title: Nutritional status modulates plasma leptin, AMPK and TOR activation, and mitochondrial biogenesis: Implications for cell metabolism and growth in skeletal muscle of the fine flounder.
abstract: Insight of how growth and metabolism in skeletal muscle are related is still lacking in early vertebrates. In this context, molecules involved in these processes, such as leptin, AMP-activated protein kinase (AMPK), target of rapamicyn (TOR), peroxisome proliferator-activated receptor γ coactivator 1α (PGC-1α, and oxidative phosphorylation complexes (OXPHOS), were assessed in the skeletal muscle of a fish species. Periods of fasting followed by a period of refeeding were implemented, using the fine flounder as a model (Paralichthys adspersus). This species exhibits remarkably slow growth and food intake, which is linked to an inherent growth hormone (GH) resistance and high circulating levels of leptin. Leptin increased during fasting concomitantly with AMPK activation, which was inversely correlated with TOR activation. On the other hand, AMPK was directly correlated with an increase in PGC-1α and OXPHOS complexes contents. Dramatic changes in the activation and content of these molecules were observed during short-term refeeding. Leptin, AMPK activation, and PGC-1α/OXPHOS complexes contents decreased radically; whereas, TOR activation increased significantly. During long-term refeeding these molecules returned to basal levels. These results suggest that there is a relation among these components; thus, during fasting periods ATP-consuming biosynthetic pathways are repressed and alternative sources of ATP/energy are promoted, a phenomenon that is reversed during anabolic periods. These results provide novel insight on the control of metabolism and growth in the skeletal muscle of a non-mammalian species, suggesting that both processes in fish muscle are closely related and coordinated by a subset of common molecules.
authors.affiliation: Universidad Andres Bello, Departmento de Ciencias Biologicas, Facultad de Ciencias Biologicas, Av. Republica 217, Santiago, Chile. edua.fuentes@uandresbello.edu
authors.forename: Eduardo N
authors.initials: EN
authors.lastname: Fuentes
authors.forename: Diego
authors.initials: D
authors.lastname: Safian
authors.forename: Ingibjörg Eir
authors.initials: IE
authors.lastname: Einarsdottir
authors.forename: Juan Antonio
authors.initials: JA
authors.lastname: Valdés
authors.forename: Alvaro A
authors.initials: AA
authors.lastname: Elorza
authors.forename: Alfredo
authors.initials: A
authors.lastname: Molina
authors.forename: Björn Thrandur
authors.initials: BT
authors.lastname: Björnsson
mesh_terms: D055372:AMP-Activated Protein Kinases / Q000097:blood*; D000818:Animals; D005432:Flounder / Q000097:blood / Q000378:metabolism; D020738:Leptin / Q000097:blood*; D063269:Mitochondrial Turnover / Q000502:physiology*; D018482:Muscle, Skeletal / Q000378:metabolism*; D009752:Nutritional Status / Q000502:physiology*; D047495:PPAR gamma; D015398:Signal Transduction
chemical_list: D020738:Leptin; D047495:PPAR gamma; D055372:AMP-Activated Protein Kinases