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

Fibronectin (FN; also called large external transformation-sensitive [LETS] protein or cell-surface protein [CSP]) is a large cell-surface glycoprotein that is frequently observed to be either absent or greatly reduced on the surfaces of malignant cells grown in vitro. Because FN may be a useful molecular marker of cellular malignancy, we have carried out an extensive screening to test the specific association among the degree of expression of FN, anchorage-independent growth, and tumorigenicity in the athymic nude mouse. A variety of diploid cell strains and established cell lines were tested for the expression of surface FN by indirect immunofluorescence using rabbit antisera against human cold insoluble globulin, rodent plasma FN, or chicken cell-surface FN. Concomitantly, the cells were assayed for tumor formation in nude mice and for the ability to form colonies in methylcellulose. Tumorigenic cells often showed very low surface fluorescence, confirming earlier reports. However, many highly tumorigenic fibroblast lines from several species stained strongly with all three antisera. In contrast, the anchorage-independent phenotype was nearly always associated with tumorigenicity in approximately 35 cell lines examined in this study. In another series of experiments, FN-positive but anchorage-independent cells were grown as tumors in nude mice and then reintroduced into culture. In five of the six tumor-derived cell lines, cell-surface FN was not significantly reduced; one such cell line showed very little surface FN. Our data thus indicate that the loss of cell-surface FN is not a necessary step in the process of malignant transformation and that the growth of FN-positive cells as tumors does not require a prior selection in vivo for FN-negative subpopulations.
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PMID:Cellular tumorigenicity in nude mice. Test of associations among loss of cell-surface fibronectin, anchorage independence, and tumor-forming ability. 38 23

Cold shock (10 degrees C) treatment to Saccharomyces cerevisiae cells normally grown at 30 degrees C resulted in splitting of vacuoles and retarded membrane fluidity as detected by phase contrast microscopy and in vivo nuclear magnetic resonance (NMR) studies, respectively. The treatment was found to impart protection against subsequent freezing as studied by cell viability and colony forming efficiency. We have earlier reported similar protection and retarded membrane fluidity as a result of heat shock treatment to these cells (Obuchi et al., 1990). This suggests that cold shock and heat shock treatments to yeast cells evoke some analogous responses. However, biochemically a new 33 kDa protein (CSP 33) was detected upon cold shock treatment which is distinct from heat shock induced family of proteins (Kaul et al., 1992). We present here the first report of this kind and its practical implications for protection against freezing.
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PMID:Cold shock response of yeast cells: induction of a 33 kDa protein and protection against freezing injury. 148 8

Like other bacteria, Bacillus subtilis possesses a family of homologous small acidic proteins (CspB, CspC and CspD, identity >70%) that are strongly induced in response to cold shock. We show that deletion of cspC or cspD genes did not result in a detectable phenotype; in contrast, csp double mutants exhibited severe reduction in cellular growth at 15 degrees C as well as at 37 degrees C, including impairment of survival during the stationary phase. Two-dimensional gel analysis showed that protein synthesis was deregulated in csp double mutants and that the loss of one or two CSPs led to an increase in the synthesis of the remaining CSP(s) at 37 degrees C and after cold shock, suggesting that CSPs down-regulate production of members from this protein family. A cspB/C/D triple mutant (64BCDbt) could only be generated in the presence of cspB in trans on a plasmid that was not lost, in spite of lack of antibiotic pressure, indicating that a minimum of one csp gene is essential for viability of B. subtilis. After cold shock, synthesis of CspB in 64BCDbt was drastically lower than in wild-type cells accompanied by cessation in growth and strong reduction in general protein synthesis. As CspB, CspC and CspD are shown to bind to RNA in a co-operative and interactive manner, CSPs are suggested to function as RNA chaperones facilitating the initiation of translation under optimal and low temperatures.
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PMID:A family of cold shock proteins in Bacillus subtilis is essential for cellular growth and for efficient protein synthesis at optimal and low temperatures. 937 3

Bacillus subtilis possesses three homologous small cold shock proteins (CSPs; CspB, CspC, CspD, sequence identity >72%). They share a similar beta-sheet structure, as shown by circular dichroism, and have a very low conformational stability, with CspC being the least stable. Similar to CspB, CspC and CspD unfold and refold extremely fast in a N <==> U two-state reaction with average lifetimes of only 100-150 ms for the native state and 1-6 ms for the unfolded states at 25 degreesC. As a consequence of their low stability and low kinetic protection against unfolding, all three cold shock proteins are rapidly degraded by proteases in vitro. Analysis of the CSP stabilities in vivo by pulse-chase experiments revealed that CspB and CspD are stable during logarithmic growth at 37 degreesC as well as after cold shock. The cellular half-life of CspC is shortened at 37 degreesC, but under cold shock conditions CspC becomes stable. The proteolytic susceptibility of the CSPs in vitro was strongly reduced in the presence of a nucleic acid ligand, suggesting that the observed stabilization of CSPs in vivo is mediated by binding to their substrate mRNA at 37 degreesC and, in particular, under cold shock conditions.
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PMID:The family of cold shock proteins of Bacillus subtilis. Stability and dynamics in vitro and in vivo. 992 Aug 84

Low-temperature adaptation and cryoprotection were studied in the lactic acid bacterium Lactococcus lactis MG1363. An approximately 100-fold increased survival after freezing was observed when cells were shocked to 10 degrees C for 4 h compared to mid-exponential-phase cells grown at 30 degrees C, indicating an active protection against freezing. Using two-dimensional gel electrophoresis a group of 7 kDa cold-induced proteins (CSPs) was identified that corresponds to a previously described family of csp genes of L. lactis MG1363 (Wouters et al., 1998, Microbiology 144, 2885-2893). The 7 kDa CSPs appeared to be the most strongly induced proteins upon cold shock to 10 degrees C. Northern blotting and two-dimensional gel electrophoresis showed that the csp genes were maximally expressed at 10 degrees C, while induction was lower at 20 and 4 degrees C. However, pre-incubation at 20 and 4 degrees C, as well as stationary-phase conditions, also induced cryoprotection (approx. 30-, 130- and 20-fold, respectively, compared to 30 degrees C mid-exponential phase). For all treatments leading to an increased freeze survival (exposure to 4, 10 and 20 degrees C and stationary-phase conditions), increased levels of three proteins (26, 43 and 45 kDa) were observed for which a role in cryoprotection might be suggested. Increased freeze survival coincides with increased CSP expression, except for stationary-phase conditions. However, the level of observed freeze protection does not directly correlate with the csp gene expression levels. In addition, for the first time specific overproduction of a CSP in relation to freeze survival was studied. This revealed that L. lactis cells overproducing CspD at 30 degrees C show a 2-10-fold increased survival after freezing compared to control cells. This indicates that the 7 kDa cold-shock protein CspD may enhance the survival capacity after freezing but that other factors supply additional cryoprotection.
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PMID:Analysis of the role of 7 kDa cold-shock proteins of Lactococcus lactis MG1363 in cryoprotection. 1058 27

DNA damage by reactive oxygen species is of special interest in the development of cancer and in aging. The renally excreted amount of 8-oxo-7,8-dihydro-2'-deoxyguanosine (oxo(8)dG) is a potential noninvasive marker of oxidative DNA damage. The respiratory chain of mitochondria is one source for the formation of reactive oxygen species. In the present study we investigated in Wistar rats (n = 7; mean body weight at start, 307.4 +/- 11 g) the effect of an increased O(2) consumption, i.e., energy expenditure, due to cold stress on the renally excreted amount of oxo(8)dG. First, the rats were housed for 4 days at 23.5 degrees C (basic period, BP), and then for 6 days at 10 degrees C (cold stress period, CSP), and finally for 3 days at 23.5 degrees C (recovery period, RP). The O(2) consumption (L O(2)/day/kg weight) was significantly (P < 0.0001) on average 50% higher in CSP (69.0 +/- 3.9) than in BP (45.8 +/- 4.8), and similar in BP and RP (44.3 +/- 5.4). The average renal excretion of oxo(8)dG (pmol/day/kg weight) was significantly (P < 0.025) on average 13% higher in CSP (375.5 +/- 27.7) than in BP (333.2 +/- 47. 4) and similar in BP and RP (331.8 +/- 34.3). Maximum increase in oxo(8)dG excretion of on average 17% was on the third to fifth day of the CSP. This study reveals that an increase in O(2) consumption of 50% resulted in a much lower increase in the renal excretion of oxo(8)dG.
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PMID:Renal excretion of 8-oxo-7,8-dihydro-2'-deoxyguanosine in Wistar rats with increased O(2) consumption due to cold stress. 1077 19

