Characterization of cold-induced heat shock protein expression in neonatal rat cardiomyocytes

Cardiac surgery is usually performed under conditions of cardioplegic ischemic arrest. To protect the heart during the ischemic period, the myocardium is exposed to varying degrees of hypothermia. Although hyperthermia is known to induce the heat shock response, the molecular effects of hypothermia...

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Veröffentlicht in:Molecular and cellular biochemistry 1997-08, Vol.173 (1-2), p.153-159
Hauptverfasser: Laios, E, Rebeyka, I M, Prody, C A
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Rebeyka, I M
Prody, C A
description Cardiac surgery is usually performed under conditions of cardioplegic ischemic arrest. To protect the heart during the ischemic period, the myocardium is exposed to varying degrees of hypothermia. Although hyperthermia is known to induce the heat shock response, the molecular effects of hypothermia on the myocardium have not been investigated. We have studied the effect of hypothermia on the induction of heat shock proteins in primary cultures of neonatal cardiomyocytes. Cold stress in cardiomyocytes induced a 6 fold increase in the heat shock protein HSP70 as compared to control. Increased HSP70 protein levels correlated with induction of HSP70 mRNAs. Maximal levels of HSP70 protein appeared 4-6 h following recovery from cold shock, indicating the transient nature of the response. Induction of HSP25 mRNA was also observed in cold-shocked cardiomyocytes, even though increased HSP25 protein levels were not detected. Our results indicate that hypothermia is capable of inducing the heat shock response in neonatal cardiomyocytes.
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To protect the heart during the ischemic period, the myocardium is exposed to varying degrees of hypothermia. Although hyperthermia is known to induce the heat shock response, the molecular effects of hypothermia on the myocardium have not been investigated. We have studied the effect of hypothermia on the induction of heat shock proteins in primary cultures of neonatal cardiomyocytes. Cold stress in cardiomyocytes induced a 6 fold increase in the heat shock protein HSP70 as compared to control. Increased HSP70 protein levels correlated with induction of HSP70 mRNAs. Maximal levels of HSP70 protein appeared 4-6 h following recovery from cold shock, indicating the transient nature of the response. Induction of HSP25 mRNA was also observed in cold-shocked cardiomyocytes, even though increased HSP25 protein levels were not detected. 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subjects Animals
Animals, Newborn - metabolism
Bacteria
Cardiomyocytes
Cold Temperature
Heat shock proteins
Heat-Shock Proteins - biosynthesis
HSP70 Heat-Shock Proteins - biosynthesis
HSP90 Heat-Shock Proteins - biosynthesis
Hypothermia
Hypothermia - physiopathology
Myocardium - cytology
Myocardium - metabolism
Proteins
Rats
Rats, Wistar
RNA, Messenger - analysis
RNA, Messenger - biosynthesis
Temperature
Time Factors
title Characterization of cold-induced heat shock protein expression in neonatal rat cardiomyocytes
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