Apoptosis in response to heat stress is positively associated with heat-shock protein 90 expression in chicken myocardial cells in vitro.
10.4142/jvs.2017.18.2.129
- Author:
Xiao Hui ZHANG
1
;
Hong WU
;
Shu TANG
;
Qiao Ning LI
;
Jiao XU
;
Miao ZHANG
;
Ya Nan SU
;
Bin YIN
;
Qi Ling ZHAO
;
Nicole KEMPER
;
Joerg HARTUNG
;
En Dong BAO
Author Information
1. College of Veterinary Medicine, Nanjing Agricultural University, Nanjing 210095, China. b_endong@njau.edu.cn
- Publication Type:Original Article
- Keywords:
Hsp90 heat-shock proteins;
anti-apoptosis;
chicken primary myocardial cells;
heat stress disorders
- MeSH:
Apoptosis*;
Aspirin;
Cell Survival;
Chickens*;
Heat Stress Disorders;
Heat-Shock Proteins*;
Hot Temperature*;
HSP90 Heat-Shock Proteins;
In Vitro Techniques*;
Proto-Oncogene Proteins c-akt;
Reactive Oxygen Species;
Transducers
- From:Journal of Veterinary Science
2017;18(2):129-140
- CountryRepublic of Korea
- Language:English
-
Abstract:
To determine heat-shock protein (Hsp)90 expression is connected with cellular apoptotic response to heat stress and its mechanism, chicken (Gallus gallus) primary myocardial cells were treated with the Hsp90 promoter, aspirin, and its inhibitor, geldanamycin (GA), before heat stress. Cellular viability, heat-stressed apoptosis and reactive oxygen species level under different treatments were measured, and the expression of key proteins of the signaling pathway related to Hsp90 and their colocalization with Hsp90 were detected. The results showed that aspirin treatment increased the expression of protein kinase B (Akt), the signal transducer and activator of transcription (STAT)-3 and p-IKKα/β and the colocalization of Akt and STAT-3 with Hsp90 during heat stress, which was accompanied by improved viability and low apoptosis. GA significantly inhibited Akt expression and p-IKKα/β level, but not STAT-3 quantity, while the colocalization of Akt and STAT-3 with Hsp90 was weakened, followed by lower cell viability and higher apoptosis. Aspirin after GA treatment partially improved the stress response and apoptosis rate of tested cells caused by the recovery of Akt expression and colocalization, rather than the level of STAT-3 (including its co-localization with Hsp90) and p-IKKα/β. Therefore, Hsp90 expression has a positive effect on cellular capacity to resist heat-stressed injury and apoptosis. Moreover, inhibition of Hsp90 before stress partially attenuated its positive effects.
