Induction of the mitochondrial NDUFA4L2 protein by HIF-1α decreases oxygen consumption by inhibiting complex i activity

The fine regulation of mitochondrial function has proved to be an essential metabolic adaptation to fluctuations in oxygen availability. During hypoxia, cells activate an anaerobic switch that favors glycolysis and attenuates the mitochondrial activity. This switch involves the hypoxia-inducible tra...

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Detalles Bibliográficos
Autores: Tello, Daniel, Balsa Martínez, Eduardo, Acosta-Iborra, Bárbara, Fuertes-Yebra, Esther, Elorza, Ainara, Ordóñez, Ángel, Corral-Escariz, María, Soro, Inés, López-Bernardo, Elia, Perales-Clemente, Ester, Martínez-Ruiz, Antonio, Enríquez, José Antonio, Aragonés López, Julián, Cadenas, Susana, Landázuri, Manuel O.
Tipo de recurso: artículo
Fecha de publicación:2011
País:España
Institución:Universidad Autónoma de Madrid
Repositorio:Biblos-e Archivo. Repositorio Institucional de la UAM
Idioma:inglés
OAI Identifier:oai:repositorio.uam.es:10486/710316
Acceso en línea:http://hdl.handle.net/10486/710316
https://dx.doi.org/10.1016/j.cmet.2011.10.008
Access Level:acceso abierto
Palabra clave:Renal Cell Carcinoma
Kidney Neoplasms
Acetyl Coenzyme A Acetyltransferase
Biología y Biomedicina / Biología
Descripción
Sumario:The fine regulation of mitochondrial function has proved to be an essential metabolic adaptation to fluctuations in oxygen availability. During hypoxia, cells activate an anaerobic switch that favors glycolysis and attenuates the mitochondrial activity. This switch involves the hypoxia-inducible transcription factor-1 (HIF-1). We have identified a HIF-1 target gene, the mitochondrial NDUFA4L2 (NADH dehydrogenase [ubiquinone] 1 alpha subcomplex, 4-like 2). Our results, obtained employing NDUFA4L2-silenced cells and NDUFA4L2 knockout murine embryonic fibroblasts, indicate that hypoxia-induced NDUFA4L2 attenuates mitochondrial oxygen consumption involving inhibition of Complex I activity, which limits the intracellular ROS production under low-oxygen conditions. Thus, reducing mitochondrial Complex I activity via NDUFA4L2 appears to be an essential element in the mitochondrial reprogramming induced by HIF-1