Reactive Oxygen Species Play an Important Role in the Activation of Heat Shock Factor 1 in Ischemic-Reperfused Heart

Nishizawa, Junichiro; Nakai, Asami; Matsuda, Katsuhiko; Komeda, Masashi; Ban, Toshihiko; Nagata, Kazuhiro

doi:10.1161/01.cir.99.7.934

Cited by 97 publications

(78 citation statements)

References 54 publications

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“…Both sustained hypoglycemia and hyperglycemia (40), as well as oxidative stress, lead to increases in GRP78 expression (41). Hyperglycaemia increases ROS formation in cultured endothelial cells (42), and increased ROS formation and oxidative stress in heart muscle leads to increased mRNA levels of HSP 70 and HSP 90 (43). However, we observed no relationship between fasting plasma glucose levels and the levels of HSP 90␤ or GRP78 arguing against hyperglycemia as the direct cause of cellular stress.…”

Section: Table III Sum Of Expression Of Protein Markers Isoformscontrasting

confidence: 69%

Proteome Analysis Reveals Phosphorylation of ATP Synthase β-Subunit in Human Skeletal Muscle and Proteins with Potential Roles in Type 2 Diabetes

Højlund

Wrzesinski

Larsen

et al. 2003

Journal of Biological Chemistry

209

156

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Insulin resistance in skeletal muscle is a hallmark feature of type 2 diabetes. An increasing number of enzymes and metabolic pathways have been implicated in the development of insulin resistance. However, the primary cellular cause of insulin resistance remains uncertain. Proteome analysis can quantitate a large number of proteins and their post-translational modifications simultaneously and is a powerful tool to study polygenic diseases like type 2 diabetes. Using this approach on human skeletal muscle biopsies, we have identified eight potential protein markers for type 2 diabetes in the fasting state. The observed changes in protein expression indicate increased cellular stress, e.g. up-regulation of two heat shock proteins, and perturbations in ATP (re)synthesis and mitochondrial metabolism, e.g. down-regulation of ATP synthase ␤-subunit and creatine kinase B, in skeletal muscle of patients with type 2 diabetes. Phosphorylation appears to play a key, potentially coordinating role for most of the proteins identified in this study. In particular, we demonstrated that the catalytic ␤-subunit of ATP synthase is phosphorylated in vivo and that the levels of a down-regulated ATP synthase ␤-subunit phosphoisoform in diabetic muscle correlated inversely with fasting plasma glucose levels. These data suggest a role for phosphorylation of ATP synthase ␤-subunit in the regulation of ATP synthesis and that alterations in the regulation of ATP synthesis and cellular stress proteins may contribute to the pathogenesis of type 2 diabetes.Insulin resistance in skeletal muscle, defined as reduced insulin-stimulated glucose disposal, is a characteristic feature of type 2 diabetes mellitus (T2DM) 1 and is believed to be largely accounted for by reduced non-oxidative glucose metabolism (1-3). Furthermore, insulin stimulation of glucose oxidation and suppression of lipid oxidation is significantly impaired in patients with T2DM (2, 3). Conversely, in the basal, fasting state increased glucose oxidation and reduced lipid oxidation is seen in skeletal muscle of insulin resistant subjects, whether caused by T2DM or obesity alone (4). These defects suggest an impaired capacity to switch between carbohydrate and fat as oxidative energy sources in insulin-resistant subjects. Together with reports of reduced oxidative enzyme activity and dysfunction of mitochondria in skeletal muscle of patients with T2DM (4 -6) and the fact that mitochondrial DNA defects cause T2DM through impairment of oxidative phosphorylation (7, 8), these abnormalities in fuel metabolism have led to the hypotheses that perturbations in skeletal muscle mitochondrial metabolism (6, 9, 10) and defects in the signaling pathways of AMP-activated protein kinase (AMPK) are implicated in the pathogenesis of T2DM (11). That rates of fuel oxidation and mitochondrial function can affect glucose uptake and glycogen synthesis has been reported earlier (12, 13). In addition, both chronic activation of AMPK and induced expression of the transcriptional co-activator of peroxisom...

