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Arsenic impairs insulin signaling in differentiated neuroblastoma SH-SY5Y cells.
Niyomchan, Apichaya; Visitnonthachai, Daranee; Suntararuks, Sumitra; Ngamsiri, Pronrumpa; Watcharasit, Piyajit; Satayavivad, Jutamaad.
Afiliación
  • Niyomchan A; Laboratory of Pharmacology, Chulabhorn Research Institute, Thailand; Chulabhorn Graduate Institute, 54 Kamphaeng Phet 6 Rd, Bangkok, 10210, Thailand.
  • Visitnonthachai D; Laboratory of Pharmacology, Chulabhorn Research Institute, Thailand.
  • Suntararuks S; Laboratory of Pharmacology, Chulabhorn Research Institute, Thailand.
  • Ngamsiri P; Laboratory of Pharmacology, Chulabhorn Research Institute, Thailand.
  • Watcharasit P; Laboratory of Pharmacology, Chulabhorn Research Institute, Thailand; Chulabhorn Graduate Institute, 54 Kamphaeng Phet 6 Rd, Bangkok, 10210, Thailand; Center of Excellence on Environmental Health and Toxicology (EHT), Office of the Higher Education Commission, Thailand. Electronic address: Piyajit@cr
  • Satayavivad J; Laboratory of Pharmacology, Chulabhorn Research Institute, Thailand; Chulabhorn Graduate Institute, 54 Kamphaeng Phet 6 Rd, Bangkok, 10210, Thailand; Center of Excellence on Environmental Health and Toxicology (EHT), Office of the Higher Education Commission, Thailand.
Neurotoxicology ; 66: 22-31, 2018 05.
Article en En | MEDLINE | ID: mdl-29526746
A strong correlation between chronic arsenic exposure and neuropsychological disorders leads to a growing concern about a potential risk of arsenic related neurodegeneration. Evidently, brain insulin signaling contributes to physiological effects, including energy homeostasis, and learning and memory. Arsenic has been shown to impair insulin signaling in adipocytes and myocytes, however, this impairment has not yet been explored in neurons. Here we showed that NaAsO2 caused significant reduction in basal levels of glucose, plasma membrane glucose transporter, GLUT 3 and Akt phosphorylation in differentiated human neuroblastoma SH-SY5Y cells. NaAsO2 significantly decreased insulin-mediated glucose uptake, as well as GLUT1 and 3 membrane translocation. Furthermore, the ability of insulin to increase Akt phosphorylation, a well-recognized insulin signaling response, was significantly lessened by NaAsO2 treatment. In addition, the classical tyrosine phosphorylation response of insulin was reduced by NaAsO2, as evidenced by reduction of insulin-induced tyrosine phosphorylation of insulin receptor (IR) and insulin receptor substrate-1(IRS-1). Moreover, NaAsO2 lowered the ratio of p110, a catalytic subunit to p85, a regulatory subunit of PI3K causing an imbalance between p110 and p85, the conditions reported to contribute to insulin sensitivity. Additionally, increment of IRS-1 interaction with GSK3ß, and p85-PI3K were observed in NaAsO2 treated cells. These molecular modulations may be mechanistically attributed to neuronal insulin signaling impairment by arsenic.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Arsénico / Insulina Límite: Humans Idioma: En Revista: Neurotoxicology Año: 2018 Tipo del documento: Article País de afiliación: Tailandia Pais de publicación: Países Bajos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Arsénico / Insulina Límite: Humans Idioma: En Revista: Neurotoxicology Año: 2018 Tipo del documento: Article País de afiliación: Tailandia Pais de publicación: Países Bajos