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A2A-D2 Heteromers on Striatal Astrocytes: Biochemical and Biophysical Evidence

1
Department of Pharmacy, Section of Pharmacology and Toxicology, University of Genova, Viale Cembrano 4, 16148 Genova, Italy
2
Department of Neuroscience, University of Padova, Via Gabelli 63, 35122 Padova, Italy
3
Department of Experimental Medicine, Section of Biochemistry, University of Genova, Viale Benedetto XV, 1, 16132 Genova, Italy
4
Division of Experimental Oncology, San Raffaele Scientific Institute, Via Olgettina 60, 20132 Milano, Italy
5
Department of Biomedical and NeuroMotor Sciences (DIBINEM) Alma Mater Studiorum-University of Bologna, Via Altura 3, 40139 Bologna, Italy
6
IRCCS Istituto delle Scienze Neurologiche di Bologna, Via Altura 3, 40139 Bologna, Italy
7
Department of Diagnostic, Clinical Medicine and Public Health, University of Modena and Reggio Emilia, Via Campi 287, 41125 Modena, Italy
8
Department of Neuroscience, Karolinska Institutet, Retzius väg 8, 171 65 Stockholm, Sweden
9
Centre of Excellence for Biomedical Research CEBR, University of Genova, Viale Benedetto XV, 5, 16132 Genova, Italy
*
Author to whom correspondence should be addressed.
Present address: Telethon Institute of Genetics and Medicine (TIGEM) Via Campi Flegrei 34, 80078 Pozzuoli (NA), Italy.
Present address: Department of surgical, medical, dental and morphological sciences-University of Modena and Reggio Emilia, Largo del Pozzo 71, 41125 Modena, Italy.
Int. J. Mol. Sci. 2019, 20(10), 2457; https://doi.org/10.3390/ijms20102457
Received: 15 April 2019 / Revised: 14 May 2019 / Accepted: 16 May 2019 / Published: 17 May 2019
(This article belongs to the Special Issue G Protein-Coupled Adenosine Receptors: Molecular Aspects and Beyond)
PDF [2281 KB, uploaded 17 May 2019]

Abstract

Our previous findings indicate that A2A and D2 receptors are co-expressed on adult rat striatal astrocytes and on the astrocyte processes, and that A2A-D2 receptor–receptor interaction can control the release of glutamate from the processes. Functional evidence suggests that the receptor–receptor interaction was based on heteromerization of native A2A and D2 receptors at the plasma membrane of striatal astrocyte processes. We here provide biochemical and biophysical evidence confirming that receptor–receptor interaction between A2A and D2 receptors at the astrocyte plasma membrane is based on A2A-D2 heteromerization. To our knowledge, this is the first direct demonstration of the ability of native A2A and D2 receptors to heteromerize on glial cells. As striatal astrocytes are recognized to be involved in Parkinson’s pathophysiology, the findings that adenosine A2A and dopamine D2 receptors can form A2A-D2 heteromers on the astrocytes in the striatum (and that these heteromers can play roles in the control of the striatal glutamatergic transmission) may shed light on the molecular mechanisms involved in the pathogenesis of the disease.
Keywords: A2A-D2 heteromers; co-immunoprecipitation; proximity ligation assay; rat striatum; striatal astrocyte processes; striatal slices A2A-D2 heteromers; co-immunoprecipitation; proximity ligation assay; rat striatum; striatal astrocyte processes; striatal slices
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
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Pelassa, S.; Guidolin, D.; Venturini, A.; Averna, M.; Frumento, G.; Campanini, L.; Bernardi, R.; Cortelli, P.; Calandra Buonaura, G.; Maura, G.; Agnati, L.F.; Cervetto, C.; Marcoli, M. A2A-D2 Heteromers on Striatal Astrocytes: Biochemical and Biophysical Evidence. Int. J. Mol. Sci. 2019, 20, 2457.

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