Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 7 de 7
Filtrar
Mais filtros










Base de dados
Intervalo de ano de publicação
1.
J Holist Nurs ; : 8980101241265534, 2024 Jul 23.
Artigo em Inglês | MEDLINE | ID: mdl-39042182

RESUMO

Purpose: To identify the effects of Reiki on stress among Japanese nurses. Design: Mixed method and intervention design. Method: A nonprobability snowball sampling was used. Twenty-one nurses were invited to receive the Reiki intervention. Physical responses were measured by pulse rate, respiration rate, blood pressure rate, and salivary α-amylase activity pre- and postintervention. Psychological responses were evaluated by the mood dimensions and Total Mood Disturbance of the Profile of Mood States 2nd Edition. To obtain qualitative data, semistructured interviews were conducted after the intervention, and a web-based questionnaire was completed the following day. Findings: Twenty-one participants completed the study, and results indicated that the Reiki intervention significantly improved psychological stress reactions. No significant differences were found in physical stress. Two categories were identified from qualitative data: "positive effects" and "negative effects". Codes including "warm," "body feeling more comfortable," and "stress awareness" emerged as the positive effects. No adverse events were indicated. Conclusion: The results are the first step toward holistic nursing care in Japan and quantitative and qualitative data confirmed that Reiki improved the psychological aspect of stress responses of Japanese nurses.

2.
J Nutr Sci Vitaminol (Tokyo) ; 68(2): 112-119, 2022.
Artigo em Inglês | MEDLINE | ID: mdl-35491200

RESUMO

It is well known that branched-chain amino acids (BCAAs) promote protein synthesis in skeletal muscle and can cause muscle hypertrophy. However, it has also been reported that they may inhibit muscle atrophy induced by load-bearing and age-related changes. In this study, we investigated the effects of BCAA intake during joint fixation on the levels of protein kinase B (Akt), mammalian target of rapamycin (mTOR), and nebulin in a rat model of joint fixation. Akt and mTOR are signal factors of protein synthesis, whereas nebulin is a structural protein in the muscle. The effects of BCAAs on muscle atrophy were also investigated. The phosphorylation rate of mTOR was higher than that of Akt and increased with BCAA intake in the rat hind limb muscles (soleus) when the ankle joint was fixed. The relative level of nebulin and the phosphorylation rate of Neural Wiskott-Aldrich syndrome protein (N-WASP) also increased as a result of BCAA intake during fixation. This is important because nebulin and N-WASP are involved in the formation of the structure of sarcomere thin filaments. Furthermore, when the cross-sectional areas (CSAs) of different types of muscle fibers were measured during histological evaluation of muscle atrophy, it was found that the inhibitory effect of BCAA on muscle atrophy was higher in Type 1 fibers. Additionally, a positive correlation was found between nebulin level and the CSAs of the muscle fibers. It was found that there is a close relationship between the content of structural proteins and muscle atrophy.


Assuntos
Aminoácidos de Cadeia Ramificada , Proteínas Proto-Oncogênicas c-akt , Animais , Mamíferos/metabolismo , Proteínas Musculares , Atrofia Muscular/metabolismo , Proteínas Proto-Oncogênicas c-akt/metabolismo , Ratos , Serina-Treonina Quinases TOR
3.
Cancer Chemother Pharmacol ; 74(6): 1207-15, 2014 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-25267597

RESUMO

INTRODUCTION: Fluoropyrimidine plus platinum (FP)-based chemotherapy has been widely used as a first-line regimen for advanced or recurrent esophageal cancer, and taxanes have shown efficacy after FP-based chemotherapy, but there is no standard regimen for second-line chemotherapy (SLC). We retrospectively investigated the clinical features of taxane therapy in SLC for esophageal squamous cell carcinoma (ESCC). METHODS: The selection criteria were pathologically proven ESCC; advanced or recurrent disease previously treated with FP at our hospital; performance status (PS) 0-2; and adequate organ function. Docetaxel (DTX) was administered 3-weekly at 70 mg/m(2). Paclitaxel (PTX) was administered at 100 mg/m(2) weekly for 6 weeks, with 1 week's rest. RESULTS: The analysis covered 163 patients from August 2006 to June 2012. Median age was 64 years (range 37-83: DTX group 132 patients and PTX group 31). Progression-free survival and median overall survival (OS) were 2.3 and 6.1 months, respectively, with PTX and 2.3 and 5.3 months with DTX. Response rates were 20.7 % for PTX and 5.9 % for DTX. The rate of grades 3-4 neutropenia was higher with DTX (32.6 %) than with PTX (16.1 %). Grade 3 febrile neutropenia was seen in 6.1 % of DTX recipients but in no PTX group. According to multivariate analyses of OS, PS 2, number of metastatic sites ≧2, and CRP ≧1 mg/dL were independent predictors of poor prognosis. CONCLUSIONS: PTX and DTX were both effective in SLC for ESCC, but their toxicity profiles differed. In terms of febrile neutropenia, PTX seems more appropriate.


