Simultaneous induction of mitochondrial heat shock protein mRNAs in rat forebrain ischemia

Okubo, Atsuya; Kinouchi, Hiroyuki; Owada, Yuji; Kunizuka, Hisanori; Itoh, Hidenori; Izaki, Kenji; Kondo, Hisatake; Tashima, Yohtalou; Yoshimoto, Takashi; Mizoi, Kazuo

doi:10.1016/s0169-328x(00)00200-x

Cited by 21 publications

(14 citation statements)

References 61 publications

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“…Rat models of cerebral [24,25] and cardiac ischemia [26,27] showed a simultaneous overexpression of HSP10 and HSP60. More recently, an up-regulation of these chaperones was demonstrated also in human myocardium during chronic atrial fibrillation [28].…”

Section: Discussionmentioning

confidence: 96%

Ten kilodalton heat shock protein (HSP10) is overexpressed during carcinogenesis of large bowel and uterine exocervix

Cappello¹,

Bellafiore²,

David³

et al. 2003

Cancer Letters

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In the present study, we evaluated the presence and the level of expression of HSP10 in two carcinogenetic models: the 'adenoma -carcinoma sequence' of large bowel and the 'dysplasia -carcinoma sequence' of uterine exocervix. We found HSP10 was overexpressed during the carcinogenesis of both organs. In particular, HSP10 was overexpressed early in large bowel carcinogenesis, while the expression of this protein in exocervical carcinogenesis gradually increased from normal through dysplastic to neoplastic tissues. The quantitative analysis of immunohistochemistry and the Western blotting confirmed these results. Our previous observations showed overexpression of HSP60 in the same carcinogenetic models. This report correlates the overexpression of HSP10 with that of HSP60 during carcinogenesis in vivo. These results could stimulate further studies on the pathogenetic role of these proteins during the carcinogenesis as well as their use as diagnostic and prognostic tools in oncology. q

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Section: Discussionmentioning

confidence: 96%

Ten kilodalton heat shock protein (HSP10) is overexpressed during carcinogenesis of large bowel and uterine exocervix

Cappello¹,

Bellafiore²,

David³

et al. 2003

Cancer Letters

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“…These data provide consistent evidence that a profound interplay between Hsps exists and further sustain the importance of Hsps in mediating neuroprotective effects. Most mitochondrial proteins are synthesized in the cytosol and must be imported into the organelles in an unfolded state [39,40]. During translocation, this proteins interact with Hsp70 ATP-dependent binding and the release of Hsp70 provide the major driving force for complete transport of polypeptides into the matrix.…”

Section: Redox Regulation Of Gene Expressionmentioning

confidence: 99%

“…During translocation, this proteins interact with Hsp70 ATP-dependent binding and the release of Hsp70 provide the major driving force for complete transport of polypeptides into the matrix. Although, most imported polypeptides are released from soluble Hsp70, however, a subset of aggregation-sensitive polypeptides must be transferred from Hsp70 to Hsp60 for folding [40]. Owing to the close functional interaction between this chaperonin system and the Hsp70 system, it is likely that up-regulation of Hsp60…”

Section: Redox Regulation Of Gene Expressionmentioning

confidence: 99%

Redox Regulation of Cellular Stress Response in Aging and Neurodegenerative Disorders: Role of Vitagenes

