Overexpression of heat shock protein 60/10 in myocardium of patients with chronic atrial fibrillation

Schafler, A. E.; Kirmanoglou, Kiriakos; Pecher, P.; Hannekum, A; Schumacher, B.

doi:10.1016/s0003-4975(02)03830-4

Cited by 25 publications

(20 citation statements)

References 16 publications

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“…More recently, an up-regulation of these chaperones was demonstrated also in human myocardium during chronic atrial fibrillation [28]. These data indicate a protective role of these HSPs during the hypoxic-ischemic stress.…”

Section: Discussionmentioning

confidence: 64%

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: 64%

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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“…HSP10 was also found to be increased [48]. Interestingly, HSP60 levels in atrial myocardium of moderate, severe, and profound myolysis groups of patients with AF were significantly lower than in specimens from patients with light myolysis, while no differences were found for other HSPs [49].…”

Section: Hsp60 Increase In Atrial Fibrillation: Cause or Consequence?mentioning

confidence: 84%

“…HSP60 protein was found to be increased in atrial myocardial samples of patients with chronic AF compared with patients in sinus rhythm [47,48]. HSP10 was also found to be increased [48].…”

Section: Hsp60 Increase In Atrial Fibrillation: Cause or Consequence?mentioning

confidence: 87%

Heat Shock Protein-60 and Risk for Cardiovascular Disease

Rizzo¹,

Macario²,

Macario³

et al. 2011

CPD

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Cardiovascular disease (CVD) is a leading cause of morbidity and mortality worldwide. There is growing evidence that molecular chaperones, many of which are heat shock proteins HSPs, are involved in CVD pathogenesis. In this review we focus on HSP60, the human mitochondrial chaperone that also displays extramitochondrial and extracellular functions. HSP60 is typically cytoprotective but a number of stress conditions determine its conversion to a potentially toxic molecule for cells and tissues. We present illustrative examples of specific subtypes of CVD where HSP60 is implicated in the initiation and/or progression of disease. The data not only indicate a pathogenic role for HSP60 but also its potential as a biomarker with applications for diagnosis, assessing prognosis and response to treatment, as well as for preventing and treating CVD.

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“…It has only been proven that combined and individual overexpression of chaperonins may protect cells from ischemia-reoxygenation induced cell death. It has also been shown that Hsp10/60 accumula- In the myocardium of patients with chronic atrial fibrillation, the expression of the mitochondrial heat shock proteins Hsp60 and Hsp10 is increased (Schafler et al 2002;Kirmanoglou et al 2004); similar to what happens in the brainstem after subarachnoid hemorrhage (Satoh et al 2003). It has been elucidated that myocyte protection by Hsp10 involves the mobile loop and attenuation of the Ras GTPase pathway (Lin et al 2004).…”

Section: Sat1mentioning

confidence: 95%

Heat shock protein 10 and signal transduction: a “capsula eburnea” of carcinogenesis?

Czarnecka

Campanella²,

Zummo³

et al. 2006

Cell Stress Chaper

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To date, little is known either about the physical interactions of heat shock protein 10 (Hsp10) with other proteins within the cell or its involvement in signal transduction pathways. Hsp10 has been considered mainly as a partner of Hsp60 in the Hsp60/10 protein folding machine. Only recently, Hsp10 was reported to interact with proteins involved in deoxyribonucleic acid checkpoint inactivation, termination of M-phase, messenger ribonucleic acid export, import of nuclear proteins, nucleocytoplasmic transport, and pheromone signaling pathways. At the same time, Hsp10 expression can be up-regulated in cancer cells, because it accumulates as the cell transformation progresses. Recent data suggest that Hsp10 may be not only a component of the folding machine but also an active player of the cell signaling network, influencing cell cycle, nucleocytoplasmic transport, and metabolism, with putative roles in the lack of cell differentiation and in the inhibition of apoptosis. In this review, we revise the involvement of Hsp10 in signal transduction pathways and its possible role in cancer etiology.

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Overexpression of heat shock protein 60/10 in myocardium of patients with chronic atrial fibrillation

Cited by 25 publications

References 16 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

Heat Shock Protein-60 and Risk for Cardiovascular Disease

Heat shock protein 10 and signal transduction: a “capsula eburnea” of carcinogenesis?

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