Effects of beta-adrenoceptor activation on metabolism in neonatal rat cardiomyocytes.
- Author:
Jie YAN
1
;
Kai CHEN
;
Ming XU
;
Zhi-Zhen LU
;
Qi-De HAN
;
You-Yi ZHANG
Author Information
1. Institute of Vascular medicine, peking university third hospital and Key Laboratory of Molecular Cardiology, Education Ministry, Beijing 100083, China.
- Publication Type:Journal Article
- MeSH:
AMP-Activated Protein Kinases;
Animals;
Animals, Newborn;
Cells, Cultured;
Glucose;
metabolism;
Multienzyme Complexes;
metabolism;
Muscle Proteins;
biosynthesis;
Myocytes, Cardiac;
cytology;
metabolism;
Protein-Serine-Threonine Kinases;
metabolism;
Rats;
Rats, Sprague-Dawley;
Receptors, Adrenergic, beta
- From:
Acta Physiologica Sinica
2004;56(2):224-229
- CountryChina
- Language:Chinese
-
Abstract:
The aim of the present study was to investigate the effects of beta-adrenergic receptor (beta-AR) activation on metabolism in cultured neonatal rat cardiomyocytes. The protein synthesis and total protein content of cardiomyocytes were determined by [(3)H]-leucine incorporation and BCA protein content assay. Cardiomyocyte glucose uptake was measured by [(3)H]-2-deoxy-D-glucose uptake analysis. Adenosine monophosphate activated protein kinase (AMPK) phosphorylation was detected by Western blot. The results showed that sustained stimulation with isoproterenol (ISO), a beta-adrenoceptor agonist, had no effect on [(3)H]-leucine incorporation and total protein content in cardiomyocytes. With beta-AR activation by ISO or NE (pretreated with a selective blocker of the alpha(1)-adrenoceptor prazosin) for 48 h, both the glucose uptake and AMPK phosphorylation increased significantly compared with unstimulated cardiomyocytes. These results suggest that although sustained beta-AR activation has no effect on cardiomyocyte protein metabolism, glucose uptake and AMPK activity are increased significantly. The role of these beta-AR activation-induced changes in cardiac hypertrophy remains to be further investigated.
