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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Protein disulfide isomerases: Redox connections in and out of the endoplasmic reticulum

Texto completo
Autor(es):
Soares Moretti, Ana Iochabel ; Martins Laurindo, Francisco Rafael
Número total de Autores: 2
Tipo de documento: Artigo Científico
Fonte: Archives of Biochemistry and Biophysics; v. 617, n. SI, p. 106-119, MAR 1 2017.
Citações Web of Science: 29
Resumo

Protein disulfide isomerases are thiol oxidoreductase chaperones from thioredoxin superfamily. As redox folding catalysts from the endoplasmic reticulum (ER), their roles in ER-related redox homeostasis and signaling are well-studied. PDIA1 exerts thiol oxidation/reduction and isomerization, plus chaperone effects. Also, substantial evidence indicates that PDIs regulate thiol-disulfide switches in other cell locations such as cell surface and possibly cytosol. Subcellular PDI translocation routes remain unclear and seem Golgi-independent. The list of signaling and structural proteins reportedly regulated by PDIs keeps growing, via thiol switches involving oxidation, reduction and isomerization, S-(de)nytrosylation, (de) glutathyonylation and protein oligomerization. PDIA1 is required for agonist-triggered Nox NADPH oxidase activation and cell migration in vascular cells and macrophages, while PDIA1-dependent cytoskeletal regulation appears a converging pathway. Extracellularly, PDIs crucially regulate thiol redox signaling of thrombosis/platelet activation, e.g., integrins, and PDIA1 supports expansive caliber remodeling during injury repair via matrix/cytoskeletal organization. Some proteins display regulatory PDI-like motifs. PDI effects are orchestrated by expression levels or post-translational modifications. PDI is redox-sensitive, although probably not a mass-effect redox sensor due to kinetic constraints. Rather, the ``all-in-one{''} organization of its peculiar redox/chaperone properties likely provide PDIs with precision and versatility in redox signaling, making them promising therapeutic targets. (C) 2016 Published by Elsevier Inc. (AU)

Processo FAPESP: 11/50469-0 - Interação entre dissulfeto isomera interação entre dissulfeto isomerase proteica, rhogdie GTPases da família Rho e ras:identificacao de complexos proteicos
Beneficiário:Ana Iochabel Soares Moretti
Linha de fomento: Bolsas no Brasil - Pós-Doutorado
Processo FAPESP: 13/07937-8 - Redoxoma
Beneficiário:Ohara Augusto
Linha de fomento: Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs
Processo FAPESP: 14/23657-8 - Estudo funcional da interação entre a proteína disulfeto isomerase (PDI) e a proteína ligante de actina, Profilina 1
Beneficiário:Ana Iochabel Soares Moretti
Linha de fomento: Bolsas no Exterior - Estágio de Pesquisa - Pós-Doutorado
Processo FAPESP: 09/54764-6 - Regulação da homeostase redox e resposta integrada a estresse pela dissulfeto isomerase protéica (PDI): mecanismos e papel na fisiopatologia e terapêutica de doenças vasculares
Beneficiário:Francisco Rafael Martins Laurindo
Linha de fomento: Auxílio à Pesquisa - Temático