Induction of HSP70 in cultured rat neonatal cardiomyocytes by hypoxia and metabolic stress.

Iwaki, Kazumi; Chi, Shun-Hua; Dillmann, Wolfgang H.; Mestril, Ruben

doi:10.1161/01.cir.87.6.2023

Cited by 160 publications

(85 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Myocardial ischemia is a known potent inducer of the stress protein response. Several stimuli trigger the upregulation of myocardial stress proteins in response to ischemia (Benjamin et al, 1992;Iwaki et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

Temporal variations of Hsp60 and HSF-1 in primary rat myocardial cells in vitro under heat stress

Rehana

Lv²,

Islam³

et al. 2013

Genet. Mol. Res.

View full text Add to dashboard Cite

ABSTRACT. The mechanisms involved in sudden animal death due to acute heart failure during heat stress are not well understood. We examined the relationship between heat stress-induced variations of protective Hsp60 and expression of its regulatory factor, HSF-1, in heat-stressed primary myocardial cells of neonatal rats in vitro through cardiac enzyme detection, immunoblotting, immunocytochemistry, and qPCR. Increases in cardiac damage-related enzyme levels demonstrated injury to myocardial cells after heat exposure at 42°C. Hsp60 expression levels fluctuated during heat stress; they decreased significantly after 20 min, then increased at 120 min and decreased again at 360 min after initiation of heat stress. The highest levels of Hsp60 were observed at 240 min, while the lowest were at 60 min. Damage to myocardial cells was characterized by increases in cardiac enzyme levels and low levels of Hsp60 due to functional disorder of myocardial cells at early stages of heat stress. However, the significant induction of hsp60 mRNA levels from the beginning up to 240 min of heat stress was not consistent with the classic regulatory mechanisms that link transcription and translation, suggesting that Hsp60 expression is delayed due to loss of Hsp60 during the early stages of heat stress. hsf-1 mRNA levels were significantly increased from 10 min of heat stress; however, HSF-1 protein levels did not simultaneously increase, indicating that HSF-1 is not the sole regulator of Hsp60 expression.

show abstract

Section: Introductionmentioning

confidence: 99%

Temporal variations of Hsp60 and HSF-1 in primary rat myocardial cells in vitro under heat stress

Rehana

Lv²,

Islam³

et al. 2013

Genet. Mol. Res.

View full text Add to dashboard Cite

show abstract

“…Among these stressors, one finds oxygen deprivation, ATP depletion, Ca2+ influx, glucose deprivation, accumulation of toxic metabolites, decrease in cellular pH, and other changes. Recently, we have found that several ofthe these alterations caused by ischemia will also induce the expression ofthe HSP70 family of proteins in rat neonatal cardiac myocytes ( 12) and in a rat embryonic heart cell line H9c2(2-1 ). Given the strong HSP70 response to ischemia-related events, it is of great interest to examine the potential protective role of the HSP70 in cardiac cells under stress in vitro.…”

Section: Introductionmentioning

confidence: 99%

Expression of inducible stress protein 70 in rat heart myogenic cells confers protection against simulated ischemia-induced injury.

Mestril¹,

Chi²,

Sayen³

et al. 1994

J. Clin. Invest.

Self Cite

276

136

View full text Add to dashboard Cite

Myocardial ischemia markedly increases the expression of several members of the stress/heat shock protein (HSP) family, especially the inducible HSP70 isoforms. Increased expression of HSP70 has been shown to exert a protective effect against a lethal heat shock. We have examined the possibility of using this resistance to a lethal heat shock as a protective effect against an ischemic-like stress in vitro using a rat embryonic heart-derived cell line H9c2(2-1). Myogenic cells in which the heat shock proteins have been induced by a previous heat shock are found to become resistant to a subsequent simulated ischemic stress. In addition, to address the question of how much does the presence of the HSP70 contribute to this protective effect, we have generated stably transfected cell lines overexpressing the human-inducible HSP70. Embryonal rat heartderived H9c2(2-1 ) cells were used for this purpose. This stably transfected cell line was found to be significantly more resistant to an ischemic-like stress than control myogenic cells only expressing the selectable marker (neomycin) or the parental cell line H9c2(2-1). This finding implicates the inducible HSP70 protein as playing a major role in protecting cardiac cells against ischemic injury. (J. Clin. Invest. 1994. 93:759-767.)

show abstract

“…Chronic cyclosporine A treatment also induces in vivo HSP90 expression in the heart and is associated with modulation of protective endothelial nitric oxide synthase signaling (Rezzani et al, 2003). HSP 70 protects the heart from hypoxia or reoxygenation and postinfarction stresses in the heart (Iwaki et al, 1993;Marber et al, 1995). The results about HSP70 dynamic during chemotherapy are contradictive possibly due to the multitude of roles of HSP70s (Kampinga et al, 2010).…”

Section: Heat Shock Proteinsmentioning

confidence: 99%

Early Detection and Prediction of Cardiotoxicity - Biomarker and Echocardiographic Evaluation

Goudev¹

2012

Cardiotoxicity of Oncologic Treatments

View full text Add to dashboard Cite

Induction of HSP70 in cultured rat neonatal cardiomyocytes by hypoxia and metabolic stress.

Cited by 160 publications

References 24 publications

Temporal variations of Hsp60 and HSF-1 in primary rat myocardial cells in vitro under heat stress

Temporal variations of Hsp60 and HSF-1 in primary rat myocardial cells in vitro under heat stress

Expression of inducible stress protein 70 in rat heart myogenic cells confers protection against simulated ischemia-induced injury.

Early Detection and Prediction of Cardiotoxicity - Biomarker and Echocardiographic Evaluation

Contact Info

Product

Resources

About