Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Ischemia-induced myocardial potassium loss and post-ischemic potassium reuptake was quantitated in 8 open chest pigs during control conditions and during hemodynamic alterations which have been shown to increase steady state sarcolemmal potassium fluxes. Myocardial K+ balance was continuously computed before, during and after a 90 s occlusion of a branch of the circumflex artery during control (CTR), during pacing tachycardia (PACE: 34% increase in heart rate), during proximal aortic constriction (AC; 28% increase in LVSP), and during isoprenaline infusion (ISO; 135% increase in LVdP/dt and 35% increase in heart rate). Ischemia-induced potassium loss increased significantly (40%) during ISO only. Higher basal metabolic rate, increased sarcolemmal K+ conductance, or ischemia-induced depression of a more active Na/K-pump during ISO are possible explanations to why increased K+ loss appeared in this situation. The maximal rate of post-ischemic potassium reuptake was not different from CTR during PACE and ISO, but it was reduced during AC, which might be due to persisting subendocardial ischemia in early reperfusion when ventricular wall stress is high. The extent of potassium restoration was not different from CTR during AC, PACE and ISO.
J Mol Cell Cardiol 1989 Dec
PMID:Effects of hemodynamic variables on myocardial K+ balance during and after shortlasting ischemia. 263 10

The fur gene of Escherichia coli is involved in all iron-regulated transcriptions hitherto studied. The nucleotide sequence of an 868 basepair fragment containing the fur gene was determined. There was only a single longer reading frame. The amino acid sequence derived from the nucleotide sequence comprised 148 amino acids that together made a polypeptide of 16,795 daltons. The amino acid sequence was confirmed by determination of the amino acid composition, the carboxy-terminal lysine residue and the internal Lys-Lys and Lys-Arg sequences of the isolated Fur protein. The nucleotide sequence contains typical initiation and termination sites for transcription and translation.
Mol Gen Genet 1985
PMID:Nucleotide sequence of the iron regulatory gene fur. 299 6

A selection procedure using Mn2+ is described. A high percentage of the Mn2+ resistant mutants had constitutive iron transport systems. By P1 transduction, and complementation with the cloned fur gene it could be shown that nearly all the mutants constitutive in the expression of the operon fusion fiu::lambda placMu were only defective in fur. High concentrations of manganese inhibited the derepression of an iron-regulated lac operon fusion. In another iron-regulated lac operon fusion that was inducible by iron, manganese also induced the production of beta-galactosidase. Most of the fur mutants isolated (80%) were not able to grow on succinate, fumarate or acetate. After transformation with a fur+ plasmid all 39 mutants tested were able to grow on succinate. In fur mutants the presence of succinate in the growth medium reduced succinate uptake rates by 50%-70%. Succinate dehydrogenase activity was reduced to 10% of that of the parent strain.
Mol Gen Genet 1987 Nov
PMID:Selection procedure for deregulated iron transport mutants (fur) in Escherichia coli K 12: fur not only affects iron metabolism. 332 34

Comparison of nucleotide sequence data of the 5' region of a fes/fps viral oncogene with those of the v-fes/fps homologous regions of man and cat revealed the position of the 3' portion of an as yet unidentified c-fes/fps exon. Comparative Southern blot and heteroduplex analysis of human and feline DNA immediately upstream of the v-fes/fps homologous regions showed extensive but discontinuous homology over a 9 kbp DNA stretch, which we have designated as fur. Northern blot analysis of mRNA from KG-1 myeloid cells with fes/fps- or fur-specific probes revealed a 3.0 kb fes/fps and a 4.5 kb fur transcript. Analysis of a number of tissues of an adult Wistar Lewis rat for the presence of fur transcripts revealed its differential expression pattern. An 0.95 kbp fes/fps-related and a 2.2 kbp fur-related cDNA recombinant clone were isolated from an oligo(dT)-primed KG-1 cDNA library. Comparative nucleotide sequence analysis of the fes/fps cDNA and its human genomic counterpart indicated that the cDNA contained genetic sequences that were identical to and colinear with exon 15-19 and, furthermore, that the poly(A) addition signal near the 3' end of exon 19 was functional. Similar analysis of the 2.2 kbp fur cDNA indicated that the poly(A) addition signal of the fur transcript was in close proximity of the newly discovered fes/fps exon. The region in between contained a CATT sequence but no 'TATA' box. The fur transcript was characterized by a long noncoding region at its 3' end.
Mol Biol Rep 1986
PMID:Characterization of human c-fes/fps reveals a new transcription unit (fur) in the immediately upstream region of the proto-oncogene. 348 99

