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Apelin receptor dimer: Classification, future prospects, and pathophysiological perspectives.
Hu, Shujuan; Wang, Dexiu; Liu, Wenkai; Wang, Yixiang; Chen, Jing; Cai, Xin.
Afiliación
  • Hu S; School of Basic Medical Sciences, Shandong Second Medical University, Weifang, Shandong 261042, PR China.
  • Wang D; School of Basic Medical Sciences, Shandong Second Medical University, Weifang, Shandong 261042, PR China.
  • Liu W; School of Basic Medical Sciences, Shandong Second Medical University, Weifang, Shandong 261042, PR China.
  • Wang Y; School of Clinical Medicine, Shandong Second Medical University, Weifang, Shandong 261042, PR China.
  • Chen J; Neurobiology Institute, Jining Medical University, Jining, Shandong 272067, PR China; Division of Biomedical Sciences, Warwick Medical School, University of Warwick, Coventry CV4 7AL, UK. Electronic address: Jing.Chen@warwick.ac.uk.
  • Cai X; School of Basic Medical Sciences, Shandong Second Medical University, Weifang, Shandong 261042, PR China. Electronic address: caixin@sdsmu.edu.cn.
Biochim Biophys Acta Mol Basis Dis ; 1870(6): 167257, 2024 08.
Article en En | MEDLINE | ID: mdl-38795836
ABSTRACT
Apelin receptor (APJ), a member of the class A family of G protein-coupled receptor (GPCR), plays a crucial role in regulating cardiovascular and central nervous systems function. APJ influences the onset and progression of various diseases such as hypertension, atherosclerosis, and cerebral stroke, making it an important target for drug development. Our preliminary findings indicate that APJ can form homodimers, heterodimers, or even higher-order oligomers, which participate in different signaling pathways and have distinct functions compared with monomers. APJ homodimers can serve as neuroprotectors against, and provide new pharmaceutical targets for vascular dementia (VD). This review article aims to summarize the structural characteristics of APJ dimers and their roles in physiology and pathology, as well as explore their potential pharmacological applications.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Multimerización de Proteína / Receptores de Apelina Límite: Animals / Humans Idioma: En Revista: Biochim Biophys Acta Mol Basis Dis Año: 2024 Tipo del documento: Article Pais de publicación: Países Bajos
Texto completo
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Imprimir
XML
PubMed Links
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Multimerización de Proteína / Receptores de Apelina Límite: Animals / Humans Idioma: En Revista: Biochim Biophys Acta Mol Basis Dis Año: 2024 Tipo del documento: Article Pais de publicación: Países Bajos