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Section: Table III Sum Of Expression Of Protein Markers Isoformscontrasting

confidence: 69%

Proteome Analysis Reveals Phosphorylation of ATP Synthase β-Subunit in Human Skeletal Muscle and Proteins with Potential Roles in Type 2 Diabetes

Højlund

Wrzesinski

Larsen

et al. 2003

Journal of Biological Chemistry

209

156

View full text Add to dashboard Cite

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“…In close proximity to the STAT binding regions, the Hsp70 and Hsp90␤ promoters also contain binding sites for the stress-activated transcription factor, HSF1 (50). Activation of HSF-1 has been reported in heart tissue perfused with H 2 O 2 (48). Therefore, a concomitant role for HSF1 in thrombin-induced expression of Hsp70 and Hsp90 is possible in view of the stimulation of ROS in thrombintreated VSMC.…”

Section: Discussionmentioning

confidence: 97%

“…Accumulation of Hsps has been reported in cardiac tissue during ischemia and reperfusion, conditions known to produce ROS (48,49). In addition, Hsp70 and Hsp90␤ promoters contain functional STAT-binding sites (50).…”

Section: Thrombin-induced Heat Shock Protein (Hsp70 and Hsp90) Expresmentioning

confidence: 99%

Thrombin Regulates Vascular Smooth Muscle Cell Growth and Heat Shock Proteins via the JAK-STAT Pathway

Madamanchi

Patterson

et al. 2001

Journal of Biological Chemistry

112

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The growth-stimulating effects of thrombin are mediated primarily via activation of a G protein-coupled receptor, PAR-1. Because PAR-1 has no intrinsic tyrosine kinase activity, yet requires tyrosine phosphorylation events to induce mitogenesis, we investigated the role of the Janus tyrosine kinases (JAKs) in thrombin-mediated signaling. JAK2 was activated rapidly in rat vascular smooth muscle cells (

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“…Reactive oxygen species (ROS) also play an essential role in delayed cardioprotection of ischaemic preconditioning [18,25]. There is evidence showing that generation of ROS by heat stress increases HSPs, which in turn renders cardioprotection [13]. There is also evidence that generation of ROS by heat stress renders cardioprotection independent of HSP production [1].…”

Section: Discussionmentioning

confidence: 99%

Failure to confer cardioprotection and to increase the expression of heat-shock protein 70 by preconditioning with a ?-opioid receptor agonist during ischaemia and reperfusion in streptozotocin-induced diabetic rats

Kam

Chen

et al. 2004

Diabetologia

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Aims/hypothesis. The aim of this study was to determine the effects of preconditioning on injury and expression of heat shock proteins 70 in diabetic rat hearts. Methods. Diabetes was induced by an intraperitoneal injection of 65 mg kg −1 streptozotocin. Daily subcutaneous injection of 4 IU insulin started 2 weeks after streptozotocin treatment for 4 weeks. Rats were preconditioned by intravenous injection of 10 mg kg −1 U50,488H, a selective κ-opioid receptor agonist (U50,488H preconditioning). The effects of U50,488H preconditioning had previously been shown to be blocked by a selective κ-opioid receptor antagonist, nor-binaltorphimine. Twenty-four hours later, rats were subjected to 30 min of regional ischaemia by occlusion of the left coronary artery followed by 4 h of reperfusion. Infarct size was determined at the end of reperfusion. Stress-inducible and constitutive heat shock proteins 70 were analysed at the end of ischaemia and reperfusion by Western blotting.Results. Myocardial infarcts induced by ischaemia and reperfusion were greater in diabetic rats. U50,488H preconditioning significantly reduced the infarct size and increased the expression of stress-inducible heatshock protein 70 in normal rats. The effects of U50,488H preconditioning were abolished in streptozotocin-induced diabetic rats, but restored by insulin replacement. Conclusion/interpretation. In addition to a greater susceptibility to ischaemic insults, the delayed cardioprotection of U50,488H preconditioning was lost, which could at least partly be due to impaired synthesis of stress-inducible heat-shock protein 70 in diabetic rats. [Diabetologia (2004) 47:214-220] Keywords U50,488H preconditioning · κ-opioid receptor · Streptozotocin · Diabetic rats · Ischaemia and reperfusion · Cardioprotection stress inducible heat shock protein 70

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Reactive Oxygen Species Play an Important Role in the Activation of Heat Shock Factor 1 in Ischemic-Reperfused Heart

Abstract: Our findings demonstrate that ROSs play an important role in the activation of HSF1 and the accumulation of mRNA for HSP70 and HSP90 in the ischemic-reperfused heart.

Cited by 97 publications

References 54 publications

Proteome Analysis Reveals Phosphorylation of ATP Synthase β-Subunit in Human Skeletal Muscle and Proteins with Potential Roles in Type 2 Diabetes

Proteome Analysis Reveals Phosphorylation of ATP Synthase β-Subunit in Human Skeletal Muscle and Proteins with Potential Roles in Type 2 Diabetes

Thrombin Regulates Vascular Smooth Muscle Cell Growth and Heat Shock Proteins via the JAK-STAT Pathway

Failure to confer cardioprotection and to increase the expression of heat-shock protein 70 by preconditioning with a ?-opioid receptor agonist during ischaemia and reperfusion in streptozotocin-induced diabetic rats

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