Effects of testosterone on extracellular signal-regulated kinase 1/2 phosphorylation in human umbilical vein endothelial cells.
- Author:
Hong JIN
1
;
Xiao-ying ZHANG
;
Geng PENG
;
Wen-bing QIU
;
Dong-ming WANG
;
Yu-guang LI
Author Information
- Publication Type:Journal Article
- MeSH: Androgen Receptor Antagonists; Blotting, Western; Cells, Cultured; Endothelial Cells; cytology; drug effects; metabolism; Enzyme Activation; drug effects; Extracellular Signal-Regulated MAP Kinases; metabolism; Humans; Mitogen-Activated Protein Kinase 1; metabolism; Mitogen-Activated Protein Kinase 3; metabolism; Phosphorylation; drug effects; Receptors, Androgen; metabolism; Testosterone; pharmacology; Umbilical Veins; cytology
- From: National Journal of Andrology 2007;13(9):777-779
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo investigate the effects of testosterone on extracellular signal-regulated kinase l/2 ( ERK1/2) phosphorylation in human umbilical vein endothelial cells (HUVEC).
METHODSActivations of ERK1/2 stimulated by physiological testosterone were detected by Western blotting in cultured HUVEC.
RESULTSA rapid phosphorylation expression of ERK1/2 was observed by treatment of the HUVECs with 3 x 10(-8) mol/L testosterone, especially at 30 minutes. This phosphorylation was greatly inhibited by incubation with androgen receptor antagonist flutamide for 3 hours previously.
CONCLUSIONTestosterone at physiological concentrations induces the mitogen-activated protein kinase (MAPK, ERK1/2 and MEK1/2) phosphorylation within a short time, and flutamide could impair the process.
