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1.
Comp Biochem Physiol B Biochem Mol Biol ; 165(4): 226-35, 2013 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-23701991

RESUMO

The full-length cDNAs of three pepsinogens (Pgs) were cloned from the stomach of newt, Cynops pyrrhogaster, and nucleotide sequences of the full-length cDNAs were determined. Molecular phylogenetic analysis showed that two Pgs, named PgC1 and PgC2, belong to the pepsinogen C group, and one Pg, named PgA, belongs to the pepsinogen A group. The sequences contain an open reading frame (ORF) encoding 385 amino acid residues for PgC1, 383 amino acid residues for PgC2 and 377 amino acid residues for PgA. In addition, all of the three amino acid sequences conserve some unique characteristics such as six cysteine residues and putative active site two aspartic acid residues. All of the pepsinogen mRNAs were detected in the stomach by RT-PCR but not in other organs. Although a slight difference at the time of the start of expression was seen among the three pepsinogen genes, all of them were expressed in the larval stage after hatching. This is the first report on cloning of pepsinogens from urodele stomach.


Assuntos
Mucosa Gástrica/metabolismo , Pepsinogênio A/genética , Pepsinogênio C/genética , Salamandridae/genética , Sequência de Aminoácidos , Animais , Sequência de Bases , Clonagem Molecular , Análise por Conglomerados , Primers do DNA/genética , DNA Complementar/genética , Funções Verossimilhança , Modelos Genéticos , Dados de Sequência Molecular , Pepsinogênio A/metabolismo , Pepsinogênio C/metabolismo , Reação em Cadeia da Polimerase Via Transcriptase Reversa , Salamandridae/metabolismo , Alinhamento de Sequência , Análise de Sequência de DNA
2.
Hinyokika Kiyo ; 57(10): 545-9, 2011 Oct.
Artigo em Japonês | MEDLINE | ID: mdl-22089151

RESUMO

To evaluate the diagnostic accuracy of prostate magnetic resonance imaging (MRI), we compared MRI findings with the results of biopsy as well as findings from specimens following total prostatectomy. The subjects consisted of 260 males who showed a prostate specific antigen (PSA) level in the gray zone (4 ng/ml ≤PSA <10 ng/ml) and also underwent digital rectal examination (DRE), transrectal ultrasound (TRUS), and MRI prior to prostate biopsy between April 2005 and December 2009. In Evaluation 1, the results of DRE/TRUS/MRI were compared with those of prostate biopsy. The biopsy-positive rate was higher in males positive in each examination. However, 24.8% of males negative in all examinations were biopsypositive. Thus, these examinations were considered to be inappropriate for secondary screening. In evaluation 2, the prostate was divided into 4 regions, and the findings from specimens following total prostatectomy were compared with MRI findings in each region. For the region containing prostate cancer, MRI showed a sensitivity of 26.0%, specificity of 98.3%, positive predictive value of 96.2%, and negative predictive value of 44. 4%. In patients with a Gleason score ≥7, cancer foci were more frequently detectable using MRI. MRI prior to prostate biopsy in patients in the PSA gray zone is inappropriate for secondary screening due to its low sensitivity. However, by virtue of its high positive predictive value, MRI is useful for determining patients indicated for biopsy, as well as DRE and TRUS. Accurate evaluation of the localization of all cancer lesions is difficult using MRI. However, when MRI findings are present, they frequently indicate the cancer lesion, which may be useful information for treatment.


Assuntos
Biópsia por Agulha , Imageamento por Ressonância Magnética , Antígeno Prostático Específico/análise , Próstata/patologia , Neoplasias da Próstata/diagnóstico , Humanos , Masculino , Estudos Retrospectivos , Sensibilidade e Especificidade
3.
Mol Biol Cell ; 21(1): 106-16, 2010 Jan 01.
Artigo em Inglês | MEDLINE | ID: mdl-19864465

RESUMO

The heat-shock response is characterized by the expression of a set of classical heat-shock genes, and is regulated by heat-shock transcription factor 1 (HSF1) in mammals. However, comprehensive analyses of gene expression have revealed very large numbers of inducible genes in cells exposed to heat shock. It is believed that HSF1 is required for the heat-inducible expression of these genes although HSF2 and HSF4 modulate some of the gene expression. Here, we identified a novel mouse HSF3 (mHSF3) translocated into the nucleus during heat shock. However, mHSF3 did not activate classical heat-shock genes such as Hsp70. Remarkably, overexpression of mHSF3 restored the expression of nonclassical heat-shock genes such as PDZK3 and PROM2 in HSF1-null mouse embryonic fibroblasts (MEFs). Although down-regulation of mHSF3 expression had no effect on gene expression or cell survival in wild-type MEF cells, it abolished the moderate expression of PDZK3 mRNA and reduced cell survival in HSF1-null MEF cells during heat shock. We propose that mHSF3 represents a unique HSF that has the potential to activate only nonclassical heat-shock genes to protect cells from detrimental stresses.


Assuntos
Regulação da Expressão Gênica , Proteínas de Choque Térmico/metabolismo , Resposta ao Choque Térmico/genética , Fatores de Transcrição/metabolismo , Animais , Células COS , Núcleo Celular/metabolismo , Galinhas , Chlorocebus aethiops , Citoproteção , DNA/metabolismo , DNA Helicases/metabolismo , Genoma/genética , Proteínas de Choque Térmico HSP70/genética , Proteínas de Choque Térmico HSP70/metabolismo , Humanos , Camundongos , Dados de Sequência Molecular , Família Multigênica/genética , Proteínas Nucleares/metabolismo , Ligação Proteica , Transporte Proteico , Estresse Fisiológico , Temperatura
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