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1.
Clin Transl Oncol ; 23(8): 1585-1592, 2021 Aug.
Artículo en Inglés | MEDLINE | ID: mdl-33502740

RESUMEN

PURPOSE: This study aimed to determine the outcomes and prognostic factors associated with octogenarians who underwent pulmonary resection for lung cancer. METHODS/PATIENTS: From 2009 to 2018, 76 octogenarians underwent pulmonary surgery for lung cancer at the Kanazawa Medical University, Japan. They were divided into two groups (early and late octogenarians), and their clinicopathological characteristics and outcomes were investigated. Overall survival rates and recurrence-free survival rates were determined using Kaplan-Meier curves. Univariate and multivariate analyses were performed to identify prognostic factors. RESULTS: Limited surgery was performed more often in the late octogenarian group; however, most perioperative factors were not significantly different between the two groups. The 3-year overall survival and recurrence-free survival rates were 61.2% and 52.8%, respectively. The median observation period was 37.5 (8.9-112.3) months postoperatively. Kaplan-Meier curves showed that age ≥ 85 years (late octogenarian), smoking history, and squamous cell carcinoma on histology were associated with worse survival rates. Multivariate analysis identified age ≥ 85 years (late octogenarian) (p = 0.011) and cigarette smoking (p = 0.025) as unfavorable prognostic factors for overall survival and recurrence-free survival, respectively. CONCLUSIONS: Most octogenarians with an indication for surgery can tolerate pulmonary surgery. However, owing to the limitations of this retrospective, single-center study, future studies involving multiple-institutions are required to confirm our findings.


Asunto(s)
Carcinoma de Células Escamosas/cirugía , Neoplasias Pulmonares/cirugía , Pulmón/cirugía , Factores de Edad , Anciano de 80 o más Años , Análisis de Varianza , Carcinoma de Células Escamosas/mortalidad , Femenino , Humanos , Japón , Estimación de Kaplan-Meier , Neoplasias Pulmonares/mortalidad , Masculino , Pronóstico , Supervivencia sin Progresión , Estudios Retrospectivos , Fumar/efectos adversos , Tasa de Supervivencia , Cirugía Torácica Asistida por Video , Resultado del Tratamiento
2.
J Periodontal Res ; 45(6): 780-7, 2010 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-20626585

RESUMEN

BACKGROUND AND OBJECTIVE: Neutrophils are essential in host defense against periodontopathic bacteria. Immunoglobulin G Fc receptor IIIb (FcγRIIIb) is a neutrophil-specific receptor for immunoglobulin G and bears the functional NA1-NA2 polymorphism. Accumulating evidence suggests a significant association between FcγRIIIb gene polymorphism and periodontitis. In this study, we employed a proteomic approach to evaluate the relevance of FcγRIIIb polymorphism to protein expression profiles of neutrophils. MATERIAL AND METHODS: Neutrophils were collected from ten healthy subjects whose FcγRIIIb genotypes were determined by allele-specific PCRs. Expressions of proteins induced by interaction via FcγRIIIb were examined between the FcγRIIIb genotypes with two-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis. Proteins that were significantly different in expression levels between the FcγRIIIb genotypes were determined with computer image analysis, and identified with mass spectrometry and protein databases. RESULTS: A total of 757 protein spots were observed in the two-dimensional electrophoretograms of neutrophils from five FcγRIIIb-NA1/NA1 and five FcγRIIIb-NA2/NA2 donors. A statistical analysis revealed that the expression levels of five proteins were significantly different between the FcγRIIIb genotypes (p < 0.05). The FcγRIIIb-NA1/NA1 neutrophils exhibited two spots that were significantly underexpressed (protein-arginine deiminase type-4 and annexin VI) and three spots that were significantly overexpressed (Cdc42hs-Gdp complex, myosin light chain 12A and coactosin-like 1) when compared with FcγRIIIb-NA2/NA2 neutrophils. The same expression profiles of protein-arginine deiminase type-4 were obtained by ELISA. CONCLUSION: Differential protein expression profiles were observed in neutrophils between FcγRIIIb genotypes.


