TY - JOUR
T1 - The peptidyl-prolyl isomerase pin1 up-regulation and proapoptotic function in dopaminergic neurons
T2 - Relevance to the pathogenesis of parkinson disease
AU - Ghosh, Anamitra
AU - Saminathan, Hariharan
AU - Kanthasamy, Arthi
AU - Anantharam, Vellareddy
AU - Jin, Huajun
AU - Sondarva, Gautam
AU - Harischandra, Dilshan S.
AU - Qian, Ziqing
AU - Rana, Ajay
AU - Kanthasamy, Anumantha G.
PY - 2013/7/26
Y1 - 2013/7/26
N2 - Background: Pin1 regulates several signaling proteins by isomerizing the cis/trans conformation of the Ser(P)-Pro peptide bond. Results: Pin1 is up-regulated in dopaminergic neurons in cell culture, animal models, and human PD brains. Pin1 inhibition protects dopaminergic neurons in PD models. Conclusion: Pin1 up-regulation plays a proapoptotic function in PD. Significance: Pin1 inhibition may be a viable translational strategy in PD.
AB - Background: Pin1 regulates several signaling proteins by isomerizing the cis/trans conformation of the Ser(P)-Pro peptide bond. Results: Pin1 is up-regulated in dopaminergic neurons in cell culture, animal models, and human PD brains. Pin1 inhibition protects dopaminergic neurons in PD models. Conclusion: Pin1 up-regulation plays a proapoptotic function in PD. Significance: Pin1 inhibition may be a viable translational strategy in PD.
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U2 - 10.1074/jbc.M112.444224
DO - 10.1074/jbc.M112.444224
M3 - Article
C2 - 23754278
AN - SCOPUS:84881224985
SN - 0021-9258
VL - 288
SP - 21955
EP - 21971
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 30
ER -