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Revisiting the roles of VHR/DUSP3 phosphatase in human diseases
Russo, Lilian Cristina; Farias, Jéssica Oliveira; Ferruzo, Pault Yeison Minaya; Monteiro, Lucas Falcão; Forti, Fábio Luís.
Afiliação
  • Russo, Lilian Cristina; Universidade de Sao Paulo. Instituto de Quimica. Departamento de Bioquímica. Sao Paulo. BR
  • Farias, Jéssica Oliveira; Universidade de Sao Paulo. Instituto de Quimica. Departamento de Bioquímica. Sao Paulo. BR
  • Ferruzo, Pault Yeison Minaya; Universidade de Sao Paulo. Instituto de Quimica. Departamento de Bioquímica. Sao Paulo. BR
  • Monteiro, Lucas Falcão; Universidade de Sao Paulo. Instituto de Quimica. Departamento de Bioquímica. Sao Paulo. BR
  • Forti, Fábio Luís; Universidade de Sao Paulo. Instituto de Quimica. Departamento de Bioquímica. Sao Paulo. BR
Clinics ; Clinics;73(supl.1): e466s, 2018. graf
Article em En | LILACS | ID: biblio-952823
Biblioteca responsável: BR1.1
ABSTRACT
Protein tyrosine phosphatases have long been considered key regulators of biological processes and are therefore implicated in the origins of various human diseases. Heterozygosity, mutations, deletions, and the complete loss of some of these enzymes have been reported to cause neurodegenerative diseases, autoimmune syndromes, genetic disorders, metabolic diseases, cancers, and many other physiological imbalances. Vaccinia H1-related phosphatase, also known as dual-specificity phosphatase 3, is a protein tyrosine phosphatase enzyme that regulates the phosphorylation of the mitogen-activated protein kinase signaling pathway, a central mediator of a diversity of biological responses. It has been suggested that vaccinia H1-related phosphatase can act as a tumor suppressor or tumor-promoting phosphatase in different cancers. Furthermore, emerging evidence suggests that this enzyme has many other biological functions, such as roles in immune responses, thrombosis, hemostasis, angiogenesis, and genomic stability, and this broad spectrum of vaccinia H1-related phosphatase activity is likely the result of its diversity of substrates. Hence, fully identifying and characterizing these substrate-phosphatase interactions will facilitate the identification of pharmacological inhibitors of vaccinia H1-related phosphatase that can be evaluated in clinical trials. In this review, we describe the biological processes mediated by vaccinia H1-related phosphatase, especially those related to genomic stability. We also focus on validated substrates and signaling circuitry with clinical relevance in human diseases, particularly oncogenesis.
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Texto completo: 1 Coleções: 01-internacional Base de dados: LILACS Assunto principal: Fosfatase 3 de Especificidade Dupla / Neoplasias Limite: Humans Idioma: En Revista: Clinics Assunto da revista: MEDICINA Ano de publicação: 2018 Tipo de documento: Article País de afiliação: Brasil País de publicação: Brasil

Texto completo: 1 Coleções: 01-internacional Base de dados: LILACS Assunto principal: Fosfatase 3 de Especificidade Dupla / Neoplasias Limite: Humans Idioma: En Revista: Clinics Assunto da revista: MEDICINA Ano de publicação: 2018 Tipo de documento: Article País de afiliação: Brasil País de publicação: Brasil