Constitutive and Inducible hsp70s are Involved in Oxidative Resistance Evoked by Heat Shock or Ethanol

Su, Ching‐Yuan; Chong, Kowit-Yu; Owen, Oliver E.; Dillmann, Wolfgang H.; Chang, Chawnshang; Lai, Chen-Ching

doi:10.1006/jmcc.1997.0622

Cited by 85 publications

(34 citation statements)

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“…(b) Result of densitometric scanning and equalisation for actin levels for three replicate blots. stressful stimuli (Su et al 1998). This study clearly reports no significant changes in inducible hsp70 protein expression by UCN.…”

Section: Discussionsupporting

confidence: 47%

Urocortin increases the expression of heat shock protein 90 in rat cardiac myocytes in a MEK1/2-dependent manner

Brar¹,

Railson²,

Stephanou³

et al. 2002

Journal of Endocrinology

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We have previously demonstrated that urocortin protects cultured cardiac myocytes from ischaemic and reoxygenation injury and decreases the infarct size in the rat heart exposed to regional ischaemia and reperfusion. Urocortin-mediated cardioprotection is via activation of the mitogen-activated protein kinase (MAP kinase, MEK1/2) pathway. In addition, it is well documented that heat shock protein (hsp) 70 and hsp90 are cardioprotective against lethal stress. In this study we show, for the first time, that urocortin induces the expression of hsp90 but not hsp70 in primary cultures of rat neonatal cardiac myocytes. Levels of hsp90 protein increase by 1·5-fold over untreated cells within 10 min of urocortin treatment and are sustained for 24 h with a maximal increase of 2·5-fold at 60 min (P<0·05 at all time points). The increase in hsp90 expression by urocortin was not inhibited by actinomycin D, and urocortin failed to increase hsp90 promoter activity. Urocortin induction of hsp90 was inhibited by the MEK1/2 inhibitor PD98059 (P<0·001) and by cycloheximide, and both inhibitors abrogate urocortin-mediated cardioprotection (P<0·05 for cycloheximide, P<0·001 for PD98059). Hence, MEK1/2 and protein synthesis are involved in the cardioprotective effect of urocortin against hypoxic-mediated cell death, possibly due to an increase in expression of hsp90 protein. This is the first report of heat shock protein induction by urocortin or any other member of the corticotrophin-releasing hormone family.

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Section: Discussionsupporting

confidence: 47%

Urocortin increases the expression of heat shock protein 90 in rat cardiac myocytes in a MEK1/2-dependent manner

Brar¹,

Railson²,

Stephanou³

et al. 2002

Journal of Endocrinology

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“…The cardioprotective action of Hsp70 has been particularly well-demonstrated by numerous groups, 46 -49 and this and other heat-shock-induced effectors may limit cell death by acting as "molecular chaperones" for damaged proteins, 50 inhibiting pro-apoptotic signaling, 51 or opposing oxidative stress. 52 The presence of both host (rat) and graft (human) vessels within the hESC-derived cardiac implants is also intriguing. Although the present histological study cannot address whether the human-derived vessels are in fact interconnected with the rest of the rodent vasculature, their extensive ingrowth invites speculation that they may be expanding to support the growth of the cardiac implants and that deliberate "doping" of the implanted hESC-derived cardiomyocytes with hESC-derived endothelial cells might further promote graft survival.…”

Section: Discussionmentioning

confidence: 99%

Formation of Human Myocardium in the Rat Heart from Human Embryonic Stem Cells

Laflamme

Gold

et al. 2005

The American Journal of Pathology

401

285

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Human embryonic stem cells (hESCs) offer the opportunity to replenish cells lost in the postinfarct heart. We explored whether human myocardium could be generated in rat hearts by injecting differentiated cardiac-enriched hESC progeny into the left ventricular wall of athymic rats. Although initial grafts were predominantly epithelial, noncardiac elements were lost over time, and grafts consisted predominantly of cardiomyocytes by 4 weeks. No teratomatous elements were observed. Engrafted cardiomyocytes were glycogen-rich and expressed expected cardiac markers including ␤-myosin heavy chain, myosin light chain 2v, and atrial natriuretic factor. Heat-shock treatment improved graft size approximately threefold. The cardiac implants exhibited substantial angiogenesis, both recipient and graft derived. Importantly, there was greater proliferation in human cardiomyocytes than previously seen in rodent-derived cardiomyocytes: 14.4% of graft cardiomyocytes expressed the proliferation marker Ki-67, and 2.7% incorporated the thymidine analog BrdU 4 weeks after transplantation. This proliferation was associated with a sevenfold increase in graft size over the 4-week interval. Thus, hESCs can form human myocardium in the rat heart, permitting studies of human myocardial development and physiology and supporting the feasibility of their use in myocardial repair.

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“…H9c2 cells treated with 6 % ethanol for 1 h developed thermotolerance and resistance to H 2 O 2 , which might be due to the elevated expression of Hsp70 (Su et al 1998). It has also been revealed that prior administration of ethanol offers a protective effect against neuronal damage due to cerebral ischemia reperfusion in gerbils (Wang et al 2007).…”

Section: Heat Shock Proteins and Their Roles In Membrane Protectionmentioning

confidence: 99%

Alcohol stress, membranes, and chaperones

Tóth

Vı́gh

Sántha

2014

Cell Stress and Chaperones

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Ethanol, which affects all body organs, exerts a number of cytotoxic effects, most of them independent of cell type. Ethanol treatment leads to increased membrane fluidity and to changes in membrane protein composition. It can also interact directly with membrane proteins, causing conformational changes and thereby influencing their function. The cytotoxic action may include an increased level of oxidative stress. Heat shock protein molecular chaperones are ubiquitously expressed evolutionarily conserved proteins which serve as critical regulators of cellular homeostasis. Heat shock proteins can be induced by various forms of stresses such as elevated temperature, alcohol treatment, or ischemia, and they are also upregulated in certain pathological conditions. As heat shock and ethanol stress provoke similar responses, it is likely that heat shock protein activation also has a role in the protection of membranes and other cellular components during alcohol stress.

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Constitutive and Inducible hsp70s are Involved in Oxidative Resistance Evoked by Heat Shock or Ethanol

Cited by 85 publications

References 0 publications

Urocortin increases the expression of heat shock protein 90 in rat cardiac myocytes in a MEK1/2-dependent manner

Urocortin increases the expression of heat shock protein 90 in rat cardiac myocytes in a MEK1/2-dependent manner

Formation of Human Myocardium in the Rat Heart from Human Embryonic Stem Cells

Alcohol stress, membranes, and chaperones

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