Transgenic mice expressing the human heat shock protein 70 have improved post-ischemic myocardial recovery.

Plumier, Jean-Christophe; Ross, B.; Currie, R. William; Angelidis, Charalampos; Kazlaris, H.; Kollias, George; Pagoulatos, Gerassimos N.

doi:10.1172/jci117865

Cited by 529 publications

(280 citation statements)

References 36 publications

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“…Glucose-insulin-potassium infusion improves the survival of patients with ischemic heart disease, partially because of enhanced glucose uptake and glycolysis by the ischemic myocardium (1). Studies in transgenic mice overexpressing HSP70 and in rats that had received HSP70 expression vectors also indicate that this protein protects myocardium against ischemiareperfusion injury (17,24,26,29,31). Recently we reported (18) that in human fetal cardiac cells, adenovirus-mediated expression of HIF-1␣/VP16 upregulated VEGF, Glut-1, Glut-3, IGFBP-3, gp130, survivin, TNF-␣-inducible protein, and glycolytic enzymes.…”

Section: Fig 1 Effects Of Preconditioning (Pc) On Cell Viability (Amentioning

confidence: 99%

“…Activation of protein kinase C (4), protein tyrosine kinases (16), and mitogen-activated protein kinases (33) by these triggers leads to increased expression of the mediators of the late phase of preconditioning. Myocardial protein synthesis of several mediators (or effectors), including inducible NO synthase (iNOS), cyclooxygenase-2 (COX-2), aldose reductase, antioxidant enzymes, and heat shock proteins (HSPs), and activation of ATP-sensitive K ϩ (K ATP ) channels play a critical role in late-phase preconditioning (8,15,21,23,24,29). It has been proposed that activator protein 1 (AP-1) and nuclear factor-B (NF-B) may mediate the transcriptional activation of iNOS, COX-2, aldose reductase, and other genes (22,36).…”

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confidence: 99%

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Expression of constitutively stable hybrid hypoxia-inducible factor-1α protects cultured rat cardiomyocytes against simulated ischemia-reperfusion injury

Date¹,

Mochizuki²,

Belanger³

et al. 2005

American Journal of Physiology-Cell Physiology

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Section: Fig 1 Effects Of Preconditioning (Pc) On Cell Viability (Amentioning

confidence: 99%

mentioning

confidence: 99%

Expression of constitutively stable hybrid hypoxia-inducible factor-1α protects cultured rat cardiomyocytes against simulated ischemia-reperfusion injury

Date¹,

Mochizuki²,

Belanger³

et al. 2005

American Journal of Physiology-Cell Physiology

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“…The geese heart Hsp70 expression increased under heat stress suggesting that HSP70 had a protective function in cells . Overexpression of Hsp70 is associated with myocardial protection (Plumier et al 1995;Jayakumar et al 2001;Liu et al 2007). Hao et al (2010) reported the effect of transport stress on variation in the expression of Hsp27, Hsp70, and Hsp90, and the results suggested that Hsps could protect cardiac muscle cells from transport stress.…”

Section: Introductionmentioning

confidence: 99%

The role of heat shock proteins in inflammatory injury induced by cold stress in chicken hearts

Zhao

Zhang

Wang

et al. 2013

Cell Stress and Chaperones

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The aim of this study was to investigate the effects of cold stress on the expression levels of heat shock proteins (Hsps90, 70, 60, 40, and 27) and inflammatory factors (iNOS, COX-2, NF-κB, TNF-α, and PTGEs) and oxidative indexes in hearts of chickens. Two hundred forty 15-day-old male chickens were randomly divided into 12 groups and kept at the temperature of 12±1°C for acute and chronic cold stress. There were one control group and five treatment groups for acute cold stress, three control groups, and three treatment groups for chronic cold stress. After cold stress, malondialdehyde level increased in chicken heart; the activity of superoxide dismutase and glutathione peroxidase in the heart first increased and then decreased. The inflammatory factors mRNA levels were increased in cold stress groups relative to control groups. The histopathological analysis showed that heart tissues were seriously injured in the cold stress group. Additionally, the mRNA levels of Hsps (70, 60, 40, and 27) increased significantly (P<0.05) in the cold stress groups relative to the corresponding control group. Meanwhile, the mRNA level and protein expression of Hsp90 decreased significantly (P<0.05) in the stress group, and showed a gradually decreasing tendency. These results suggested that the levels of inflammatory factors and Hsps expression levels in heart tissues can be influenced by cold stress. Hsps commonly played an important role in the protection of the heart after cold stress.

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“…Overexpression of Hsps, and of Hsp72 in particular, has been shown to protect cells and tissues during episodes of stress (Johnston and Kucey 1988;Riabowol et al 1988;Karmazyn et al 1990;Li et al 1991;Plumier et al 1995). The exact mechanism by which Hsps provide protection remains unknown, but it is thought to relate to their ability to act as molecular chaperones.…”

Section: Introductionmentioning

confidence: 99%

Heat shock transcription factor activation and Hsp72 accumulation in aged skeletal muscle

Locke¹

2000

Cell Stress Chaper

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Induction of the protective heat shock proteins (Hsps), and of Hsp72 in particular, has been reported to be decreased in certain tissues from aged animals. To determine if both fast and slow skeletal muscles from aged animals demonstrate an altered ability to induce and accumulate Hsp72, adult (age, 6 months) and aged (age, 20 months) Fischer 344 rats were subjected to heat stress. At selected times (0, 1, 3, and 24 hours) after a 10-minute, 41ЊC heat stress, fast (white gastrocnemius [WG]) and slow (soleus) skeletal muscles were examined for either heat shock transcription factor (HSF) activation (trimerization and DNA-binding activity) or Hsp72 content using electrophoretic gel mobility shift assays and Western blotting, respectively. Immediately after heat stress, the level of HSF activation between aged and adult animals was similar for both muscles. HSF activation was undetectable at 1 and 3 hours after heat stress in all cases. Twenty-four hours after heat stress, Hsp72 content in the WG muscles from both aged and adult animals was significantly increased compared with unstressed, age-matched controls (P Ͻ 0.05). In contrast, perhaps because of their high constitutive Hsp72 levels, soleus muscles from both aged and adult animals did not demonstrate a significant increase in Hsp72 content after heat shock, but there was a trend toward increased levels. Hsp72 content in both the soleus and WG muscles demonstrated no significant differences between adult and aged animals in either the unstressed state (controls) or after heat shock. These results suggest that skeletal muscles from aged animals are capable of inducing the heat shock response and accumulating Hsp72.

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Transgenic mice expressing the human heat shock protein 70 have improved post-ischemic myocardial recovery.

Cited by 529 publications

References 36 publications

Expression of constitutively stable hybrid hypoxia-inducible factor-1α protects cultured rat cardiomyocytes against simulated ischemia-reperfusion injury

Expression of constitutively stable hybrid hypoxia-inducible factor-1α protects cultured rat cardiomyocytes against simulated ischemia-reperfusion injury

The role of heat shock proteins in inflammatory injury induced by cold stress in chicken hearts

Heat shock transcription factor activation and Hsp72 accumulation in aged skeletal muscle

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