In Escherichia coli the iron uptake systems are regulated by the fur gene product. The synthesis of the outer membrane proteins fiu, fepA, fecA, fhuA, fhuE and cir is derepressed at low iron concentrations in the medium or constitutive in a fur mutant. The fur gene region cloned into pACYC184 was analysed by restriction analysis, Tn1000 mutagenesis and complementation studies. The presence of fur+ plasmids repressed synthesis of the proteins fepA, fecA, fhuE and cir in a chromosomal fur mutant. More quantitatively, the repression to wild-type levels was shown with lac fusions to the genes fiu, fepA and cir. In minicells an 18,000 dalton protein was identified as the fur gene product. Correlated with the fur protein a slightly smaller protein, possibly a degradation product, was observed. The gene fur was mapped on the E. coli chromosome near nagA at about 15.5 min.
Mol Gen Genet 1984
PMID:Cloning of the repressor protein gene of iron-regulated systems in Escherichia coli K12. 609 98

The lac genes were inserted with phage Mu(Ap, lac) into the fhuA, fepA, cir and tonB genes which specify components of iron uptake systems. The expression of lac in all these operon fusions was controlled by the availability of iron to the cells, thereby facilitating a quick and simple measurement of the expression of the genes listed above. In an iron rich medium under anaerobic conditions all systems were strongly repressed. fhuA was depressed at higher iron concentration than was fepA or cir, and tonB was repressed only under anaerobic conditions and could be induced by iron limitation. Mutants constitutive for the expression of beta-galactosidase were selected in a fhuA-lac fusion strain. The outer membrane proteins Cir, FhuA, FecA, 76K and 83K were made constitutively in such mutant strains. Therefore, they were termed fur mutants. In these fur mutant strains, the synthesis of a 19K protein was reduced. Furthermore, it was found that transport of ferric enterochelin and ferrichrome was also constitutive in the fur mutant cells, and that ferric citrate uptake could be induced by only 10 microM citrate in the growth medium in contrast to wild-type cells in which at least 100 microM citrate was necessary. The fepA gene was concluded to be under an additional control, because it was not fully derepressed by the fur mutation.
Mol Gen Genet 1981
PMID:Regulation of ferric iron transport in Escherichia coli K12: isolation of a constitutive mutant. 702 76

The total amino acid concentration and the amino acid pattern, i.e. the relative proportion of each amino acid (protein-bound plus free) to the total amino acids, in the milks of the Northern elephant seal, Antarctic fur seal, California sea lion, and Australian sea lion were determined. Total amino acid concentration was 10% (w/v) or greater and did not vary significantly among species. The most abundant amino acids in the milks of all species were glutamate, proline and leucine. Essential amino acids were 40%, branched-chain amino acids were 20%, and sulfur amino acids were 4% of the total milk amino acids in all species. There were differences among the pinnipeds in some of the individual amino acids; the milk of the Northern elephant seal was the most distinct among the pinnipeds with higher histidine, serine and cystine contents and a lower methionine content than that of other pinnipeds. There was little effect of stage of lactation on total amino acid concentration or amino acid pattern in pinniped milk. Comparison of milk from the four pinniped species with that of 14 other mammalian species suggests commonality in milk amino acid pattern despite the wide variation in total amino acid concentration among the species.
Comp Biochem Physiol B Biochem Mol Biol 1995 Mar
PMID:Amino acid composition of pinniped milk. 758 37

