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Ghrelin through GHSR1a and OX1R heterodimers reveals a Gαs–cAMP-cAMP response element binding protein signaling pathway in vitro

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Xue, Qingjie, Bai, Bo, Ji, Bingyuan, Chen, Xiaoyu, Wang, Chunmei, Wang, Peixiang, Yang, Chunqing, Zhang, Rumin, Jiang, Yunlu, Pan, Yanyou, Cheng, Baohua and Chen, Jing (2018) Ghrelin through GHSR1a and OX1R heterodimers reveals a Gαs–cAMP-cAMP response element binding protein signaling pathway in vitro. Frontiers in Molecular Neuroscience, 11 . 245. doi:10.3389/fnmol.2018.00245

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Official URL: http://dx.doi.org/10.3389/fnmol.2018.00245

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Abstract

Growth hormone secretagogue receptor 1α (GHSR1a) and Orexin 1 receptor (OX1R) are involved in various important physiological processes, and have many similar characteristics in function and distribution in peripheral tissues and the central nervous system. We explored the possibility of heterodimerization between GHSR1a and OX1R and revealed a signal transduction pathway mechanism. In this study, bioluminescence and fluorescence resonance energy transfer and co-immunoprecipitation (Co-IP) analyses were performed to demonstrate the formation of functional GHSR1a/OX1R heterodimers. This showed that a peptide corresponding to the 5-transmembrane domain of OX1R impaired heterodimer construction. We found that ghrelin stimulated GHSR1a/OX1R heterodimer cells to increase the activation of Gαs protein, compared to the cells that express GHSR1a. Stimulation of GHSR1a/OX1R heterodimers with orexin-A did not alter GPCR interactions with Gα protein subunits. GHSR1a/OX1R heterodimers induced Gαs and downstream signaling pathway activity, including increase of cAMP-response element luciferase reporter activity and cAMP levels. In addition, ghrelin induced a higher proliferation rate in SH-SY5Y cells than in controls. This suggests that ghrelin GHSR1a/OX1R heterodimers promotes an upregulation of a Gαs-cAMP-cAMP-responsive element signaling pathway in vitro and an increase in neuroblastoma cell proliferation.

Item Type: Journal Article
Subjects: Q Science > QP Physiology
Divisions: Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School > Biomedical Sciences
Faculty of Science, Engineering and Medicine > Medicine > Warwick Medical School
Library of Congress Subject Headings (LCSH): Growth -- Physiological aspects, Peptides, Orexins, Allosteric proteins, Neuroblastoma
Journal or Publication Title: Frontiers in Molecular Neuroscience
Publisher: Frontiers Research Foundation
ISSN: 1662-5099
Official Date: 2018
Dates:
DateEvent
2018Published
17 June 2018Available
25 June 2018Accepted
Volume: 11
Article Number: 245
DOI: 10.3389/fnmol.2018.00245
Status: Peer Reviewed
Publication Status: Published
Access rights to Published version: Open Access
RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
31271243 [NSFC] National Natural Science Foundation of Chinahttp://dx.doi.org/10.13039/501100001809
81070961[NSFC] National Natural Science Foundation of Chinahttp://dx.doi.org/10.13039/501100001809
31600949[NSFC] National Natural Science Foundation of Chinahttp://dx.doi.org/10.13039/501100001809
ZR2012HM037Natural Science Foundation of Shandong Provincehttp://dx.doi.org/10.13039/501100007129
ZR2015CL031Natural Science Foundation of Shandong Provincehttp://dx.doi.org/10.13039/501100007129
ZR2015CL021Natural Science Foundation of Shandong Provincehttp://dx.doi.org/10.13039/501100007129
ZR2018MC005Natural Science Foundation of Shandong Provincehttp://dx.doi.org/10.13039/501100007129
J12LK56Department of Science and Technology of Shandong Provincehttp://dx.doi.org/10.13039/100012905
J16LE01Department of Science and Technology of Shandong Provincehttp://dx.doi.org/10.13039/100012905
Young Teachers ProgramShandong University of Science and Technologyhttp://dx.doi.org/10.13039/501100004295

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