Your browser doesn't support javascript.
loading
An Update to Calcium Binding Proteins.
Elíes, Jacobo; Yáñez, Matilde; Pereira, Thiago M C; Gil-Longo, José; MacDougall, David A; Campos-Toimil, Manuel.
Afiliação
  • Elíes J; Pharmacology and Experimental Therapeutics, Faculty of Life Sciences, University of Bradford, Bradford, UK.
  • Yáñez M; Pharmacology of Chronic Diseases (CD Pharma), Centro de Investigación en Medicina Molecular y Enfermedades Crónicas (CIMUS), Universidad de Santiago de Compostela, Santiago de Compostela, Spain.
  • Pereira TMC; Pharmaceutical Sciences Graduate Program, Vila Velha University (UVV), Vila Velha, ES, Brazil.
  • Gil-Longo J; Federal Institute of Education, Science and Technology (IFES), Vila Velha, ES, Brazil.
  • MacDougall DA; Pharmacology and Experimental Therapeutics, Faculty of Life Sciences, University of Bradford, Bradford, UK.
  • Campos-Toimil M; Research and Enterprise, University of Huddersfield, Huddersfield, UK.
Adv Exp Med Biol ; 1131: 183-213, 2020.
Article em En | MEDLINE | ID: mdl-31646511
ABSTRACT
Ca2+ binding proteins (CBP) are of key importance for calcium to play its role as a pivotal second messenger. CBP bind Ca2+ in specific domains, contributing to the regulation of its concentration at the cytosol and intracellular stores. They also participate in numerous cellular functions by acting as Ca2+ transporters across cell membranes or as Ca2+-modulated sensors, i.e. decoding Ca2+ signals. Since CBP are integral to normal physiological processes, possible roles for them in a variety of diseases has attracted growing interest in recent years. In addition, research on CBP has been reinforced with advances in the structural characterization of new CBP family members. In this chapter we have updated a previous review on CBP, covering in more depth potential participation in physiopathological processes and candidacy for pharmacological targets in many diseases. We review intracellular CBP that contain the structural EF-hand domain parvalbumin, calmodulin, S100 proteins, calcineurin and neuronal Ca2+ sensor proteins (NCS). We also address intracellular CBP lacking the EF-hand domain annexins, CBP within intracellular Ca2+ stores (paying special attention to calreticulin and calsequestrin), proteins that contain a C2 domain (such as protein kinase C (PKC) or synaptotagmin) and other proteins of interest, such as regucalcin or proprotein convertase subtisilin kexins (PCSK). Finally, we summarise the latest findings on extracellular CBP, classified according to their Ca2+ binding structures (i) EF-hand domains; (ii) EGF-like domains; (iii) ɣ-carboxyl glutamic acid (GLA)-rich domains; (iv) cadherin domains; (v) Ca2+-dependent (C)-type lectin-like domains; (vi) Ca2+-binding pockets of family C G-protein-coupled receptors.
Assuntos
Palavras-chave

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Ligação ao Cálcio Limite: Humans Idioma: En Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Ligação ao Cálcio Limite: Humans Idioma: En Ano de publicação: 2020 Tipo de documento: Article