Publication: Calpastatin reduces calpain and caspase activation in methamphetamine-induced toxicity in human neuroblastoma SH-SY5Y cultured cells
Issued Date
2012-09-20
Resource Type
ISSN
18727972
03043940
03043940
Other identifier(s)
2-s2.0-84865627845
Rights
Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Neuroscience Letters. Vol.526, No.1 (2012), 49-53
Suggested Citation
Wilasinee Suwanjang, Pansiri Phansuwan-Pujito, Piyarat Govitrapong, Banthit Chetsawang Calpastatin reduces calpain and caspase activation in methamphetamine-induced toxicity in human neuroblastoma SH-SY5Y cultured cells. Neuroscience Letters. Vol.526, No.1 (2012), 49-53. doi:10.1016/j.neulet.2012.07.066 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/15126
Research Projects
Organizational Units
Authors
Journal Issue
Thesis
Title
Calpastatin reduces calpain and caspase activation in methamphetamine-induced toxicity in human neuroblastoma SH-SY5Y cultured cells
Other Contributor(s)
Abstract
Methamphetamine (METH) is an abused psychostimulant drug that can cause neurotoxicity to dopaminergic cells. It has been demonstrated that METH can induce caspase- and calpain-dependent death cascades. The purpose of the present study was to investigate the functional role of calpastatin, a specific endogenous calpain inhibitor protein, on caspase and calpain activation in METH-induced degeneration in neuroblastoma SH-SY5Y cell cultures. In this study, we found that METH significantly decreased cell viability, tyrosine hydroxylase phosphorylation and calpastatin levels. Supplementation of cells with exogenous calpastatin was able to reverse the toxic effect of METH on reduction in cell viability and tyrosine hydroxylase phosphorylation. METH also significantly increased calpain levels, the formation of calpain-specific breakdown products and cleaved caspase-3 levels; once again, these effects were diminished by pretreating the cells with calpastatin. These data suggest the contribution of calpastatin as a potential regulatory factor for calpain- and caspase-dependent death processes. © 2012 Elsevier Ireland Ltd.