Publication:
Melatonin inhibits amphetamine-induced increase in α-synuclein and decrease in phosphorylated tyrosine hydroxylase in SK-N-SH cells

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Issued Date

2008

Resource Type

Article

File Type

application/pdf

ISSN

3043940

DOI

10.1016/j.neulet.2008.03.053

Other identifier(s)

2-s2.0-43049165779

Rights Holder(s)

มหาวิทยาลัยศรีนครินทรวิโรฒ

Bibliographic Citation

Neuroscience Letters. Vol 436, No.3 (2008), p.309-313

Suggested Citation

Klongpanichapak S., Phansuwan-Pujito P., Ebadi M., Govitrapong P. Melatonin inhibits amphetamine-induced increase in α-synuclein and decrease in phosphorylated tyrosine hydroxylase in SK-N-SH cells. Neuroscience Letters. Vol 436, No.3 (2008), p.309-313. doi:10.1016/j.neulet.2008.03.053 Retrieved from: https://hdl.handle.net/20.500.14740/4028

Title

Melatonin inhibits amphetamine-induced increase in α-synuclein and decrease in phosphorylated tyrosine hydroxylase in SK-N-SH cells

Author(s)

Klongpanichapak S.
 Phansuwan-Pujito P.
 Ebadi M.
 Govitrapong P.

Abstract

α-Synuclein is an abundant presynaptic protein implicated in neuronal plasticity and neurodegeneration disorders. Understanding α-synuclein function in dopaminergic cells could add to our knowledge of this key protein which is implicated in Parkinson's disease. Chronic or intermittent amphetamine (AMPH) abuse may create temporary or permanent disturbances in the dopaminergic system of the brain that may predispose individuals to Parkinsonism. Our previous studies showed that neurotoxicity induced by AMPH was mediated by enhanced oxidative stress and these effects were abolished by melatonin, a main secretory product of pineal gland. The present study was conducted to investigate the effect of AMPH on α-synuclein in regulating tyrosine hydroxylase (TH), a rate limiting enzyme for dopamine synthesis, in cultured human dopaminergic SK-N-SH cells. Of these, phosphorylation of Ser40 (pSer40) contributes significantly to TH activation and dopamine synthesis. Our data indicated that AMPH significantly increased the level of α-synuclein to 183% of the control value while reducing the levels of phosphorylated TH (TH-pSer40) enzyme and mitochondrial complex I to 78 and 52.9% of the control values, respectively and these effects were attenuated by melatonin. Further studies are needed to explore the mechanism by which α-synuclein contributes to TH-pSer40 dephosphorylation and the mechanism by which melatonin contributes to this interaction. © 2008 Elsevier Ireland Ltd. All rights reserved.

Subject(s)

Alpha synuclein
 Amphetamine
 Melatonin
 Reduced nicotinamide adenine dinucleotide dehydrogenase (ubiquinone)
 Tyrosine 3 monooxygenase
 Article
 Cell culture
 Controlled study
 Dopamine metabolism
 Drug effect
 Human
 Human cell
 Immunofluorescence
 Mitochondrial respiration
 Neuroblastoma cell
 Neurotoxicity
 Oxidative stress
 Priority journal
 Protein expression
 Protein phosphorylation
 Western blotting
 Alpha-Synuclein
 Amphetamine
 Antioxidants
 Cell Line, Tumor
 Central Nervous System Stimulants
 Dose-Response Relationship, Drug
 Drug Interactions
 Electron Transport Complex I
 Gene Expression Regulation, Neoplastic
 Humans
 Melatonin
 Neuroblastoma
 Phosphorylation
 Serine
 Tyrosine 3-Monooxygenase

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URI

https://hdl.handle.net/20.500.14740/4028

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Scopus: Year 1983-2021

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