RPE.40 mutant cells differ from wild-type Chinese hamster ovary (CHO-K1) cells in their increased resistance to Pseudomonas exotoxin A and their inability to process the insulin proreceptor and certain viral envelope proproteins. Northern analysis revealed that RPE.40 cells maintained a substantially lower steady-state level of 4.0 kb fur mRNA than did CHO-K1 cells. Analysis of fur cDNAs showed that RPE.40 cells were diploid at the fur locus, and RPE.40 cells had a Cys (TGC) to Tyr (TAC) mutation in codon 196 of one allele (allele I). Approximately 25-30% of the CHO-K1 cells were also heterozygous (Tyr/Cys) at codon 196, and pre-mRNAs transcribed from the second allele (allele II) in RPE.40 cells were defectively spliced. All other pre-mRNAs were correctly spliced. Rapid turnover of defectively spliced transcripts may account for the reduced steady-state level of fur mRNA observed in RPE.40 cells. Our results provide a mechanistic basis for the endoprotease-deficient phenotype of RPE.40 cells.
Somat Cell Mol Genet 1995 Jan
PMID:Analysis of mutations in alleles of the fur gene from an endoprotease-deficient Chinese hamster ovary cell strain. 760 55

Pseudobactin 358 is the yellow-green fluorescent siderophore produced by Pseudomonas putida WCS358 in conditions of iron limitation. The genes encoding for siderophore biosynthesis are iron-regulated at the transcriptional level. Previous work has shown that a positive regulator, PfrA, is absolutely required for the activation under iron-limiting conditions of pseudobactin 358 biosynthesis. In this study we identified a set of Tn5 insertion mutants of strain WCS358 which lost the ability to activate an iron-regulated siderophore promoter. These mutants no longer produced pseudobactin 358. Molecular analysis revealed that they carried a Tn5 insertion in a gene, designated pfrl (Pseudomonas ferric regulator), which codes for a protein (Pfrl) of 19.5 kDa. Pfrl contains a putative helix-turn-helix motif typical of DNA-binding proteins and has homology to two DNA-binding transcriptional activators, Fecl from Escherichia coli and Pupl from P. putida. The proposed role of Pfrl in strain WCS358 is an activator protein regulating pseudobactin 358 biosynthesis under iron limitation. The pfrl promoter region contains a sequence which displays high identity to the Fur-box consensus. This 19 bp consensus sequence is recognized by Fur, an iron-binding repressor protein found in many different bacteria. The E. coli Fur protein can bind to the pfrl promoter region, indicating that this activator gene is likely to be iron-regulated by Fur. We also report the identification and characterization of the P. putida WCS358 fur gene. The Fur protein of strain WCS358 is structurally and functionally similar to other cloned Fur proteins from other bacterial species.
Mol Microbiol 1995 Mar
PMID:Iron regulation of siderophore biosynthesis and transport in Pseudomonas putida WCS358: involvement of a transcriptional activator and of the Fur protein. 762 64

Sequencing of cDNA clones reveals a precursor protein that can be processed into 10 different hepta-FaRPs. Two of the peptides are previously undescribed and are N-terminally extended forms of-YMRFamide, making them the only methionine-containing peptides in the precursor. They are separated from the main cluster of hepta-FaRPs by a recognition site (RQKR) for the Golgi-resident proteolytic enzyme furin. Antisera raised against the synthetic peptide KQDPFLRFGK specifically stain the clusters of neurons in the parietal ganglia that have been shown to contain hepta-FaRP mRNA. These antisera recognize two major protein bands of 35 and 23 kDa on immunoblots. Evidence is presented to identify the larger band as the precursor protein and the smaller band as the fragment containing the main cluster of hepta-FaRPs produced after furin cleavage. A series of immunostaining bands of 22-13 kDa suggests sequential and non-preferential N- or C-terminal cleavage at the mainly monobasic (K and R) sites that link all of the peptide sequences throughout the 23-kDa fragment, to yield the preamidated hepta-FaRPs. Immunostaining of sections shows punctate staining in the perikarya of the parietal cluster neurons commensurate with label within the endoplasmic reticulum and Golgi apparatus. Staining is followed through the axons to many fibers in the nerve trunks and is picked up as fine processes within the skin. These observations indicate that the antiserum used here recognizes one or more of the processed hepta-FaRPs, a view confirmed by radioimmunoassay. The abundance of immunoreactive fibers within the skin suggests a major role for the peptides in this tissue.
Mol Cell Neurosci 1994 Dec
PMID:N-terminally extended FMRFamide-related peptides of Helix aspersa: processing of the precursor protein and distribution of the released peptides. 770 38


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