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2.
Int J Dent Hyg ; 13(3): 222-7, 2015 Aug.
Artigo em Inglês | MEDLINE | ID: mdl-25677614

RESUMO

We investigated awareness in dental hygienists of bisphosphonate-related osteonecrosis of the jaw (BRONJ) in patients with osteoporosis and cancer and assessed the situation in systemic history investigations to broaden the scope of the dental hygienists' BRONJ awareness as a basis for contributing to preventing this disease. The study was carried out through a survey; 217 dental hygienists responded to the survey. They worked at 12 university and general hospitals, 10 dental hospitals and 35 dental clinics, for a total of 57 institutions in Seoul. The survey consisted of 37 questions: general characteristics (J Oral Maxillofac Surg 65: 2007; 369), systemic history investigations (Ruggiero et al. J Oral Maxillofac Surg 62: 2004; 527) and awareness of BRONJ (Park et al. J Korean Dent Assoc 49: 2011; 389). Among them, 79.7% were aware of BRONJ. Recognition was highest among those from 25 to 35 years old (P < 0.05). In terms of work experience, those with 5-10 years experience showed the highest awareness (P < 0.05). In terms of institutions type, dental clinics showed lower awareness than general and dental hospitals (P < 0.05). It was found that 55.3% of the dental hygienists had been educated about BRONJ. Those aged 25-35 years were the most educated. In terms of institutions, dental clinic staff were the least educated. The degree of understanding about BRONJ was analysed with the average score of 6.14 points. According to these results, dental hygienists working in university hospitals and general hospitals had more opportunity to receive training than those working in dental clinics. Thus, it is considered that the development of professional training programs about BRONJ for all dental hygienists is necessary.


Assuntos
Atitude do Pessoal de Saúde , Osteonecrose da Arcada Osseodentária Associada a Difosfonatos/fisiopatologia , Higienistas Dentários/educação , Adulto , Clínicas Odontológicas , Higienistas Dentários/psicologia , Unidade Hospitalar de Odontologia , Educação Continuada , Hospitais Gerais , Hospitais Especializados , Hospitais de Ensino , Humanos , Consentimento Livre e Esclarecido , Capacitação em Serviço , Relações Interprofissionais , Anamnese , Prática Profissional , República da Coreia , Fatores de Tempo , Local de Trabalho
3.
Oncogene ; 34(11): 1354-62, 2015 Mar 12.
Artigo em Inglês | MEDLINE | ID: mdl-24681946

RESUMO

Hypoxia-inducible factor-1α (HIF-1α) is a transcription factor that has a central role in the regulation of tumour metabolism under hypoxic conditions. HIF-1α stimulates glycolytic energy production and promotes tumour growth. Sirtuins are NAD(+)-dependent protein deacetylases that regulate cellular metabolism in response to stress; however, their involvement in the hypoxic response remains unclear. In this study, it is shown that SIRT2-mediated deacetylation of HIF-1α regulates its stability in tumour cells. SIRT2 overexpression destabilized HIF-1α under hypoxic conditions, whereas HIF-1α protein levels were high in SIRT2-deficient cells. SIRT2 directly interacted with HIF-1α and deacetylated Lys709 of HIF-1α. Deacetylation of HIF-1α by SIRT2 resulted in increased binding affinity for prolyl hydroxylase 2, a key regulator of HIF-1α stability, and increased HIF-1α hydroxylation and ubiquitination. Moreover, a pharmacological agent that increased the intracellular NAD(+)/NADH ratio led to the degradation of HIF-1α by increasing SIRT2-mediated deacetylation and subsequent hydroxylation. These findings suggest that SIRT2-mediated HIF-1α deacetylation is critical for the destablization of HIF-1α and the hypoxic response of tumour cells.


Assuntos
Hipóxia Celular/genética , Subunidade alfa do Fator 1 Induzível por Hipóxia/metabolismo , Sirtuína 2/metabolismo , Animais , Linhagem Celular Tumoral , Metabolismo Energético/genética , Feminino , Células HeLa , Humanos , Hidroxilação , Camundongos , Camundongos Endogâmicos BALB C , Camundongos Nus , NAD/metabolismo , Prolil Hidroxilases/metabolismo , Ligação Proteica , Estabilidade Proteica , Interferência de RNA , RNA Interferente Pequeno , Sirtuína 2/genética , Ubiquitinação
4.
Can J Microbiol ; 42(2): 177-82, 1996 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-8742358

RESUMO

Two genes, designated repA and repB, are involved in the regulation of the synthesis of extracellular pectate lyase, protease, and alginate in Pseudomonas viridiflava. The repA gene has been shown to encode a protein highly homologous to several bacterial sensors in the two-component regulator family including the LemA of Pseudomonas syringae. In this study, the repB locus, initially identified in a 6.3-kb EcoRI genomic fragment of P. viridiflava, was further characterized. Results obtained from restriction mapping, deletion subclonings, and mini-Mu-LacZ fusions indicated that the repB gene was contained within a 0.8-kb HindIII-PstI region. Sequence analysis of this repB region revealed the presence of an open reading frame, which was predicted to encode a protein similar or identical to the gacA response regulator found in P. syringae and Pseudomonas fluorescens. The repB gene of P. viridiflava also regulated the production of fluorescent siderophores, in addition to the aforementioned extracellular enzymes and alginate. The repB or gacA homologs were detected in the genomes of nine other strains of P. viridiflava, P. fluorescens, and P. syringae included in the study. The data presented here and earlier indicate that the repA/repB gene regulatory system of P. viridiflava is analogous to the lemA/gacA system of P. syringae and P. fluorescens.


Assuntos
Proteínas de Bactérias/biossíntese , Regulação Bacteriana da Expressão Gênica , Genes Bacterianos , Pseudomonas/genética , Pseudomonas/metabolismo , Sideróforos/biossíntese , Alginatos/metabolismo , Sequência de Aminoácidos , Proteínas de Bactérias/genética , Sequência de Bases , Clonagem Molecular , Endopeptidases/biossíntese , Regulação Enzimológica da Expressão Gênica , Ácido Glucurônico , Ácidos Hexurônicos , Dados de Sequência Molecular , Plasmídeos , Polissacarídeo-Liases/biossíntese , Proteínas Recombinantes de Fusão/biossíntese , Proteínas Repressoras/biossíntese , Proteínas Repressoras/genética , Mapeamento por Restrição , Especificidade da Espécie
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