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• W2124731208 abstract "Abstract Dimerization of G protein‐coupled receptors ( GPCR s) is crucial for receptor function including agonist affinity, efficacy, trafficking and specificity of signal transduction, including G protein coupling. Emerging data suggest that the cardiovascular system is the main target of apelin, which exerts an overall neuroprotective role, and is a positive regulator of angiotensin‐converting enzyme 2 ( ACE 2) in heart failure. Moreover, ACE 2 cleaves off C‐terminal residues of vasoactive peptides including apelin‐13, and neurotensin that activate the apelin receptor ( APJ ) and neurotensin receptor 1 ( NTSR 1) respectively, that belong to the A class of GPCR s. Therefore, based on the similar mode of modification by ACE 2 at peptide level, the homology at amino acid level and the capability of forming dimers with other GPCR s, we have been suggested that APJ and NTSR 1 can form a functional heterodimer. Using co‐immunoprecipitation, BRET and FRET , we provided conclusive evidence of heterodimerization between APJ and NTSR 1 in a constitutive and induced form. Upon agonist stimulation, hetrodimerization enhanced ERK 1/2 activation and increased proliferation via activation of Gq α‐subunits. These novel data provide evidence for a physiological role of APJ / NTSR 1 heterodimers in terms of ERK 1/2 activation and increased intracellular calcium and induced cell proliferation and provide potential new pharmaceutical targets for cardiovascular disease." @default.
• W2124731208 created "2016-06-24" @default.
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• W2124731208 date "2014-08-28" @default.
• W2124731208 modified "2023-10-03" @default.
• W2124731208 title "Heterodimerization of apelin receptor and neurotensin receptor 1 induces phosphorylation of ERK _1/2 and cell proliferation <i>via</i> Gαq‐mediated mechanism" @default.
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• W2124731208 doi "https://doi.org/10.1111/jcmm.12404" @default.
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