Fernández Dueñas, VíctorTaura, JaumeCottet, MartinGómez Soler, MaricelLópez-Cano, MarcLedent, CatherineWatanabe, MasahikoTrinquet, EricPin, Jean-PhilippeLuján, RafaelDurroux, ThierryCiruela Alférez, Francisco2018-10-292018-10-292015-01-011754-8403https://hdl.handle.net/2445/125691Parkinson's disease (PD) is a dopaminergic-related pathology in which functioning of the basal ganglia is altered. It has been postulated that a direct receptor-receptor interaction - i.e. of dopamine D-2 receptor (D2R) with adenosine A(2A) receptor (A(2A)R) (forming D2R-A(2A)R oligomers) - finely regulates this brain area. Accordingly, elucidating whether the pathology prompts changes to these complexes could provide valuable information for the design of new PD therapies. Here, we first resolved a long-standing question concerning whether D2R-A(2A)R assembly occurs in native tissue: by means of different complementary experimental approaches (i.e. immunoelectron microscopy, proximity ligation assay and TR-FRET), we unambiguously identified native D2R-A(2A)R oligomers in rat striatum. Subsequently, we determined that, under pathological conditions (i.e. in a rat PD model), D2R-A(2A)R interaction was impaired. Collectively, these results provide definitive evidence for alteration of native D2R-A(2A)R oligomers in experimental parkinsonism, thus conferring the rationale for appropriate oligomer-based PD treatments.7 p.application/pdfengcc-by (c) Fernández Dueñas, Víctor et al., 2015http://creativecommons.org/licenses/by/3.0/esMalaltia de ParkinsonAdenosinaDopaminaParkinson's diseaseAdenosineDopamineinfo:eu-repo/semantics/article6446462018-10-29info:eu-repo/semantics/openAccess25398851