, and recently, treatment of brain damage and protein production. At the cellular level, some responses of mammalian cells are similar to microorganisms; cold stress changes the lipid composition of cellular membranes, and suppresses the rate of protein synthesis and cell proliferation. Although previous studies have mostly dealt with temperatures below 20 degrees C, mild hypothermia (32 degrees C) can change the cell's response to subsequent stresses as exemplified by APG-1, a member of the HSP110 family. Furthermore, 32 degrees C induces expression of CIRP (cold-inducible RNA-binding protein), the first cold shock protein identified in mammalian cells, without recovery at 37 degrees C. Remniscent of HSP, CIRP is also expressed at 37 degrees C and developmentary regulated, possibly working as an RNA chaperone. Mammalian cells are metabolically active at 32 degrees C, and cells may survive and respond to stresses with different strategies from those at 37 degrees C. Cellular and molecular biology of mammalian cells at 32 degrees C is a new area expected to have considerable implications for medical sciences and possibly biotechnology.
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PMID:Cold shock response in mammalian cells. 1094 55

We cloned a major isoform of Xenopus homologue of cold inducible RNA binding protein (CIRP), XCIRP-1. XCIRP-1 was neither cold inducible nor essential for cell division during early embryonic development. Suppression of XCIRP-1 dose dependently produced tailbuds with deformations of the brain and internal organs. The defects were XCIRP-1 specific as they could be rescued by sense transcript. Suppression of XCIRP-1 also disrupted the morphogenetic migration of the C3 blastomeres (lineaged to become the embryonic kidney, the pronephros). In animal cap explants, depletion of XCIRP-1 inhibited activin/retinoic acid induced expressions of pronephros related Xlim-1 and WT1 genes. These results suggest that XCIRP-1 is required for the specification and morphogenetic lineage migration of the pronephros.
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PMID:Maternal cold inducible RNA binding protein is required for embryonic kidney formation in Xenopus laevis. 1101 19


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