Growth and differentiation factor 11 (GDF11): Functions in the regulation of erythropoiesis and cardiac regeneration.
Fiche publication
Date publication
décembre 2015
Journal
Pharmacology & therapeutics
Auteurs
Membres identifiés du Cancéropôle Est :
Pr COTTIN Yves, Pr VERGELY Catherine
Tous les auteurs :
Rochette L, Zeller M, Cottin Y, Vergely C
Lien Pubmed
Résumé
Members of the TGF-β superfamily transduce their signals through type I and II receptor serine/threonine kinases. The regulation of members of the TGF-β family is known to be complex, because many proteins able to bind the ligands and inhibit their activities have been identified. Growth and differentiation factor 11 (Gdf11) as activins belong to the TGF-β family. GDF11, like other members of the TGF-β superfamily, is produced from precursor proteins by proteolytic processing. The binding of activins to activin type IIA (ActRIIA) or type IIB (ActRIIB) receptors induces the recruitment and phosphorylation of an activin type I receptor which then phosphorylates the Smad2 and Smad3 intracellular signaling proteins. GDF11 signal through the ActRIIB pathway. Recent studies have reported that GDF11-ActRIIB-Smad2/3-dependent signaling is a key regulatory mechanism in proliferating erythroid precursors as it controls their late-stage maturation. The administration of GDF11 is effective in experimental cardiac hypertrophy, and the identification of GDF11 as a "rejuvenating factor" opens up perspectives for the treatment of age-related cardiac dysfunction. Recent studies of the heart indicate that exposure to young blood reverses age-related impairments. GDF11 could be one of the circulating molecules that influence the aging of different tissues. Is GDF11 an "elixir of youth"?
Mots clés
Activin Receptors, Type I, metabolism, Activins, metabolism, Bone Morphogenetic Proteins, metabolism, Erythropoiesis, physiology, Growth Differentiation Factors, metabolism, Heart, physiology, Humans, Phosphorylation, physiology, Protein-Serine-Threonine Kinases, physiology, Regeneration, physiology, Signal Transduction, Smad2 Protein, metabolism
Référence
Pharmacol. Ther.. 2015 Dec;156:26-33