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1.
J Phys Ther Sci ; 29(10): 1817-1818, 2017 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-29184295

RESUMO

[Purpose] The purpose of this study was to investigate the effect of jaw opening exercise (JOE) on aspiration in patients with dysphagia after stroke. [Subjects and Methods] Three subjects were recruited. Isometric and isotonic JOE were performed using a rubber ball, 5 days a week for 4 weeks. Aspiration was evaluated using the penetration-a spiration scale (PAS) based on a videofluoroscopic swallowing study. [Results] All subjects showed a score reduction of at least 1 point and a maximum reduction of 2 points in the PAS in the liquid type. [Conclusion] This study confirmed that JOE can be used to reduce aspiration in patients with dysphagia after stroke.

2.
J Gene Med ; 13(10): 549-55, 2011 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-21898720

RESUMO

BACKGROUND: The therapeutic potential of pCK-HGF-X7, a naked DNA designed to express two isoforms of hepatocyte growth factor (HGF(723) and HGF(728) ), was studied in the rat ischemic heart disease model. METHODS: First, the kinetics of gene expression was examined by injecting pCK-HGF-X7 DNA into the rat heart. Second, the cardioprotective effects were compared between the two naked DNA constructs, expressing a single (HGF(728) ) or both isoforms (HGF(728) and HGF(723) ) of HGF, in the rat ischemic heart disease model. The ischemic injury to the rat heart was created by ischemia-reperfusion in the anterior descending artery. The respective naked DNA constructs were injected into the anterior wall of the rat heart with the ischemia-reperfusion injury. Cardiac function, capillary density and anti-fibrotic activity were compared between the two naked DNA constructs. RESULTS: The intramyocardial administration of pCK-HGF-X7 resulted in transient and localized HGF expression for 3 weeks. At its peak, approximately 678 pg (per mg of tissue protein) of HGF was produced in the injected heart without an increase of HGF protein level in other tissues, and serum. pCK-HGF-X7 more efficiently improved the left ventricular ejection fraction and the systolic anterior wall thickness, increased the capillary density, and inhibited myocardial fibrosis, in a statistically significant manner, compared to the identical vector encoding HGF(728) only. CONCLUSIONS: These results demonstrate that transfer of the genomic-cDNA hybrid expressing both isoforms of the HGF gene might provide higher therapeutic effects than the cDNA sequence producing HGF(728) alone in the treatment of ischemic heart disease.


Assuntos
DNA/metabolismo , Terapia Genética/métodos , Fator de Crescimento de Hepatócito/metabolismo , Isquemia Miocárdica/fisiopatologia , Isquemia Miocárdica/terapia , Plasmídeos/genética , Isoformas de Proteínas/metabolismo , Animais , DNA/genética , Modelos Animais de Doenças , Técnicas de Transferência de Genes , Fator de Crescimento de Hepatócito/genética , Masculino , Isoformas de Proteínas/genética , Ratos , Ratos Sprague-Dawley
3.
CrystEngComm ; 12(11): 3467-3470, 2010 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-21113424

RESUMO

Three different ZnO nanoplate arrays on Si-wafer were successfully synthesized at 95 °C from ZnO nanoparticles with modified surface by citrate anion. Shape, size, density, and orientation of the resulting nanoplates were dramatically changed by the nucleus seed concentration, which was controlled through different coating processes on the substrate.

4.
Cell Signal ; 20(5): 884-91, 2008 May.
Artigo em Inglês | MEDLINE | ID: mdl-18262754

RESUMO

Heterotrimeric GTP-binding proteins (G proteins) mediate signal transduction generated by neurotransmitters and hormones. Go, a member of the Go/Gi family, is the most abundant heterotrimeric G protein in the brain. Most mechanistic analyses on Go activation demonstrate that its action is mediated by the Gbetagamma dimer; downstream effectors for its alpha subunit (Goalpha) have not been clearly defined. Here, we employ the yeast two-hybrid system to screen for Goalpha-interacting partners in a cDNA library from human fetal brain. The transcription factor promyelocytic leukemia zinc finger protein (PLZF) specifically bound to Goalpha. Interactions between PLZF and Goalpha were confirmed using in vitro and in vivo affinity binding assays. Activated Goalpha interacted directly with PLZF, and enhanced its function as a transcriptional and cell growth suppressor. Notably, PLZF activity was additionally promoted by the Go/ialpha-coupled cannabinoid receptor (CB) in HL60 cells endogenously expressing CB and PLZF. These results collectively suggest that Goalpha modulates the function of PLZF via direct interactions. Our novel findings provide insights into the diverse cellular roles of Goalpha and its coupled receptor.


Assuntos
Subunidades alfa Gi-Go de Proteínas de Ligação ao GTP/metabolismo , Fatores de Transcrição Kruppel-Like/metabolismo , Animais , Sequência de Bases , Linhagem Celular , Proliferação de Células , Primers do DNA/genética , Subunidades alfa Gi-Go de Proteínas de Ligação ao GTP/genética , Biblioteca Gênica , Humanos , Técnicas In Vitro , Fatores de Transcrição Kruppel-Like/genética , Camundongos , Complexos Multiproteicos , Proteína com Dedos de Zinco da Leucemia Promielocítica , Ligação Proteica , Receptores de Canabinoides/metabolismo , Proteínas Recombinantes de Fusão/genética , Proteínas Recombinantes de Fusão/metabolismo , Transdução de Sinais , Técnicas do Sistema de Duplo-Híbrido
5.
Cell Mol Biol Lett ; 14(1): 46-56, 2009.
Artigo em Inglês | MEDLINE | ID: mdl-18953495

RESUMO

Go, one of the most abundant heterotrimeric G proteins in the brain, is classified as a member of the Gi/Go family based on its homology to Gi proteins. Recently, we identified promyelocytic leukemia zinc finger protein (PLZF) as a candidate downstream effector for the alpha subunit of Go (Galphao). Activated Galphao interacts with PLZF and augments its function as a repressor of transcription and cell growth. G protein-coupled receptor-mediated Galphao activation also enhanced PLZF function. In this study, we determined that the GTPase domain of Galphao contributes to Galphao:PLZF interaction. We also showed that the Galphao GTPase domain is important in modulating the function of PLZF. This data indicates that the GTPase domain of Galphao may be necessary for the functional interaction of Galphao with PLZF.


Assuntos
GTP Fosfo-Hidrolases/química , Subunidades alfa Gi-Go de Proteínas de Ligação ao GTP/química , Subunidades alfa Gi-Go de Proteínas de Ligação ao GTP/metabolismo , Fatores de Transcrição Kruppel-Like/metabolismo , Proliferação de Células , Ciclina A/metabolismo , Humanos , Ligação Proteica , Estrutura Terciária de Proteína , Deleção de Sequência , Relação Estrutura-Atividade
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