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Ankyrin repeat and BTB/POZ domain containing protein-2 inhibits the aggregation of alpha-synuclein: Implications for Parkinson's disease.
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FEBS Lett 2013 Sep;
Authors: Avik Roy, Kalipada Pahan
Department of Neurological Sciences, Rush University Medical Center, Chicago, IL 60612, USA. Electronic address: firstname.lastname@example.org.
Aggregation of ?-synuclein is a pathological hallmark of sporadic or familial PD. However, the detailed molecular mechanism responsible for the aggregation of ?-synuclein has not been properly explored. In the present study, we have identified a novel role of an anti-tumorigenic BTB/POZ domain containing protein-2 (BPOZ-2) in the regulation of ?-synuclein accumulation in dopaminergic (DA) neurons. MPP(+), an etiological factor for PD, significantly downregulated the expression of BPOZ-2 ahead of ?-synuclein upregulation. Moreover, siRNA knockdown of BPOZ-2 alone stimulated the aggregation of ?-synuclein protein; the effect was further induced in presence of MPP(+) in mouse primary DA neurons. Finally, the absence of BPOZ-2 in ?-synuclein expressing neuronal populations of MPTP-intoxicated mouse and primate nigra indicates that the suppression of BPOZ-2 could be involved in the accumulation of ?-synuclein protein.
PMID: 24076025 [PubMed - as supplied by publisher]