Asunto(s)
Perfilación de la Expresión Génica , Isoantígenos/genética , Neutrófilos/química , Polimorfismo Genético , Receptores de IgG/genética , Adulto , Electroforesis en Gel Bidimensional , Femenino , Proteínas Ligadas a GPI/genética , Frecuencia de los Genes , Humanos , Hidrolasas/genética , Procesamiento de Imagen Asistido por Computador , Masculino , Espectrometría de Masas , Persona de Mediana Edad , Neutrófilos/metabolismo , Arginina Deiminasa Proteína-Tipo 4 , Desiminasas de la Arginina Proteica , Proteoma , Adulto Joven
3.
Toxicology ; 376: 137-145, 2017 Feb 01.
Artículo en Inglés | MEDLINE | ID: mdl-27181933

RESUMEN

Manganese (Mn) is an essential metal for mammals. It can modulate the action of endogenous substances, as neurotransmitters, but in excess also can trigger known neurotoxic effects. Many studies have been conducted assessing Mn neurotoxicity. However, Mn bioaccumulation in different brain tissues and behavior effects involving gender-specific studies are conflicted in the literature. Therefore, the aim of this work was to compare Mn effects, after 30days of intraperitoneal treatment, in male and female rats, submitted to forced swim and open field tests. After that, were evaluated Mn and Fe tissue levels in CNS, liver, and kidneys. Wistar rats were divided into saline, Mn 1mg/kg, Mn 5mg/kg, and imipramine (as forced swim control). Then, animals were euthanized by anesthesia overdose followed by decapitation and the collected tissue were striatum, hippocampus, brainstem, cortex, cerebellum, hepatic tissue, and renal tissue. Mn and Fe were determined by ICP-MS. There was a dose-dependent effect on accumulation of Mn in the cerebellum and brainstem to the dosage of 5mg/kg. In hippocampus there were bioaccumulation differences between gender and dose, and an increase of Fe in the groups exposed to Mn. Excess metals in the brain dissected has a strong influence on memory and learning processes and suggests pro-depressive effects, possibly triggered by the reduction of monoamines due to excessive metal bioaccumulation. It was concluded that, under this experimental design, Mn exposure cause metal deposition on dissected CNS, liver and kidney. There an effect at lower doses that was gender-dependent and males had more pronounced behavioral damage compared to females, although with increasing dose, females had an indication of motor damage.


Asunto(s)
Encéfalo/metabolismo , Depresión/metabolismo , Hierro/metabolismo , Riñón/metabolismo , Hígado/metabolismo , Manganeso/metabolismo , Caracteres Sexuales , Animales , Encéfalo/efectos de los fármacos , Depresión/inducido químicamente , Femenino , Inmovilización/métodos , Inyecciones Intraperitoneales , Hierro/toxicidad , Riñón/efectos de los fármacos , Hígado/efectos de los fármacos , Masculino , Manganeso/toxicidad , Ratas , Ratas Wistar
4.
Nucleic Acids Res ; 29(22): 4617-24, 2001 Nov 15.
Artículo en Inglés | MEDLINE | ID: mdl-11713311

RESUMEN

A recJ homolog was cloned from the extremely thermophilic bacterium Thermus themophilus HB8. It encodes a 527 amino acid protein that has 33% identity to Escherichia coli RecJ protein and includes the characteristic motifs conserved among RecJ homologs. Although T.thermophilus RecJ protein (ttRecJ) was expressed as an inclusion body, it was purified in soluble form through denaturation with urea and subsequent refolding steps. Limited proteolysis showed that ttRecJ has a protease-resistant core domain, which includes all the conserved motifs. We constructed a truncated ttRecJ gene that corresponds to the core domain (cd-ttRecJ). cd-ttRecJ was overexpressed in soluble form and purified. ttRecJ and cd-ttRecJ were stable up to 60 degrees C. Size exclusion chromatography indicated that ttRecJ exists in several oligomeric states, whereas cd-ttRecJ is monomeric in solution. Both proteins have 5'-->3' exonuclease activity, which was enhanced by increasing the temperature to 50 degrees C. Mg(2+), Mn(2+) or Co(2+) ions were required to activate both proteins, whereas Ca(2+) and Zn(2+) had no effects.


Asunto(s)
Proteínas Bacterianas/genética , Proteínas de Escherichia coli , Exodesoxirribonucleasas/genética , Thermus thermophilus/genética , Secuencias de Aminoácidos/genética , Secuencia de Aminoácidos , Proteínas Bacterianas/aislamiento & purificación , Proteínas Bacterianas/metabolismo , Dicroismo Circular , Clonación Molecular , ADN Bacteriano/química , ADN Bacteriano/genética , ADN de Cadena Simple/genética , ADN de Cadena Simple/metabolismo , Electroforesis en Gel de Poliacrilamida , Escherichia coli/genética , Exodesoxirribonucleasas/aislamiento & purificación , Exodesoxirribonucleasas/metabolismo , Exonucleasas/metabolismo , Regulación Bacteriana de la Expresión Génica , Genes Bacterianos/genética , Genoma Bacteriano , Cinética , Datos de Secuencia Molecular , Alineación de Secuencia , Análisis de Secuencia de ADN , Homología de Secuencia de Aminoácido , Espectrofotometría Ultravioleta , Temperatura
5.
Biochim Biophys Acta ; 1253(2): 224-8, 1995 Dec 06.
Artículo en Inglés | MEDLINE | ID: mdl-8519806

