Leptin stimulates protein synthesis-activating translation machinery in human trophoblastic cells

Autor: Pérez-Pérez, A., Julieta Maymo, Y., Gambino, É., Dueñas, J.L., Goberna, R., Varone, C., Sánchez-Margalet, V.
Jazyk: angličtina
Rok vydání: 2009
Předmět:
Leptin
protein synthesis
Placenta
protein binding
androstane derivative
Western blotting
Pregnancy
dose response
cell growth
1-Phosphatidylinositol 3-Kinase
phosphatidylinositol 3 kinase
Phosphorylation
Cells
Cultured

mitogen activated protein kinase
protein kinase inhibitor
drug effect
Trophoblast
article
cell line
2 (2 amino 3 methoxyphenyl)chromone
phosphoprotein
Leptin receptor
Trophoblasts
wortmannin
female
priority journal
Mitogen-Activated Protein Kinases
signal transduction
hormone action
analysis of variance
Blotting
Western

signal transducing adaptor protein
translation initiation
Humans
flavonoid
controlled study
human
Protein Kinase Inhibitors
Adaptor Proteins
Signal Transducing

Mechanisms of hormone action
Flavonoids
cell culture
Dose-Response Relationship
Drug

human cell
Phosphoproteins
protein phosphorylation
Androstadienes
Eukaryotic Initiation Factor-4E
Protein Biosynthesis
initiation factor 4E
physiology
metabolism
EIF4EBP1 protein
human
Zdroj: Biol. Reprod. 2009;81(5):826-832
Biblioteca Digital (UBA-FCEN)
Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales
instacron:UBA-FCEN
Popis: Leptin was originally considered as an adipocyte-derived signaling molecule for the central control of metabolism. However, pleiotropic effects of leptin have been identified in reproduction and pregnancy, particularly in placenta, where it may work as an autocrine hormone, mediating angiogenesis, growth, and immunomodulation. Leptin receptor (LEPR, also known as Ob-R) shows sequence homology to members of the class I cytokine receptor (gp130) superfamily. In fact, leptin may function as a proinflammatory cytokine. We have previously found that leptin is a trophic and mitogenic factor for trophoblastic cells. In order to further investigate the mechanism by which leptin stimulates cell growth in JEG-3 cells and trophoblastic cells, we studied the phosphorylation state of different proteins of the initiation stage of translation and the total protein synthesis by [3H]leucine incorporation in JEG-3 cells. We have found that leptin dose-dependently stimulates the phosphorylation and activation of the translation initiation factor EIF4E as well as the phosphorylation of the EIF4E binding protein EIF4EBP1 (PHAS-I), which releases EIF4E to form active complexes. Moreover, leptin dose-dependently stimulates protein synthesis, and this effect can be partially prevented by blocking mitogen-activated protein kinase (MAPK) and phosphatidylinositol 3 kinase (PIK3) pathways. In conclusion, leptin stimulates protein synthesis, at least in part activating the translation machinery, via the activation of MAPK and PIK3 pathways. © 2009 by the Society for the Study of Reproduction, Inc. Fil:Julieta Maymo, Y. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Gambino, É. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Varone, C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Databáze: OpenAIRE