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Measurement and meaning of cellular thiol:disufhide redox status.
Comini, Marcelo A.
Afiliação
  • Comini MA; a Laboratory Redox Biology of Trypanosomes , Institut Pasteur de Montevideo , Mataojo 2020 , Montevideo , Uruguay.
Free Radic Res ; 50(2): 246-71, 2016.
Article em En | MEDLINE | ID: mdl-26695718
The functional group of cysteine is a thiol group (SH) that, due to its chemical reactivity, is able to undergo a wide array of modifications each with the potential to confer a different property or function to the molecule harboring this residue. Most of these modifications involve the reversible oxidation of the thiol to sulfenic acid (SOH), and disulfide, including intra- and intermolecular disulfides between polypeptides and glutathione (glutathionylation). The reversibility of these oxidations allows thiol groups to serve as versatile chemical and structural transducing elements in several low molecular mass metabolites and proteins. A plethora of cellular functions such as DNA and protein synthesis, protein secretion, cytoskeleton architecture, differentiation, apoptosis, and anti-oxidant defense, are recognized to be modulated, at certain stage, by thiol-disulfide exchange mechanisms of redox active thiol groups. All organisms are equipped with enzymatic systems composed by NADPH-dependent reductases, redoxins, and peroxidases that provide kinetic control of global thiol-redox homeostasis as well as target selectivity. These redox systems are distributed in different subcellular compartments and are not in equilibrium with each other. In consequence, measuring cellular thiol-disulfide status represents a challenge for studies aimed to obtain dynamic and spatio-temporal resolution. This review provides a summary of the methods and tools available to quantify the thiol redox status of cells.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Compostos de Sulfidrila / Proteínas / Técnicas de Química Analítica / Proteômica / Dissulfetos / Glutationa Limite: Animals / Humans Idioma: En Revista: Free Radic Res Assunto da revista: BIOQUIMICA Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Uruguai País de publicação: Reino Unido

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Compostos de Sulfidrila / Proteínas / Técnicas de Química Analítica / Proteômica / Dissulfetos / Glutationa Limite: Animals / Humans Idioma: En Revista: Free Radic Res Assunto da revista: BIOQUIMICA Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Uruguai País de publicação: Reino Unido