RESUMO

BACKGROUND: Bisphosphonate-related osteonecrosis is an infrequent but potentially serious complication. Its treatment remains complex, and in some cases can be mutilating. Prevention, a correct diagnosis and opportune management are crucial. MATERIAL AND METHODS: A cross-sectional study was made, interviewing 410 dentists with the aim of assessing their knowledge of the subject. RESULTS: Practically all of the dental professionals (99.7%) were found to lack sufficient knowledge of the prevention, diagnosis and management of bisphosphonate-related osteonecrosis. CONCLUSIONS: Actions including increased diffusion in the professional media and inclusion of the subject in training programs are needed in order to enhance the knowledge of bisphosphonate-related osteonecrosis among dentists and thus prevent complications in this group of patients.

Assuntos

Osteonecrose da Arcada Osseodentária Associada a Difosfonatos , Odontologia , Conhecimentos, Atitudes e Prática em Saúde , Osteonecrose da Arcada Osseodentária Associada a Difosfonatos/diagnóstico , Osteonecrose da Arcada Osseodentária Associada a Difosfonatos/etiologia , Osteonecrose da Arcada Osseodentária Associada a Difosfonatos/terapia , Estudos Transversais , Humanos , México , Fatores de Risco , Autorrelato

RESUMO

This paper reports the EhGEF1-EhRacG and EhGEF1-EhRho1 molecular complexes from Entamoeba histolytica. The not conserved amino acids Gln201,Tyr299, Gln302, Lys312, Asn313, Phe314 and Ile324 were localized, by means of an in silico computational analysis, at the interface of the exposed face from the DH domain of EhGEF1, which are important to establish the contact with its target GTPases EhRacG and EhRho1. Functional studies of nucleotide exchange of Phe314Ala mutant showed a decrement of 80% on EhRacG GTPase; in contrast the Ile324Ala mutant exhibited a reduction of 77%, specifically on EhRho1; meanwhile the Gln302Ala mutant showed a reduction of approximately 50% on the exchange activity for both GTPases. Moreover, the functional studies of the protein EhGEF1 mutants in the conserved residues Thr194Ala, Asn366Ala and Glu367Ala indicated that contrary to what has been reported for other systems, the mutation of these residues did not alter considerably its catalytic activity.

Assuntos

Canais de Cloreto/química , Canais de Cloreto/genética , Entamoeba histolytica/fisiologia , Proteínas de Protozoários/química , Proteínas de Protozoários/genética , Sequência de Aminoácidos , Substituição de Aminoácidos/genética , Animais , Canais de Cloreto/metabolismo , Análise Mutacional de DNA , Entamoeba histolytica/genética , Proteínas de Ligação ao GTP/metabolismo , Guanosina Trifosfato/metabolismo , Modelos Moleculares , Dados de Sequência Molecular , Mutação de Sentido Incorreto , Ligação Proteica , Mapeamento de Interação de Proteínas , Estrutura Quaternária de Proteína , Proteínas de Protozoários/metabolismo