Strains of Rhizobium leguminosarum bv. viciae, isolated from the legume species Lathyrus japonicus and Lathyrus pratensis in northern Quebec (Canada), showed different capacities for growing at low temperature. In the present study, we investigated some mechanisms related to cold adaptation. Two cold-adapted strains (psychrotrophs) were compared to a poorly adapted strain and to a cold-sensitive strain (reference strain) for freezing survival, protein induction and fatty acid composition under low temperature. Following cold shocks (25 degrees C to 10, 5 and 0 degrees C), a common 6.1-kDa CSP (cold shock protein) was induced in all strains, but the total number of CSPs synthesized at 0 degrees C was higher in cold-adapted strains than in the cold-sensitive strain. The synthesis of CAPs (cold acclimation proteins) was observed under continuous growth at 5 degrees C in all three strains capable of growth at this temperature. Levels of survival after 24 h at -80 degrees C where higher in cold- (79%) and poorly adapted (64%) strains than in the cold-sensitive strain (33%), but a 2-h acclimation period at 5 degrees C before freezing doubled the survival of the cold-sensitive strain. Low temperature conditions affected similarly the fatty acid composition of all strains, regardless of their cold adaptation level. The proportion of unsaturated fatty acids increased significantly with the lowering of growth temperature from 25 to 5 degrees C, but showed a tendency to decrease after a cold shock from 25 to 5 degrees C. A specific unsaturated fatty acid, cis-12 octadecanoic acid, was produced during growth at 5 degrees C. The unsaturated cis-vaccenic acid was the principal component under all conditions. The cold adaptation trait was weakly reflected in symbiosis with the agronomic legume, Lathyrus sativus, with which one cold-adapted strain showed a slightly higher nitrogenase activity and shoot dry matter yield than a commercial strain under a sub-optimal temperature regime.
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PMID:Physiological adaptation to low temperatures of strains of Rhizobium leguminosarum bv. viciae associated with Lathyrus spp.(1). 1081 64

It is determined that an addition of an anti-CSP 310 antiserum to isolated winter wheat and maize mitochondria caused more significant increasing of spontaneous lipid peroxidation than the addition of stress protein CSP 310. It is shown that, at function of different mitochondrial respiratory chain complexes, the lipid peroxidation in winter wheat and maize mitochondria take place with different intensities. Under the functioning of mitochondrial respiratory chain complex IV, the maximum output of lipid peroxidation products, dienic conjugates is detected. The presence of antiserum against CSP 310 in incubation media induces lipid peroxidation more than the presence of CSP 310 in mitochondria isolated from stressed plants under these conditions. Based on data obtained, it is possible to conclude that in vivo endogenous CSP 310, during a cold stress, has an antioxidant activity the same as other known uncoupling proteins.
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PMID:An influence of stress protein CSP 310 and antiserum against this protein on lipid peroxidation in cereal mitochondria. 1148 10

It was found that an addition of antiserum obtained against stress protein 310 kD increased coupling of oxidation and phosphorylation in mitochondria isolated from cold-stress winter rye shoots and had no influence on dycotiledon mitochondria (pumpkins and sunflower). The data obtained showed a difference between molecular weights of dycotyledon polypeptides with immunochemical affinity to CSP 310 and CSP 310 subunits. It was shown that low-temperaturestress caused a transition to a low-energy state ("cold uncoupling") of free from endogenous free fatty acid cereal mitochondria. At the same time, this "cold uncoupling" in mitochondria of dycotyledon species investigated was not detected. We suppose that a special mechanism of low-temperature stress reaction in mitochondria dealing with uncoupling activity of stress protein CSP 310 exists in cereals.
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PMID:Stress protein CSP 310 causes oxidation and phosphorylation uncoupling during low-temperature stress only in cereal but not in dycotyledon mitochondria. 1150 77

Addition of the cold-stress-related protein CSP 310 to mitochondria isolated from winter wheat ( Triticum aestivum L. cv. Zalarinka), winter rye ( Secale cereale L. cv. Dymka), maize ( Zea mays L. cv. VIR 36) and pea ( Pisum sativum L. cv. Marat) caused an increase in non-phosphorylative respiration. This increase was inhibited by KCN, indicating that the protein is not a CN-resistant alternative oxidase. Unlike plant mitochondrial uncoupling proteins such as PUMP, the uncoupling action of CSP 310 did not depend on the presence of free fatty acids in the incubation medium. We propose that the mechanism of the uncoupling action of CSP 310 differs from that of other known plant uncoupling systems and that the CSP 310 uncoupling system is a third uncoupling system in cereals.
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PMID:Stress-induced protein CSP 310: a third uncoupling system in plants. 1202 77


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