Effects of aconitine on connexin43 phosphorylation status in the cultured neonatal ventricular myocytes of rat
- VernacularTitle:乌头碱对培养新生大鼠心室肌细胞Connexin43蛋白磷酸化的影响
- Author:
Shiwei ZHANG
;
Jielin REN
;
Li ZHANG
- Publication Type:Journal Article
- Keywords:
Forensic toxicology;
Cell culture;
Aconitine;
Connexin43;
Protein phosphorylation
- From:
Chinese Journal of Forensic Medicine
1986;0(02):-
- CountryChina
- Language:Chinese
-
Abstract:
Objective To set up an experiment model on cellular level in order to investigate the effects of aconitine on Connexin43(Cx43)in cardiomyocytes of rat.Methods The cultured cardiomyocytes of rat were incubated with aconitine at 6 different concentrations of 0.25,0.5,0.75,1.0,1.5 and 2.0 ?mol/L.The changes of Cx43 phosphorylation status of each group were investigated by Western blot analysis and immunofluorescent microscopy techniques.Results The total amount of Cx43 had not changed in cardiomyocytes after aconitine incubation by western blot analysis,but it began to induce Cx43 dephosphorylation after incubation of the cultures with 0.5 ?mol/L aconitine and Cx43 underwent significant dephosphorylation when the concentration of aconitine elevated to 1.0 ?mol/L,and the dephosphorylation effects of 1.5 and 2.0 ?mol/L aconitine on Cx43 were similar to that of 1.0 ?mol/L aconitine.Quantitative immunofluorescent microscopy revealed that Ser368,one of the serine amino acid phosphorylation sites in the C-terminal domain of Cx43,underwent significant dephosphorylation when incubation of the cardiomyocytes with 1.0 ?mol/L aconitine.Conclusion Under certain concentration conditions,aconitine can induce significant dephosphorylation of Cx43 in the cardiomyocytes of rat.
