Literature DB >> 23954626

Extracellular alpha-synuclein induces calpain-dependent overactivation of cyclin-dependent kinase 5 in vitro.

Grzegorz A Czapski1, Magdalena Gąssowska, Anna Wilkaniec, Magdalena Cieślik, Agata Adamczyk.   

Abstract

Extracellular alpha-synuclein (ASN) could be involved in the pathomechanism of Parkinson's disease (PD) via disturbances of calcium homeostasis, activation of nitric oxide synthase and oxidative/nitrosative stress. In this study we analyzed the role of cyclin-dependent kinase 5 (Cdk5) in the molecular mechanism(s) of ASN toxicity. We found that exposure of PC12 cells to ASN increases Cdk5 activity via calpain-dependent p25 formation and by enhancement of Cdk5 phosphorylation at Tyr15. Cdk5 and calpain inhibitors prevented ASN-evoked cell death. Our findings, indicating the participation of Cdk5 in ASN toxicity, provide new insight into how extracellular ASN may trigger dopaminergic cell dysfunction in PD.
Copyright © 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Alpha-synuclein; Calpain; Cyclin-dependent kinase 5; Parkinson’s disease; Phosphorylation; p35

Mesh：

Substances：

Year:  2013        PMID： 23954626     DOI： 10.1016/j.febslet.2013.07.053

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  11 in total

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10.  Potent inhibitors of toxic alpha-synuclein identified via cellular time-resolved FRET biosensors.

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Journal:  NPJ Parkinsons Dis       Date:  2021-06-28
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