Localization and expression of heat shock protein 70 with rat myocardial cell damage induced by heat stress in vitro and in vivo

  • Authors:
    • Hongbo Chen
    • Abdelnasir Adam
    • Yanfen Cheng
    • Shu Tang
    • Jörg Hartung
    • Endong Bao
  • View Affiliations

  • Published online on: November 20, 2014     https://doi.org/10.3892/mmr.2014.2986
  • Pages: 2276-2284
Metrics: Total Views: 0 (Spandidos Publications: | PMC Statistics: )
Total PDF Downloads: 0 (Spandidos Publications: | PMC Statistics: )


Abstract

The aim of the present study was to investigate the association between heat shock protein (Hsp) 70 expression kinetics and heat stress‑induced damage to rat myocardial cells in vitro and in vivo. The results showed that the activity of heart injury‑associated enzymes, including aspartate aminotransferase and creatine kinase, significantly increased and myocardial cells developed acute histopathological lesions; this therefore suggested that heat stress altered the integrity of myocardial cells in vitro and in vivo. Levels of Hsp70 in vitro decreased following the initiation of heat stress and then steadily increased until heat stress ceased at 100 min; however, in vivo studies demonstrated a gradual increase in Hsp70 levels in the heart cells of rats from the initiation of heat stress, followed by a sharp decline at 100 min. These results indicated that the cells sustained different degrees of injury in vivo compared with those sustained in vitro, this may be due to different regulatory mechanisms in the two environments. Intracytoplasmic Hsp70 signaling was significantly reduced at 60 min in vitro, compared with that of the in vivo study, indicating that Hsp70 consumption may have exceeded its production prior to 60 min of heat stress, and following 60 min the cells produced sufficient Hsp70 protein for their protection against heat stress. Hsp70‑positive signals in the cytoplasm of heart cells in vivo were more prominent in the intact areas compared with those of the degenerated areas and the density of Hsp70‑positive signals was significantly reduced following 60 min of heat stress. In conclusion, comprehensive comparisons of enzymes, cell morphology and Hsp70 levels indicated that decreased levels of Hsp70 were associated with the reduced protective effect on myocardial cells in vitro and in vivo.
View Figures
View References

Related Articles

Journal Cover

March-2015
Volume 11 Issue 3

Print ISSN: 1791-2997
Online ISSN:1791-3004

Sign up for eToc alerts

Recommend to Library

Copy and paste a formatted citation
x
Spandidos Publications style
Chen H, Adam A, Cheng Y, Tang S, Hartung J and Bao E: Localization and expression of heat shock protein 70 with rat myocardial cell damage induced by heat stress in vitro and in vivo. Mol Med Rep 11: 2276-2284, 2015
APA
Chen, H., Adam, A., Cheng, Y., Tang, S., Hartung, J., & Bao, E. (2015). Localization and expression of heat shock protein 70 with rat myocardial cell damage induced by heat stress in vitro and in vivo. Molecular Medicine Reports, 11, 2276-2284. https://doi.org/10.3892/mmr.2014.2986
MLA
Chen, H., Adam, A., Cheng, Y., Tang, S., Hartung, J., Bao, E."Localization and expression of heat shock protein 70 with rat myocardial cell damage induced by heat stress in vitro and in vivo". Molecular Medicine Reports 11.3 (2015): 2276-2284.
Chicago
Chen, H., Adam, A., Cheng, Y., Tang, S., Hartung, J., Bao, E."Localization and expression of heat shock protein 70 with rat myocardial cell damage induced by heat stress in vitro and in vivo". Molecular Medicine Reports 11, no. 3 (2015): 2276-2284. https://doi.org/10.3892/mmr.2014.2986