Assuntos
Antineoplásicos/uso terapêutico , Carcinoma de Células Escamosas/tratamento farmacológico , Neoplasias Esofágicas/tratamento farmacológico , Paclitaxel/uso terapêutico , Taxoides/uso terapêutico , Adulto , Idoso , Idoso de 80 Anos ou mais , Antineoplásicos/efeitos adversos , Antineoplásicos Fitogênicos/efeitos adversos , Antineoplásicos Fitogênicos/uso terapêutico , Carcinoma de Células Escamosas/patologia , Intervalo Livre de Doença , Docetaxel , Neoplasias Esofágicas/patologia , Carcinoma de Células Escamosas do Esôfago , Feminino , Humanos , Masculino , Pessoa de Meia-Idade , Análise Multivariada , Recidiva Local de Neoplasia , Neutropenia/induzido quimicamente , Neutropenia/epidemiologia , Paclitaxel/efeitos adversos , Platina/uso terapêutico , Prognóstico , Pirimidinas/uso terapêutico , Estudos Retrospectivos , Taxa de Sobrevida , Taxoides/efeitos adversos , Resultado do Tratamento
4.
Mol Biol Cell ; 17(10): 4364-78, 2006 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-16855023

RESUMO

Rapid and long-distance secretion of membrane components is critical for hyphal formation in filamentous fungi, but the mechanisms responsible for polarized trafficking are not well understood. Here, we demonstrate that in Candida albicans, the majority of the Golgi complex is redistributed to the distal region during hyphal formation. Randomly distributed Golgi puncta in yeast cells cluster toward the growing tip during hyphal formation, remain associated with the distal portion of the filament during its extension, and are almost absent from the cell body. This restricted Golgi localization pattern is distinct from other organelles, including the endoplasmic reticulum, vacuole and mitochondria, which remain distributed throughout the cell body and hypha. Hyphal-induced positioning of the Golgi and the maintenance of its structural integrity requires actin cytoskeleton, but not microtubules. Absence of the formin Bni1 causes a hyphal-specific dispersal of the Golgi into a haze of finely dispersed vesicles with a sedimentation density no different from that of normal Golgi. These results demonstrate the existence of a hyphal-specific, Bni1-dependent cue for Golgi integrity and positioning at the distal portion of the hyphal tip, and suggest that filamentous fungi have evolved a novel strategy for polarized secretion, involving a redistribution of the Golgi to the growing tip.


Assuntos
Candida albicans/crescimento & desenvolvimento , Proteínas Fúngicas/metabolismo , Complexo de Golgi/metabolismo , Hifas/crescimento & desenvolvimento , Proteínas dos Microfilamentos/metabolismo , Proteínas de Saccharomyces cerevisiae/metabolismo , Leveduras/crescimento & desenvolvimento , Actinas/fisiologia , Polaridade Celular , Células Cultivadas , Retículo Endoplasmático/metabolismo , Epitopos/genética , Imunofluorescência , Proteínas Fúngicas/genética , Proteínas Fúngicas/fisiologia , Genes Reporter/genética , Complexo de Golgi/ultraestrutura , Hifas/metabolismo , Proteínas dos Microfilamentos/genética , Proteínas dos Microfilamentos/fisiologia , Microtúbulos/fisiologia , Modelos Biológicos , Proteínas de Saccharomyces cerevisiae/genética , Proteínas de Saccharomyces cerevisiae/fisiologia , Transdução de Sinais , Vacúolos/metabolismo
5.
Glycobiology ; 14(6): 559-70, 2004 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-15044395

RESUMO

The early steps of N-linked glycosylation involve the synthesis of a lipid-linked oligosaccharide, Glc(3)Man(9)GlcNAc(2)-PP-dolichol, on the endoplasmic reticulum (ER) membrane. Prior to its lumenal translocation and transfer to nascent glycoproteins, mannosylation of Man(5)GlcNAc(2)-PP-dolichol is catalyzed by the Alg1, Alg2, and Alg11 mannosyltransferases. We provide evidence for a physical interaction between these proteins. Using a combination of biochemical and genetic assays, two distinct complexes that contain multiple copies of Alg1 were identified. The two Alg1-containing complexes differ from one another in that one complex contains Alg2 and the other contains Alg11. Alg1 self-assembles through a C-terminal domain that is distinct from the region required for its association with Alg2 or Alg11. Missense mutations affecting catalysis but not Alg1 protein stability or assembly with Alg2 or Alg11 were also identified. Overexpression of these catalytically inactive alleles resulted in dominant negative phenotypes, providing genetic evidence for functional Alg1-containing complexes in vivo. These data suggest that an additional level of regulation that ensures the fidelity of complex oligosaccharide structures involves the physical association of the related catalytic enzymes in the ER membrane.


