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

Tyrosine hydroxylase (TH) and phenylethanolamine-N-methyltransferase (PNMT) activities were assayed in adrenal glands of the following groups of the Alaskan red-backed vole (Clethrionomys rutilus dawsoni): 1) laboratory reared at 20 degrees C and 2) exposed to 5 degrees C for 1, 3, 7, and 28 days; 3) wild, summer acclimatized; 4) wild, fall acclimatized; and 5) wild, winter acclimatized. TH activity in laboratory-acclimated voles exposed to 5 degrees C was increased by 2 times after 3 days and remained elevated after 28 days. PNMT activity in these same voles was increased after 7 days and also remained elevated after 28 days of cold exposure. In wild-acclimatized voles TH activity and PNMT activity in summer were equivalent to levels in 28-day cold-acclimated laboratory voles. In fall, TH activity was increased to 2.5 times the summer value. It decreased by midwinter, but remained elevated above the summer level. In contrast, PNMT activity appeared unchanged from summer through fall and winter. Pregnant summer voles had markedly increased TH activity. Adrenal norepinephrine and epinephrine did not change significantly with cold acclimation or seasonal acclimatization. Thus, acclimatization of wild voles to fall and winter conditions involved aquisition of a greater capacity to synthesize adrenal catecholamines than that produced by exposing laboratory-reared voles to an extended period of cold.
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PMID:Catecholamine-synthesizing enzymes in adrenals of seasonally acclimatized voles. 2 32

De novo phospholipid biosynthesis was assayed in isolated hepatocytes of rainbow trout (Oncorhynchus mykiss) both fully acclimated to 5 or 20 degrees C and undergoing acclimation from one temperature extreme to the other. Incorporation of [14C]choline, [3H]ethanolamine, and [3H]serine into phosphatidyl-choline (PC), phosphatidylethanolamine (PE), or both, was followed to assess metabolic capacity. PE biosynthesis rates exceeded those for PC four- to fivefold. Methylation of PE accounted for 10 (20 degrees C)-17% (5 degrees C) of the synthetic capacity for PC, whereas 6 (20 degrees C-acclimated)-27% (5 degrees C-acclimated) of PE synthesis was derived from phosphatidylserine (PS) decarboxylation. Several factors may contribute to the altered proportions of PE and PC or unsaturated molecular species of phospholipids characteristic of thermally acclimated animals. 1) Activities of choline and ethanolamine phosphotransferase pathways were significantly higher, and decarboxylation activity lower, in 20 degrees C than in 5 degrees C-acclimated trout, resulting in maintained PE synthesis despite a general depression of lipid biosynthesis at cold temperatures. 2) PC biosynthesis depended more on temperature (Q10 = 2.6-3.0) than that of PE (Q10 = 1.8-2.2), causing the ratio of PC/PE synthesis to be positively correlated with temperature. 3) Contribution of methyltransferase pathway to the synthesis of PC was higher at 5 than 20 degrees C. 4) The percentage of ethanolamine incorporation recovered in PC increased threefold in the early stages of warm acclimation. However, not all adjustments in biosynthetic capacity (most notably a 10-fold stimulation of PC synthesis 2 days after transfer of warm-acclimated trout to 5 degrees C) influence membrane lipid composition, implicating other processes in the regulation of this parameter.
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PMID:Adaptation to temperature: phospholipid synthesis in hepatocytes of rainbow trout. 216 24

If Bacillus subtilis is incubated in radioactive methionine in the absence of protein synthesis, the methyl-accepting chemotaxis proteins (MCPs) become radioactively methylated. If the bacteria are further incubated in excess nonradioactive methionine ("cold-chased") and then given the attractant aspartate, the MCPs lose about half of their radioactivity due to turnover, in which lower specific activity methyl groups from S-adenosylmethionine (AdoMet) replace higher specific activity ones. Due to the cold-chase, the specific activity of the AdoMet pool is reduced at least 2-fold. If, later, the attractant is removed, higher specific activity methyl groups return to the MCPs. Thus, there must exist an unidentified methyl carrier that can "reversibly" receive methyl groups from the MCPs. In a similar experiment, labeled cells were transferred to a flow cell and exposed to addition and removal of attractant and of repellent. All four kinds of stimuli were found to cause methanol production. Bacteria with maximally labeled MCPs were exposed to many cycles of addition and removal of attractant; the maximum amount of radioactive methanol was evolved on the third, not the first, cycle. This result suggests that there is a precursor-product relationship between methyl groups on the MCPs and on the unidentified carrier, which might be the direct source of methanol. However, since no methanol was produced when a methyltransferase mutant, whose MCPs were unmethylated, was exposed to addition and removal of attractant or repellent, the methanol must ultimately derive from methylated MCPs.
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PMID:Novel methyl transfer during chemotaxis in Bacillus subtilis. 250 39

The adrenal gland norepinephrine content is elevated and 3H-norepinephrine lowered in adult rats exposed to cold during early postnatal period. 7-week test cooling of cold-imprinted animals induced a more obvious adrenal norepinephrine exchange than in control rats, phenylethanolamine-N-methyltransferase activity falling by a factor of two. The brown adipose tissue 3H-norepinephrine exchange was first intensified and then returned to normal level in control rats in cooling. The 3H-norepinephrine exchange was reduced in cold-imprinted animals after 7-week cooling.
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PMID:[Changes in noradrenaline metabolism in the rat subjected to cold in the early postnatal period]. 378 Oct 35

Ribosomal protein methylation has been well documented but its function remains unclear. We have examined this phenomenon using an Escherichia coli mutant (prmB2), which fails to methylate glutamine residue number 150 of ribosomal protein L3. This mutant exhibits a cold-sensitive phenotype: its growth rate at 22 degrees C is abnormally low in complete medium. In addition, strains with this mutation accumulate abnormal and unstable ribosomal particles; 50-S and 30-S subunits are formed, but at a lower rate. Once assembled, ribosomes with unmethylated L3 are fully active by several criteria. (a) Protein synthesis in vitro with purified 70-S prmB2 ribosomes is as active as wild-type using either a natural (R17) or an artificial [poly(U)] messenger. (b) The induction of beta-galactosidase in vivo exhibits normal kinetics and the enzyme has a normal rate of thermal denaturation. (c) These ribosomes are standard when exposed in vitro to a low magnesium concentration or increasing molarities of LiCl. Efficient methylation of L3 in vitro requires either unfolded ribosomes or a mixture of ribosomal protein and RNA. We suggest that the L3-specific methyltransferase may qualify as one of the postulated 'assembly factors' of the E. coli ribosome.
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PMID:Cold-sensitive ribosome assembly in an Escherichia coli mutant lacking a single methyl group in ribosomal protein L3. 617 16

The single isotopic-enzymatic assay of histamine was modified to increase its sensitivity and to facilitate measurement of plasma histamine levels. The modification involved extracting 3H-1-methylhistamine (generated by the enzyme N-methyltransferase acting on histamine in the presence of S-[methyl-3H]-adenosyl-L-methionine) into chloroform and isolating the 3H-1-methylhistamine by thin-layer chromatography (TLC). The TLC was developed in acetone:ammonium hydroxide (95:10), and the methylhistamine spot (Rf = 0.50) was identified with an o-phthalaldehyde spray, scraped from the plate, and assayed in a scintillation counter. The assay in plasma demonstrated a linear relationship from 200 to 5000 pg histamine/ml. Plasma always had higher readings than buffer, and dialysis of plasma returned these values to the same level as buffer, suggesting that the baseline elevations might be attributable to histamine. However, all histamine standard curves were run in dialyzed plasma to negate any additional influences plasma might exert on the assay. The arithmetic mean (+/- SEM) in normal plasma histamine was 318.4 +/- 25 pg/ml (n = 51), and the geometric mean was 280 +/- 35 pg/ml. Plasma histamine was significantly elevated by infusion of histamine at 0.05 to 1.0 micrograms/kg/min or by cold immersion of the hand of a cold-urticaria patient. Therefore this modified isotopic-enzymatic assay of histamine is extremely sensitive, capable of measuring fluctuations in plasma histamine levels within the normal range, and potentially useful in analysis of the role histamine plays in human physiology.
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PMID:Measurement of plasma histamine: description of an improved method and normal values. 709 24

We have tested the hypothesis that the promotion of flowering by prolonged exposure to low temperatures (vernalization) is mediated by DNA demethylation [Burn, J. E., Bagnall, D. J., Metzger, J. M., Dennis, E. S. & Peacock, W. J. (1993) Proc. Natl. Acad. Sci. USA 90, 287-291]. Arabidopsis plants that have reduced levels of DNA methylation because of the presence of a methyltransferase (METI) antisense gene flowered earlier than untransformed control plants, without the need for a cold treatment. Decreased DNA methylation mutants (ddm1) also flowered earlier than the wild-type progenitor under conditions where they respond to vernalization. We conclude that demethylation of DNA is sufficient to cause early flowering, and we have found that the promotion of flowering is directly proportional to the decrease in methylation in METI antisense lines. The early-flowering phenotype was inherited in sexual progeny, even when the antisense transgene had been lost by segregation. Methyltransferase antisense plants with low DNA methylation levels responded to a low-temperature treatment by flowering even earlier than their untreated siblings indicating that the promotion of flowering by cold and by demethylation was additive when neither treatment saturated the early-flowering response. As in untransformed control plants, the cold-induced early-flowering signal was reset in progeny of METI antisense plants. These observations suggest that the demethylation brought about by a METI antisense can account for some properties of vernalization, but not for the need for revernalization in each generation.
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PMID:DNA methylation and the promotion of flowering by vernalization. 957 69

A new gene, mutK, of Vibrio cholerae, encoding a 19-kDa protein which is involved in repairing mismatches in DNA via a presumably methyl-independent pathway, has been identified. The product of the mutK gene cloned in either high- or low-copy-number vectors can reduce the spontaneous mutation frequency of Escherichia coli mutS, mutL, mutU, and dam mutants. The spontaneous mutation frequency of a chromosomal mutK knockout mutant was almost identical to that of wild-type V. cholerae cells, indicating that when the methyl-directed mismatch repair is blocked, the repair potential of MutK becomes apparent. The complete nucleotide sequence of the mutK gene has been determined, and the deduced amino acid sequence showed three open reading frames (ORFs), of which the ORF3 represents the mutK gene product. The mutK gene product has no significant homology with any of the proteins deposited in the EMBL data bank. ORF2, located upstream of mutK, encodes a 14-kDa protein which has more than 70% homology with a hypothetical protein found only downstream of the E. coli vsr gene. ORF1, located farther upstream of mutK, has more than 80% homology with a major cold shock protein found in several bacteria. Downstream of mutK, a partial ORF having 60% homology with an RNA methyltransferase has been identified. The mutK gene has recently been positioned in the ordered cloned DNA map of the genome of the V. cholerae strain from which the gene was isolated (10).
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PMID:The mutK gene of Vibrio cholerae: a new gene involved in DNA mismatch repair. 992 51

The aspartate chemoreceptor (Tar) of Escherichia coli also serves as a thermosensor, and it is very amenable to genetic and biochemical analysis of the thermosensing mechanism. Its thermosensing properties are controlled by reversible methylation of the cytoplasmic signalling/adaptation domain of the protein. The unmethylated and the fully methylated (aspartate-bound) receptors sense, as attractant stimuli, increases (warm sensor) and decreases (cold sensor) in temperature respectively. To learn more about the mechanism of thermosensing, we replaced the four methyl-accepting glutamyl residues with non-methylatable aspartyl residues in all possible combinations. In a strain defective in both methyltransferase (CheR) and methylesterase (CheB) activities, all of the mutant Tar proteins functioned as warm sensors. To create a situation in which all of the remaining glutamyl residues were methylated, we expressed the mutant proteins in a CheB-defective, CheR-overproducing strain. The fully glutamyl-methylated proteins were designed to mimic the full range of methylation states possible for wild-type Tar. Almost all of the methylated mutant receptors, including those with single glutamyl residues, were cold sensors in the presence of aspartate. Thus, binding of aspartate to Tar and methylation of its single glutamyl residue can invert its temperature-dependent signalling properties.
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PMID:Conversion of a bacterial warm sensor to a cold sensor by methylation of a single residue in the presence of an attractant. 1023 91

Era is an essential G-protein in Escherichia coli identified originally as a homologue protein to Ras (E. coli Ras-like protein). It binds to GTP/GDP and contains a low intrinsic GTPase activity. Its function remains elusive, although it has been suggested that Era is associated with the cytoplasmic membrane, cell division, energy metabolism, and cell-cycle check point. Recently, a cold-sensitive phenotype was found to be suppressed by the overexpression of 16S rRNA methyltransferase, suggesting Era association with the ribosome. Here we demonstrate that Era specifically binds to 16S rRNA and the 30S ribosomal subunit. Both GTP and GDP, but not GMP, inhibit Era binding to ribosomal component. Involvement of Era in protein synthesis is suggested by the fact that Era depletion results in the translation defect both in vitro and in vivo.
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PMID:Era, an essential Escherichia coli small G-protein, binds to the 30S ribosomal subunit. 1052 40


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