Cysteine mediated disulfide bond formation in RAGE V domain facilitates its functionally relevant dimerization.
Biochimie
; 154: 55-61, 2018 Nov.
Article
em En
| MEDLINE
| ID: mdl-30076903
ABSTRACT
Receptor for Advanced Glycation End product (RAGE) is a multiligand receptor implicated in diverse pathological conditions such as diabetes, atherosclerosis, cancer and neural diseases. Extracellular, RAGE consists of V, C1 and C2 domains. Here, we show RAGE exists as a monomer in equilibrium with a fraction of a covalently linked dimer of monomers via its V domain through cysteine. In order to understand the functional implication of this dimer, we examined the binding capacity and functional potential of RAGE dimer via advanced glycation end products (AGEs) which shows enhanced binding capacity towards V domain, ERK phosphorylation, cytokine release and actin polymerization ability of the dimeric form for AGEs compared with the reduced monomeric form. Our data, suggests that the dimeric state of RAGE controls its function and ligand mediated signaling which may play important role in RAGE mediated various diseases.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Cisteína
/
Dissulfetos
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Multimerização Proteica
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Receptor para Produtos Finais de Glicação Avançada
Limite:
Animals
/
Humans
Idioma:
En
Revista:
Biochimie
Ano de publicação:
2018
Tipo de documento:
Article