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Updated: Feb 3, 2026

Murine Model of Intestinal Ischemia-reperfusion Injury
Published on: May 11, 2016
Expression of calcineurin, calpastatin and heat shock proteins during ischemia and reperfusion
Sreejit Parameswaran1, Rajendra K Sharma1
1Department of Pathology and Laboratory Medicine, College of Medicine, University of Saskatchewan, Saskatoon, Saskatchewan, Canada S7N 5E5.
Objective:
Calcineurin (CaN) interacts with calpains (Calpn) and causes cellular damage eventually leading to cell death. Calpastatin (Calp) is a specific Calpn inhibitor, along with CaN stimulation has been implicated in reduced cell death and self-repair. Molecular chaperones, heat shock proteins (Hsp70 and Hsp90) acts as regulators in Calpn signaling. This study aims to elucidate the role of CaN, Calp and Hsps during induced ischemia and reperfusion in primary cardiomyocyte cultures (murine).
Methods And Results:
Protein expression was analyzed concurrently with viability using flow cytometry (FACS) in ischemia- and reperfusion-induced murine cardiomyocyte cultures. The expression of Hsp70 and Hsp90, both being molecular chaperones, increased during ischemia with a concurrent increase in death of cells expressing these proteins. The relative expression of Hsp70 and Hsp90 during ischemia with respect to CaN was enhanced in comparison to Calp. Reperfusion slightly decreased the number of cells expressing these chaperones. There was no increase in death of cells co-expressing Hsp70 and Hsp90 along with CaN and Calp. CaN expression peaked during ischemia and subsequent reperfusion reduced its expression and cell death. Calp expression increased both during ischemia and subsequent reperfusion but cell death decreased during reperfusion.
Conclusion:
The present study adds to the existing knowledge that Hsp70, Hsp90, CaN and Calp interact with each other and play significant role in cardio protection.
Insights
Calcineurin (CaN) and calpains (Calp) signaling in cardiomyocytes is modulated by heat shock proteins (Hsp70, Hsp90). These proteins play a significant role in cardio protection during ischemia and reperfusion, influencing cell death and repair mechanisms.
Area of Science:
- Cardiovascular Biology
- Cellular Signaling
- Molecular Medicine
Background:
- Calcineurin (CaN) and calpains (Calpn) signaling pathways are implicated in cardiomyocyte damage and cell death.
- Calpastatin (Calp) inhibits calpains and, with CaN stimulation, may promote cell survival and repair.
- Molecular chaperones, specifically heat shock proteins (Hsp70 and Hsp90), regulate calpain signaling.
Purpose of the Study:
- To investigate the roles of CaN, Calp, Hsp70, and Hsp90 in murine cardiomyocyte cultures subjected to induced ischemia and reperfusion.
- To elucidate the interactions between these proteins and their impact on cell viability and death during ischemic events.
Main Methods:
- Primary murine cardiomyocyte cultures were subjected to induced ischemia and reperfusion.
- Protein expression levels of CaN, Calp, Hsp70, and Hsp90 were analyzed.
- Cell viability was assessed using flow cytometry (FACS).
Main Results:
- Hsp70 and Hsp90 expression increased during ischemia, correlating with increased cell death.
- Relative expression of Hsp70/Hsp90 to CaN was higher than to Calp during ischemia.
- Reperfusion led to a decrease in chaperone-expressing cells, reduced CaN expression and cell death, and increased Calp expression with decreased cell death.
Conclusions:
- Hsp70, Hsp90, CaN, and Calp interact and are crucial for cardio protection.
- These proteins collectively influence cardiomyocyte survival and death during ischemic and reperfusion injury.
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