et al. 2006

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Reduced expression and/or activity of antioxidant proteins lead to oxidative stress, accelerated aging and neurodegeneration. However, while excess reactive oxygen species (ROS) are toxic, regulated ROS play an important role in cell signaling. Perturbation of redox status, mutations favoring protein misfolding, altered glyc(osyl)ation, overloading of the product of polyunsaturated fatty acid peroxidation (hydroxynonenals, HNE) or cholesterol oxidation, can disrupt redox homeostasis. Collectively or individually these effects may impose stress and lead to accumulation of unfolded or misfolded proteins in brain cells. Alzheimer's (AD), Parkinson's and Huntington's disease, amyotrophic lateral sclerosis and Friedreich's ataxia are major neurological disorders associated with production of abnormally aggregated proteins and, as such, belong to the so-called "protein conformational diseases". The pathogenic aggregation of proteins in non-native conformation is generally associated with metabolic derangements and excessive production of ROS. The "unfolded protein response" has evolved to prevent accumulation of unfolded or misfolded proteins. Recent discoveries of the mechanisms of cellular stress signaling have led to new insights into the diverse processes that are regulated by cellular stress responses. The brain detects and overcomes oxidative stress by a complex network of "longevity assurance processes" integrated to the expression of genes termed vitagenes. Heat-shock proteins are highly conserved and facilitate correct protein folding. Heme oxygenase-1, an inducible and redox-regulated enzyme, has having an important role in cellular antioxidant defense. An emerging concept is neuroprotection afforded by heme oxygenase by its heme degrading activity and tissue-specific antioxidant effects, due to its products carbon monoxide and biliverdin, which is then reduced by biliverdin reductase in bilirubin. There is increasing interest in dietary compounds that can inhibit, retard or reverse the steps leading to neurodegeneration in AD. Specifically any dietary components that inhibit inappropriate inflammation, AbetaP oligomerization and consequent increased apoptosis are of particular interest, with respect to a chronic inflammatory response, brain injury and beta-amyloid associated pathology. Curcumin and ferulic acid, the first from the curry spice turmeric and the second a major constituent of fruit and vegetables, are candidates in this regard. Not only do these compounds serve as antioxidants but, in addition, they are strong inducers of the heat-shock response. Food supplementation with curcumin and ferulic acid are therefore being considered as a novel nutritional approach to reduce oxidative damage and amyloid pathology in AD. We review here some of the emerging concepts of pathways to neurodegeneration and how these may be overcome by a nutritional approach.

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“…These studies suggest that induction of hsp60 under pathologic conditions reflects the degree of mitochondrial stress and serves as a protective response. Increased hsp60 expression has been observed in various cerebral ischemia models [Abe et al, 1998;Izaki et al, 2001;Okubo et al, 2000;Wagstaff et al, 1996]. Alterations in mitochondrial ultrastructure [Solenski et al, 2002] and impairment in mitochondrial respiration [Sims and Pulsinelli, 1987] have also been demonstrated following experimental cerebral ischemia.…”

Section: Discussionmentioning

confidence: 99%

“…In conjunction with hsp10, hsp60 participates in the appropriate folding of proteins within the mitochondria. In the central nervous system, hsp60 expression was shown to be increased after various ischemic injury paradigms [Abe et al, 1998;Izaki et al, 2001;Okubo et al, 2000;Wagstaff et al, 1996]. However, there have been no studies examining hsp60 expression after TBI, with the exception of a study showing decreased hsp60 in leukocytes from adult TBI patients [Hashiguchi et al, 2003].…”

Section: Introductionmentioning

confidence: 99%

Mitochondrial Heat Shock Protein 60 Is Increased in Cerebrospinal Fluid following Pediatric Traumatic Brain Injury

Lai¹,

Stange²,

Wisniewski³

et al. 2006

Dev Neurosci

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Mitochondrial dysfunction occurs after traumatic brain injury (TBI) and contributes significantly to subsequent cell death. Heat shock protein 60 (hsp60) is a predominantly mitochondrial protein with important homeostatic functions. Induction of hsp60 has been demonstrated in cerebral ischemia models, possibly reflecting mitochondrial stress. We measured hsp60 concentration in the cerebrospinal fluid (CSF) of 34 infants and children after severe TBI and of 7 control patients by ELISA. Peak CSF hsp60 concentration was increased in TBI patients versus controls (0.84 ng/ml, range 0–44.59, vs. 0.0 ng/ml, range 0–0.48; p < 0.05). Induction of hsp60 occurred early after the injury. Peak hsp60 concentration was independently associated with the severity of injury, defined as the admission Glasgow Coma Scale score. These data suggest that increased hsp60 in CSF might reflect the severity of early mitochondrial stress or damage after TBI.

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Simultaneous induction of mitochondrial heat shock protein mRNAs in rat forebrain ischemia

Cited by 21 publications

References 61 publications

Ten kilodalton heat shock protein (HSP10) is overexpressed during carcinogenesis of large bowel and uterine exocervix

Ten kilodalton heat shock protein (HSP10) is overexpressed during carcinogenesis of large bowel and uterine exocervix

Redox Regulation of Cellular Stress Response in Aging and Neurodegenerative Disorders: Role of Vitagenes

Mitochondrial Heat Shock Protein 60 Is Increased in Cerebrospinal Fluid following Pediatric Traumatic Brain Injury

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