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1.
CEN Case Rep ; 12(2): 210-214, 2023 05.
Artigo em Inglês | MEDLINE | ID: mdl-36378461

RESUMO

Ureteropelvic junction obstruction (UPJO) is a congenital or acquired functionally significant impairment of urinary transport from the renal pelvis to the ureter. Congenital UPJO typically results from intrinsic disease such as the presence of an aperistaltic segment of the ureter, aberrant vessels or kidney abnormalities. Rare conditions can sometimes mimic an UPJO. We present a case of an 86-year-old woman with a UPJO diagnosed on CT. The patient was counseled on treatment options and elected to undergo a left uretherorenoscopy (URS) plus left laparoscopic pyeloplasty. The definitive histopathologic diagnosis was perinephric myxoid pseudotumor of fat, an extremely rare neoplasm, mass-forming. To the best of our knowledge, this is the first known case of a pseudotumor of fat causing UPJO. 6-month follow-up showed neither recurrence nor residual UPJO. We describe a rare presentation of extrinsic perinephric myxoid pseudotumor of fat causing UPJ obstruction. In elderly patients with no history of malignancy, UPJ obstruction can occur because of atypical masses.


Assuntos
Laparoscopia , Ureter , Obstrução Ureteral , Feminino , Humanos , Idoso , Idoso de 80 Anos ou mais , Laparoscopia/métodos , Ureter/cirurgia , Pelve Renal/patologia , Pelve Renal/cirurgia , Rim/anormalidades
2.
Ann Bot ; 117(4): 551-63, 2016 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-26975315

RESUMO

BACKGROUND AND AIMS: Trees invest in both primary (e.g. height) and secondary (e.g. diameter) growth. The trade-off between these investments varies between species and changes with the tree growing environment. To better establish this trade-off, readily available allometric exponents relating height to diameter at breast height (γ(h,dbh)) and stem volume to diameter at breast height (α(v,dbh)) were simultaneously studied. METHODS: Allometric exponents α(v,dbh) and γ(h,dbh) were obtained from 8893 individual tree stem analyses from two broadleaved species (Betula papyrifera, Populus tremuloides) and four conifers (Picea glauca, Picea mariana, Pinus banksiana, Abies balsamea) in the temperate and boreal forests of the province of Quebec, Canada. α(v,dbh) and γ(h,dbh) were related to tree age, stand density index (SDI), and mean temperature (TGS) and total precipitation (PGS) of the growing season. KEY RESULTS: α(v,dbh) and γ(h,dbh) were found to be invariant with PGS and positively related to SDI and TGS for all species except Pinus banksiana. The parameter values associated with SDI and TGS were of higher value for conifers than for broadleaved species. CONCLUSIONS: This suggests that conifers and broadleaved species have different growth patterns. This could be explained by their different mode of development, the conifer species having a stronger apical dominance than broadleaved species. Such results could be further considered in allocation studies to quantify future carbon stocks in managed forests.


Assuntos
Clima , Árvores/crescimento & desenvolvimento , Geografia , Modelos Teóricos , Estações do Ano , Especificidade da Espécie , Temperatura , Estados Unidos
3.
J Ind Microbiol Biotechnol ; 31(11): 531-9, 2004 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-15672283

RESUMO

A recombinant fungal microorganism capable of producing deacetylcephalosporin C was constructed by transforming a cephalosporin C esterase gene from Rhodosporidium toruloides into Acremonium chrysogenum. The cephalosporin C esterase gene can be expressed from its endogenous R. toruloides promoter or from the Aspergillus nidulans trpC promoter under standard Acremonium chrysogenum fermentation conditions. The expression of an active cephalosporin C esterase enzyme in A. chrysogenum results in the conversion of cephalosporin C to deacetylcephalosporin C in vivo, a novel fermentation process for the production of deacetylcephalosporin C. The stability of deacetylcephalosporin C in the fermentation broth results in a 40% increase in the cephalosporin nucleus.