Assuntos
Retículo Endoplasmático/enzimologia , Manosiltransferases/metabolismo , Proteínas de Saccharomyces cerevisiae/metabolismo , Sequência de Aminoácidos , Biopolímeros , Catálise , Manosiltransferases/química , Dados de Sequência Molecular , Ligação Proteica , Proteínas de Saccharomyces cerevisiae/química , Homologia de Sequência de Aminoácidos
6.
Yeast ; 19(8): 691-8, 2002 Jun 15.
Artigo em Inglês | MEDLINE | ID: mdl-12185838

RESUMO

Mannoproteins on the cell wall of yeast and fungi help regulate cell shape, porosity, and cell-cell interactions, including those required for attachment to host cells by fungal pathogens. The mannose-containing oligosaccharides on proteins and lipids are extended in the Golgi by glycosyltransferases that use GDP-mannose as the sugar substrate. A membrane-bound transporter that, in Saccharomyces cerevisiae, is encoded by the VRG4 gene catalyses delivery of GDP-mannose into the lumen of the Golgi. We report here the cloning of the homologous VRG4 gene from the pathogenic yeast, Candida glabrata, by functional complementation of an S. cerevisiae vrg4 mutant. The sequence of the CgVrg4 protein displays significant homology to GDP-mannose transporters from other yeast, fungi, protozoa, and plants. CgVRG4 fully complements the glycosylation defect and other cell wall associated vrg4 mutant phenotypes. Like ScVRG4, CgVRG4 is essential for the viability of C. glabrata. These results suggest that, as in S. cerevisiae, CgVrg4p accounts for all of the GDP-mannose transport activity in the Golgi lumen.


Assuntos
Candida glabrata/genética , Proteínas de Transporte/genética , Proteínas de Membrana Transportadoras/genética , Proteínas de Saccharomyces cerevisiae/genética , Saccharomyces cerevisiae/genética , Sequência de Aminoácidos , Sequência de Bases , Candida glabrata/metabolismo , Proteínas de Transporte/metabolismo , DNA Fúngico/química , DNA Fúngico/genética , Regulação Fúngica da Expressão Gênica , Biblioteca Gênica , Teste de Complementação Genética , Complexo de Golgi/enzimologia , Proteínas de Membrana Transportadoras/metabolismo , Dados de Sequência Molecular , Saccharomyces cerevisiae/metabolismo , Proteínas de Saccharomyces cerevisiae/metabolismo , Análise de Sequência de DNA , Homologia de Sequência de Aminoácidos
7.
J Bacteriol ; 184(1): 29-42, 2002 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-11741841

RESUMO

Cell surface mannan is implicated in almost every aspect of pathogenicity of Candida albicans. In Saccharomyces cerevisiae, the Vrg4 protein acts as a master regulator of mannan synthesis through its role in substrate provision. The substrate for mannosylation of proteins and lipids in the Golgi apparatus is GDP-mannose, whose lumenal transport is catalyzed by Vrg4p. This nucleotide sugar is synthesized in the cytoplasm by pathways that are highly conserved in all eukaryotes, but its lumenal transport (and hence Golgi apparatus-specific mannosylation) is a fungus-specific process. To begin to study the role of Golgi mannosylation in C. albicans, we isolated the CaVRG4 gene and analyzed the effects of loss of its function. CaVRG4 encodes a functional homologue of the S. cerevisiae GDP-mannose transporter. CaVrg4p localized to punctate spots within the cytoplasm of C. albicans in a pattern reminiscent of localization of Vrg4p in the Golgi apparatus in S. cerevisiae. Like partial loss of ScVRG4 function, partial loss of CaVRG4 function resulted in mannosylation defects, which in turn led to a number of cell wall-associated phenotypes. While heterozygotes displayed no growth phenotypes, a hemizygous strain, containing a single copy of CaVRG4 under control of the methionine-repressible MET3 promoter, did not grow in the presence of methionine and cysteine, demonstrating that CaVRG4 is essential for viability. Mutant Candida vrg4 strains were defective in hyphal formation but exhibited a constitutive polarized mode of pseudohyphal growth. Because the VRG4 gene is essential for yeast viability but does not have a mammalian homologue, it is a particularly attractive target for development of antifungal therapies.


Assuntos
Candida albicans/genética , Proteínas Fúngicas/genética , Complexo de Golgi/genética , Mananas/biossíntese , Proteínas de Membrana Transportadoras/genética , Sequência de Aminoácidos , Candida albicans/citologia , Candida albicans/metabolismo , Candida albicans/patogenicidade , Proteínas Fúngicas/metabolismo , Genes Essenciais , Genes Fúngicos , Glicosilação , Complexo de Golgi/metabolismo , Proteínas de Membrana Transportadoras/metabolismo , Dados de Sequência Molecular , Morfogênese , Mutação , Proteínas de Saccharomyces cerevisiae/genética , Proteínas de Saccharomyces cerevisiae/metabolismo , Homologia de Sequência de Aminoácidos
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA