INTRODUCTION: Parkinson’s disease (PD) is characterized by the presence in the brain of inclusions formed from misfolded α‑synuclein. It has been suggested that formation of these inclusions is inhibited by chaperones such as Hsp90 and its co-chaperones. AIM(S): In this work we analyzed the localization and level of Hsp90 co-chaperone, SGT1, in the brain of PD patients. METHOD(S): Studies were performed on the specimens derived from 5 control individuals and 5 patients with PD. Localization of SGT1 was determined by immunohistochemistry while the level of Sgt1 protein and mRNA by Western blot and qRT-PCR, respectively. Neuroblastoma NB2a cells and PLA were applied to estimate the interaction between α‑synuclein and SGT1. RESULTS: We have determined the localization of SGT1 in different brain regions. We also found that the level of SGT1 is upregulated in cortex and downregulated in putamen of patients with PD. We have demonstrated that SGT1 transiently interacts with α‑synuclein in NB2a cells. CONCLUSIONS: Our results suggest that a Hsp90 co-chaperone, SGT1, is involved in the pathogenesis of PD. FINANCIAL SUPPORT: This work has been supported by the EU Horizon 2020, Marie Sklodowska-Curie grant No 665735 and by the Polish Ministry of Science and Higher Education grant No 3548/H2020/COFUND/2016/2.
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