Assuntos
Acremonium/enzimologia , Acremonium/metabolismo , Hidrolases de Éster Carboxílico/metabolismo , Cefalosporinas/metabolismo , Acremonium/genética , Hidrolases de Éster Carboxílico/genética , Fermentação , Regulação Fúngica da Expressão Gênica
4.
J Mol Biol ; 196(3): 517-24, 1987 Aug 05.
Artigo em Inglês | MEDLINE | ID: mdl-3316662

RESUMO

A physical map of 330 x 10(3) base-pairs near the replication origin of Myxococcus xanthus chromosome has been established already. Using DNA fragments from this region, Northern blot hybridization analysis was carried out in order to identify the genes expressed during vegetative growth. One of the genes, tentatively designated as vegA, was cloned and its entire DNA sequence was determined. The amino acid sequence of the gene product deduced from the DNA sequence reveals that the VegA protein is a very basic protein with a molecular weight of 18,700. The gene was expressed in Escherichia coli using an expression vector, and its gene product was identified using SDS/polyacrylamide gel electrophoresis. From the results of S1 nuclease mapping, the vegA promoter was found to contain the sequence TAGACA at the -35 region and the sequence AAGGGT at the -10 region. These two regions are separated by 18 nucleotides. Genetic analysis suggests that the vegA gene may be essential for the growth of M. xanthus. From a computer-aided search for homologies to know protein structures, it was found that the VegA protein has homologies to histone H4 of Tetrahymena thermophila and histone H2B of sea urchin.


Assuntos
Proteínas de Bactérias/genética , Bactérias Gram-Negativas/genética , Regiões Promotoras Genéticas , Sequência de Aminoácidos , Composição de Bases , Sequência de Bases , Códon , DNA Bacteriano/genética , Escherichia coli/genética , Regulação da Expressão Gênica , Histonas/genética , Dados de Sequência Molecular , Transcrição Gênica
5.
Proc Natl Acad Sci U S A ; 80(22): 6829-33, 1983 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-6316328

RESUMO

During differentiation of Myxococcus xanthus, a large amount of protein S is produced and assembled on the surface of the myxospore by a process that specifically requires Ca2+. The gene for protein S has been cloned, and two tandemly repeated homologous genes have been found to be within a short distance of each other in the M. xanthus chromosome. We determined the DNA sequence of 3,692 bp encompassing both genes and deduced the amino acid sequences of the two gene products. The gene 1 (upstream) product and the gene 2 (downstream) product show extensive amino acid sequence homology (88%). However, from their structures, protein S was found to be produced from gene 2, indicating that gene 2 is specifically turned on during differentiation. The structure of protein S shows striking similarities with calmodulin: protein S is composed of four internally homologous domains. In particular, the first and the third domains, consisting of 38 residues each, show a high level of homology (79%), and the second and the fourth domains, consisting of 40 residues each, show homology of 65%. In the first and the third domains, there is a common sequence of nine residues, Glu (or Asp)-Asn-Asn-Thr-Ile-Ser-Ser-Val-Lys, which is highly homologous to one of the proposed Ca2+-binding sequences in bovine brain calmodulin, Asp-Gly-Asn-Gly-Thr-Ile-Thr-Thr-Lys.


Assuntos
Proteínas de Bactérias/genética , Calmodulina , Genes Bacterianos , Genes , Bactérias Gram-Negativas/genética , Sequência de Aminoácidos , Proteínas de Bactérias/isolamento & purificação , Composição de Bases , Sequência de Bases , Códon , Enzimas de Restrição do DNA
6.
EMBO J ; 2(1): 87-91, 1983.
Artigo em Inglês | MEDLINE | ID: mdl-11894915

RESUMO

A signal peptidase specifically required for the secretion of the lipoprotein of the Escherichia coli outer membrane cleaves off the signal peptide at the bond between a glycine and a cysteine residue. This cysteine residue was altered to a glycine residue by guided site-specific mutagenesis using a synthetic oligonucleotide and a plasmid carrying an inducible lipoprotein gene. The induction of mutant lipoprotein production was lethal to the cells. A large amount of the prolipoprotein was accumulated in the outer membrane fraction. No protein of the size of the mature lipoprotein was detected. These results indicate that the prolipoprotein signal peptidase requires a glyceride modified cysteine residue at the cleavage site.


