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Fasting induces nuclear factor E2-related factor 2 and ATP-binding Cassette transporters via protein kinase A and Sirtuin-1 in mouse and human.
Kulkarni, Supriya R; Donepudi, Ajay C; Xu, Jialin; Wei, Wei; Cheng, Qiuqiong C; Driscoll, Maureen V; Johnson, Delinda A; Johnson, Jeffrey A; Li, Xiaoling; Slitt, Angela L.
Afiliación
  • Kulkarni SR; 1 Department of Biomedical and Pharmaceutical Sciences, University of Rhode Island , Kingston, Rhode Island.
Antioxid Redox Signal ; 20(1): 15-30, 2014 Jan 01.
Article en En | MEDLINE | ID: mdl-23725046
AIMS: The purpose of this study was to determine whether 3'-5'-cyclic adenosine monophosphate (cAMP)-protein kinase A (PKA) and Sirtuin-1 (SIRT1) dependent mechanisms modulate ATP-binding Cassette (ABC) transport protein expression. ABC transport proteins (ABCC2-4) are essential for chemical elimination from hepatocytes and biliary excretion. Nuclear factor-E2 related-factor 2 (NRF2) is a transcription factor that mediates ABCC induction in response to chemical inducers and liver injury. However, a role for NRF2 in the regulation of transporter expression in nonchemical models of liver perturbation is largely undescribed. RESULTS: Here we show that fasting increased NRF2 target gene expression through NRF2- and SIRT1-dependent mechanisms. In intact mouse liver, fasting induces NRF2 target gene expression by at least 1.5 to 5-fold. In mouse and human hepatocytes, treatment with 8-Bromoadenosine-cAMP, a cAMP analogue, increased NRF2 target gene expression and antioxidant response element activity, which was decreased by the PKA inhibitor, H-89. Moreover, fasting induced NRF2 target gene expression was decreased in liver and hepatocytes of SIRT1 liver-specific null mice and NRF2-null mice. Lastly, NRF2 and SIRT1 were recruited to MAREs and Antioxidant Response Elements (AREs) in the human ABCC2 promoter. INNOVATION: Oxidative stress mediated NRF2 activation is well described, yet the influence of basic metabolic processes on NRF2 activation is just emerging. CONCLUSION: The current data point toward a novel role of nutrient status in regulation of NRF2 activity and the antioxidant response, and indicates that cAMP/PKA and SIRT1 are upstream regulators for fasting-induced activation of the NRF2-ARE pathway.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Regulación de la Expresión Génica / Ayuno / Proteínas Quinasas Dependientes de AMP Cíclico / Transportadoras de Casetes de Unión a ATP / Factor 2 Relacionado con NF-E2 / Sirtuina 1 Tipo de estudio: Prognostic_studies Límite: Animals / Humans / Male Idioma: En Revista: Antioxid Redox Signal Asunto de la revista: METABOLISMO Año: 2014 Tipo del documento: Article Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Regulación de la Expresión Génica / Ayuno / Proteínas Quinasas Dependientes de AMP Cíclico / Transportadoras de Casetes de Unión a ATP / Factor 2 Relacionado con NF-E2 / Sirtuina 1 Tipo de estudio: Prognostic_studies Límite: Animals / Humans / Male Idioma: En Revista: Antioxid Redox Signal Asunto de la revista: METABOLISMO Año: 2014 Tipo del documento: Article Pais de publicación: Estados Unidos