Calpain mediates cardiac troponin I degradation in tail-suspended rats.
- Author:
Peng-Tao XU
1
;
Zhen SONG
;
Quan LI
;
Lin ZHANG
;
Yun-Ying WANG
;
Zhi-Bin YU
Author Information
1. Department of Aerospace Physiology, the Fourth Military Medical University, Xi'an 710032, China.
- Publication Type:Journal Article
- MeSH:
Animals;
Calcium-Binding Proteins;
metabolism;
Calpain;
metabolism;
Hindlimb Suspension;
Myocardium;
metabolism;
Proteolysis;
Rats;
Troponin I;
metabolism;
Weightlessness Simulation
- From:
Acta Physiologica Sinica
2010;62(5):415-420
- CountryChina
- Language:Chinese
-
Abstract:
The aim of the present study was to investigate the expressions of calpain and calpastatin in the myocardium of simulated weightlessness rats, and to elucidate the underlying mechanism of cardiac troponin I (cTnI) degradations. Tail-suspended (SUS) rats were used as a simulated weightlessness model on the ground. The myocardium of rats was homogenized, and the expressions of calpain-1, calpain-2, calpastatin and cTnI were analyzed by Western blotting technique. Calpastatin expression was significantly decreased in 2- and 4-week SUS groups compared with that in the synchronous controls (P<0.05). Calpain-2 expression was slightly decreased, whereas calpain-1 expression was unaltered in SUS groups. However, calpain-1/calpastatin and calpain-2/calpastatin ratios were increased after tail-suspension, being significantly higher in 2- and 4-week SUS groups than those in the synchronous controls (P<0.05, P<0.01). Cardiac TnI degradation was significantly increased after tail-suspension (P<0.01), but cTnI degradation in both SUS and control groups was significantly inhibited by a non-specific inhibitor of calpain, PD150606 (P<0.01). These results suggest that an increase in calpain activity may enhance cTnI degradation in the myocardium of tail-suspended rats.