RESUMEN

A proteinase was purified 230-fold to apparent homogeneity from culture filtrates of Bacillus subtilis by a series of column chromatographies on DE52, DEAE-Toyopearl, Cellulofine GC200M, and Mono-Q, using Boc-Ala-Ala-Pro-Ser-pNA as a substrate. The molecular weight of the proteinase was estimated to be 42,000 by SDS-PAGE in the presence of 2-mercaptoethanol. Studies on the substrate specificity with peptide p-nitroanilides and natural peptides revealed that this proteinase preferentially hydrolyzed the peptide bond on the carboxyl-terminal side of either serine or alanine residues at the P1 position and hydrophobic bulky amino acids at P2. It was most active at pH 9.5 for the hydrolysis of Boc-Ala-Ala-Pro-Ser-pNA. The enzyme was inactivated by diisopropyl fluorophosphate (DFP), but not by tosyl-L-phenylalanine chloromethylketone (TPCK) or by EDTA. Based on the reactivity toward substrates and inhibitors, this enzyme differs from elastase- or subtilisin-like proteinase, hence it is a new type of proteinase with specificity for amino acids at P1 and P2 positions.


Asunto(s)
Bacillus subtilis/enzimología , Serina Endopeptidasas/metabolismo , Secuencia de Aminoácidos , Insulina/metabolismo , Péptidos y Proteínas de Señalización Intercelular , Punto Isoeléctrico , Datos de Secuencia Molecular , Peso Molecular , Oligopéptidos/metabolismo , Péptidos , Serina Endopeptidasas/aislamiento & purificación , Inhibidores de Serina Proteinasa/farmacología , Especificidad por Sustrato , Venenos de Avispas/metabolismo
6.
Gene ; 34(2-3): 243-51, 1985.
Artículo en Inglés | MEDLINE | ID: mdl-2989108

RESUMEN

The insecticidal crystal protein (ICP) gene, icp, from a 68-kb plasmid derived from Bacillus thuringiensis subsp. sotto was cloned in Escherichia coli. The icp expression in E. coli cells was confirmed by both immunological and insect-toxicity assays of the cell extract. The entire icp gene resides in the 6.6-kb PstI fragment, which codes for a 144-kDal peptide identical to the intact ICP, as determined by its size and reaction with anti-ICP antibody. Deletion analysis further revealed that the 2.8-kb region within the 6.6-kb PstI fragment codes for ICP. Analysis of the nucleotide sequence indicated that a peptide of 934 amino acid residues truncated at the C-terminal end is encoded by this 2.8-kb fragment. A unique feature of this truncated ICP is the abundance of cysteine and lysine residues within its C-terminal region.


Asunto(s)
Bacillus thuringiensis/genética , Proteínas Bacterianas/genética , Toxinas Bacterianas , Endotoxinas , Toxinas de Bacillus thuringiensis , Secuencia de Bases , Clonación Molecular , Enzimas de Restricción del ADN , ADN Bacteriano/genética , Escherichia coli/genética , Genes Bacterianos , Proteínas Hemolisinas , Peso Molecular , Control Biológico de Vectores , Plásmidos , Relación Estructura-Actividad
7.
Kansenshogaku Zasshi ; 73(2): 191-6, 1999 Feb.
Artículo en Japonés | MEDLINE | ID: mdl-10213998

RESUMEN

A 40-year-old female was admitted with right chest pain. SLE was absent from her past history, although she complained of polyarthralgia in winter. Atypical pneumonia/pleuritis was suspected by chest X-ray film, showing a nodular shadow in the right lower field and moderate pleural effusion. Chlamydia pneumonia was diagnosed by elevated anti-C. psittsci antibody, while characteristics of pleural fluid revealed serositis accompanied by SLE because of the high titered anti-DNA antibody and the low titered complement. She was cured by clarithromycin and subsequent administration of prednisolone and cyclophosphamide.