Assuntos
Proteínas da Membrana Bacteriana Externa/metabolismo , Cisteína/metabolismo , Proteínas de Escherichia coli , Escherichia coli/enzimologia , Lipoproteínas , Proteínas de Membrana , Precursores de Proteínas/metabolismo , Serina Endopeptidases/metabolismo , Proteínas da Membrana Bacteriana Externa/genética , Sítios de Ligação , Cisteína/genética , Escherichia coli/genética , Escherichia coli/isolamento & purificação , Expressão Gênica , Genes Bacterianos , Mutagênese , Precursores de Proteínas/genética , Serina Endopeptidases/genética
7.
Proc Natl Acad Sci U S A ; 79(11): 3438-41, 1982 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-7048305

RESUMO

The positively charged amino-terminal region of the signal peptide has been proposed to have an important role at an initial step of protein secretion across the membrane (loop model). To test this hypothesis, the charge on the amino-terminal region of the signal peptide of the prolipoprotein of the Escherichia coli outer membrane was altered by using synthetic oligonucleotides from +2 to +1, 0, and -1 by guided site specific mutagenesis of a plasmid DNA carrying an inducible lipoprotein gene. The wild-type sequence of this sectio, Met-Lys-Ala-Thr-Lys (+2), was thus changed to Met-Lys-Asp-Thr-Lys (I-1; +1), Met-Ala-Thr-Lys (I-2; +1), Met-Asp-Thr-Lys (I-3; 0), and Met-Glu-Asp-Thr-Lys (I-4; -1). After induction of lipoprotein production, cells were pulse labeled with [35S]methionine for 10 sec. The lipoprotein of I-1, I-2, and I-3 was assembled in the membrane, although the rates of lipoprotein production progressively decreased as the charge on the signal peptide became more negative. Conversely, in the case of I-4, only a small amount of lipoprotein assembled in the membrane while a large amount of glycerol-unmodified prolipoprotein accumulated in the cytoplasm. This soluble prolipoprotein was gradually and posttranslationally secreted across the membrane to be modified and assembled in the membrane. These results indicate that the positively charged amino-terminal region of the signal peptide plays an important role in efficient protein secretion across the membrane.


Assuntos
Peptídeos/fisiologia , Proteínas/metabolismo , Sequência de Aminoácidos , Proteínas de Bactérias/metabolismo , Transporte Biológico , Escherichia coli , Lipoproteínas/metabolismo , Proteínas de Membrana/metabolismo , Mutação , Precursores de Proteínas/metabolismo , Sinais Direcionadores de Proteínas , Relação Estrutura-Atividade
8.
Microbios ; 25(100): 85-91, 1979.
Artigo em Inglês | MEDLINE | ID: mdl-232233

RESUMO

Extraction of Clostridium perfringens type A spores with dithiothreitol (DTT), DTT plus sodium dodecyl sulphate (DTT-SDS), urea-mercaptoethanol (UME), or alkali, solubilized from 18.6 to 46.5 of the total dry weight of spores. The initiation of germination and lysis of such treated spores with lysozyme and an initiation protein (IP) from the culture supernatant fluid of sporulating cells of C. perfringens was studied under various conditions. The ability of lysozyme and the crude IP to induce germination and lysis of extracted spores was concentration dependent up to 0.5 microgram/ml and 5.6 mg/ml respectively. IP showed an optimum of activity between pH 7 and 8 for DTT-SDS and DTT extracted spores, and between pH 6 and 9 for UME extracted spores. The optimum temperature of activity for IP was 55 degrees C. Dissimilarities in the extent to which lysozyme and the IP initiated germination and lysis of spores extracted by various methods may have been a reflection of the differences in amounts of protein solubilized by each treatment.


Assuntos
Proteínas de Bactérias/farmacologia , Clostridium perfringens/efeitos dos fármacos , Clostridium perfringens/análise , Clostridium perfringens/fisiologia , Ditiotreitol/farmacologia , Muramidase/farmacologia , Dodecilsulfato de Sódio/farmacologia , Esporos Bacterianos/análise , Esporos Bacterianos/efeitos dos fármacos , Esporos Bacterianos/fisiologia , Temperatura
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