Your browser doesn't support javascript.
loading
O-GlcNAcylation in Renal (Patho)Physiology.
Silva-Aguiar, Rodrigo P; Peruchetti, Diogo B; Pinheiro, Ana Acacia S; Caruso-Neves, Celso; Dias, Wagner B.
Afiliação
  • Silva-Aguiar RP; Carlos Chagas Filho Institute of Biophysics, Federal University of Rio de Janeiro, Rio de Janeiro 21941-901, Brazil.
  • Peruchetti DB; Carlos Chagas Filho Institute of Biophysics, Federal University of Rio de Janeiro, Rio de Janeiro 21941-901, Brazil.
  • Pinheiro AAS; Carlos Chagas Filho Institute of Biophysics, Federal University of Rio de Janeiro, Rio de Janeiro 21941-901, Brazil.
  • Caruso-Neves C; Rio de Janeiro Innovation Network in Nanosystems for Health-NanoSAÚDE/FAPERJ, Rio de Janeiro 21045-900, Brazil.
  • Dias WB; Carlos Chagas Filho Institute of Biophysics, Federal University of Rio de Janeiro, Rio de Janeiro 21941-901, Brazil.
Int J Mol Sci ; 23(19)2022 Sep 24.
Article em En | MEDLINE | ID: mdl-36232558
ABSTRACT
Kidneys maintain internal milieu homeostasis through a well-regulated manipulation of body fluid composition. This task is performed by the correlation between structure and function in the nephron. Kidney diseases are chronic conditions impacting healthcare programs globally, and despite efforts, therapeutic options for its treatment are limited. The development of chronic degenerative diseases is associated with changes in protein O-GlcNAcylation, a post-translation modification involved in the regulation of diverse cell function. O-GlcNAcylation is regulated by the enzymatic balance between O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) which add and remove GlcNAc residues on target proteins, respectively. Furthermore, the hexosamine biosynthetic pathway provides the substrate for protein O-GlcNAcylation. Beyond its physiological role, several reports indicate the participation of protein O-GlcNAcylation in cardiovascular, neurodegenerative, and metabolic diseases. In this review, we discuss the impact of protein O-GlcNAcylation on physiological renal function, disease conditions, and possible future directions in the field.
Assuntos
Palavras-chave

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Acetilglucosamina / N-Acetilglucosaminiltransferases Idioma: En Revista: Int J Mol Sci Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Brasil

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Acetilglucosamina / N-Acetilglucosaminiltransferases Idioma: En Revista: Int J Mol Sci Ano de publicação: 2022 Tipo de documento: Article País de afiliação: Brasil