Asunto(s)
Infecciones por Chlamydia/complicaciones , Lupus Eritematoso Sistémico/complicaciones , Neumonía Bacteriana/complicaciones , Neumonía Bacteriana/microbiología , Adulto , Femenino , Humanos
8.
Jpn J Antibiot ; 35(5): 1136-44, 1982 May.
Artículo en Japonés | MEDLINE | ID: mdl-6290697

RESUMEN

Cefotiam (CTM) was administered to 52 patients with infectious disease associated with respiratory system, hematological malignancy, urinary system and other system. Good clinical responses were obtained in 38 out of 52 cases (73.1%). Neither objective and subjective side effects nor extreme abnormalities of laboratory tests were observed in these patients. It can be, therefore, concluded that CTM is 1 of the most useful drugs for infectious diseases in respiratory system, hematological malignancy, urinary system and other system.


Asunto(s)
Cefotaxima/análogos & derivados , Infecciones del Sistema Respiratorio/tratamiento farmacológico , Adolescente , Adulto , Anciano , Infecciones Bacterianas/tratamiento farmacológico , Cefotaxima/efectos adversos , Cefotaxima/uso terapéutico , Cefotiam , Evaluación de Medicamentos , Femenino , Enfermedades Hematológicas/complicaciones , Humanos , Masculino , Persona de Mediana Edad , Sepsis/tratamiento farmacológico , Infecciones Urinarias/tratamiento farmacológico
19.
Gamete Res ; 19(2): 215-25, 1988 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-3209183

RESUMEN

The ultrastructural features of spermatogenesis were investigated in the hermaphroditic sea star Asterina minor. The primordial germ cells in the genital rachis contain small clusters of electron-dense material (nuage material) and a stack of annulate lamellae. They also have a flagellum and basal body complex situated close to the Golgi complex. After the development of the genital rachis into the ovotestis, spermatogenic cells increase in number and differentiation begins. Nuage material is observed in spermatogonia, but it gradually disappears in spermatocytes. The annulate lamellae do not exist beyond the early spermatogonial stage. By contrast, a flagellum and basal body complex are found throughout spermatogenesis. The Golgi-derived proacrosomal vesicles appear in the spermatocyte and coalesce to form an acrosomal vesicle in the early spermatid. The process of acrosome formation is as follows: (1) a lamella of endoplasmic reticulum (ER) continuous with the outer nuclear membrane encloses the posterior portion of the acrosomal vesicle; (2) the vesicle attaches to the cell membrane with its anterior portion; (3) periacrosomal material accumulates in the space between the acrosomal vesicle and the ER; (4) the nucleus proper changes its features to surround the acrosome; (5) amorphous, electron-dense material is deposited under the electron-dense disk; and (6) the nucleus forms a hollow opposite the electron-dense material.


Asunto(s)
Equinodermos/citología , Espermatogénesis , Espermatozoides/ultraestructura , Animales , Masculino , Espermatozoides/fisiología
20.
Neurochem Res ; 16(4): 469-73, 1991 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-1833658

RESUMEN

Although the use of aging experimental animals for studying serotonergic neuronal changes is limited because of species differences, cholinergic neuronal deterioration does appear to be a feature common to mammalian aging brains. In the present study, a recently introduced experimental animal, Suncus murinus (house musk shrew, an insectivore classified as being at the stem of the mammalian phylogenic tree) which in certain physiological characteristics is more closely related to the primate than is the rat, was used as an experimental animal model for serotonergic neuronal deterioration in aging brain. We examined the changes in binding to the membrane fraction of aging brain cortex of the experimental animals Suncus and Fischer rat of the serotonergic ligands, 5-HT, imipramine, and 8-OH-DPAT. Morphological study of the brain stem including the Nucleus raphae by immunohistochemical staining demonstrated that in Suncus all the serotonergic ligands had decreasing affinity to the membrane of aging brain; binding of 8-OH-DPAT and imipramine decreased to a greater extent than that of 5-HT. In contrast, the aging rat brain showed no appreciable change in the binding of serotonergic ligands.


Asunto(s)
Encéfalo/metabolismo , Imipramina/metabolismo , Receptores de Serotonina/metabolismo , Antagonistas de la Serotonina/metabolismo , Serotonina/metabolismo , Tetrahidronaftalenos/metabolismo , 8-Hidroxi-2-(di-n-propilamino)tetralin , Acetilcolina/metabolismo , Envejecimiento , Animales , Encéfalo/crecimiento & desarrollo , Membrana Celular/metabolismo , Cerebelo/crecimiento & desarrollo , Cerebelo/metabolismo , Colina/metabolismo , Hipocampo/crecimiento & desarrollo , Hipocampo/metabolismo , Ratas , Ratas Endogámicas F344 , Ratas Endogámicas , Especificidad de la Especie
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