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AMP-activated protein kinase regulation and action in skeletal muscle during exercise.
Musi, N; Yu, H; Goodyear, L J.
Afiliación
  • Musi N; Research Division, Joslin Diabetes Center and Department of Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02215, USA.
Biochem Soc Trans ; 31(Pt 1): 191-5, 2003 Feb.
Article en En | MEDLINE | ID: mdl-12546683
Physical exercise increases muscle glucose uptake, enhances insulin sensitivity and leads to fatty acid oxidation in muscle. The AMP-activated protein kinase (AMPK) is an energy-sensing enzyme that is strongly activated during muscle contraction due to acute decreases in ATP/AMP and phosphocreatine/creatine ratios. Accumulating evidence suggests that AMPK plays an important role in mediating these metabolic processes. Furthermore, AMPK has been implicated in regulating gene transcription and therefore may play a role in some of the cellular adaptations to training exercise. There is also evidence that changes in AMPK activity result in altered cellular glycogen content, suggesting that this enzyme regulates glycogen metabolism. Recent studies have shown that the magnitude of AMPK activation and associated metabolic responses are affected by factors such as glycogen content, exercise training and fibre type. In summary, AMPK regulates several metabolic pathways during acute exercise and modifies the expression of many genes involved in the adaptive changes to exercise training.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ejercicio Físico / Proteínas Serina-Treonina Quinasas / Músculo Esquelético / Complejos Multienzimáticos Límite: Animals / Humans Idioma: En Revista: Biochem Soc Trans Año: 2003 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ejercicio Físico / Proteínas Serina-Treonina Quinasas / Músculo Esquelético / Complejos Multienzimáticos Límite: Animals / Humans Idioma: En Revista: Biochem Soc Trans Año: 2003 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Reino Unido