Publication:
Calpastatin reduces calpain and caspase activation in methamphetamine-induced toxicity in human neuroblastoma SH-SY5Y cultured cells

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Issued Date

2012

Resource Type

Article

File Type

application/pdf

ISSN

3043940

DOI

10.1016/j.neulet.2012.07.066

Other identifier(s)

2-s2.0-84865627845

Rights Holder(s)

Scopus

Bibliographic Citation

Neuroscience Letters. Vol 526, No.1 (2012), p.49-53

Suggested Citation

Suwanjang W., Phansuwan-Pujito P., Govitrapong P., Chetsawang B. Calpastatin reduces calpain and caspase activation in methamphetamine-induced toxicity in human neuroblastoma SH-SY5Y cultured cells. Neuroscience Letters. Vol 526, No.1 (2012), p.49-53. doi:10.1016/j.neulet.2012.07.066 Retrieved from: https://hdl.handle.net/20.500.14740/6971

Title

Calpastatin reduces calpain and caspase activation in methamphetamine-induced toxicity in human neuroblastoma SH-SY5Y cultured cells

Author(s)

Suwanjang W.
 Phansuwan-Pujito P.
 Govitrapong P.
 Chetsawang B.

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.

Subject(s)

Calpain
 Calpastatin
 Caspase 3
 Methamphetamine
 Tyrosine 3 monooxygenase
 Article
 Cell culture
 Cell strain
 Cell viability
 Controlled study
 Enzyme activation
 Human
 Human cell
 Neuroblastoma
 Priority journal
 Protein blood level
 Protein degradation
 Protein phosphorylation
 Calcium-Binding Proteins
 Calpain
 Caspase 3
 Caspases
 Cell Line, Tumor
 Cell Survival
 Central Nervous System Stimulants
 Enzyme Activation
 Humans
 Methamphetamine
 Neuroblastoma
 Neuroprotective Agents
 Phosphorylation
 Tyrosine 3-Monooxygenase

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URI

https://hdl.handle.net/20.500.14740/6971

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Scopus: Year 1983-2021

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