Rat Hsp20 Confers Thermoresistance in a Clonal Survival Assay, but Fails to Protect Coexpressed Luciferase in Chinese Hamster Ovary Cells

Klundert, Francy A. J. M. van de; IJssel, Paul R.L.A. van den; Stege, G. J. J.; Jong, Wilfried W. de

doi:10.1006/bbrc.1998.9917

Cited by 23 publications

(14 citation statements)

References 24 publications

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“…It was shown that the recombinant human Hsp20 has chaperone activity that is comparable with that of commercial α crystallin [10]. These data agree with earlier published data of van de Klundert et al [49]. These authors have shown that overexpression of either Hsp20 or αB crystallin confer thermal resistance in Chinese hamster ovary cells.…”

supporting

confidence: 89%

Structure, Properties, and Probable Physiological Role of Small Heat Shock Protein with Molecular Mass 20 kD (Hsp20, HspB6)

Gusev

Bukach

Marston

2005

Biochemistry (Moscow)

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This review is devoted to critical analysis of data concerning the structure and functions of small heat shock proteins with apparent molecular mass 20 kD (Hsp20). We describe the structure of Hsp20, its phosphorylation by different protein kinases, interaction of Hsp20 with other small heat shock proteins, and chaperone activity of Hsp20. The distribution of Hsp20 in different animal tissues and the factors affecting expression of Hsp20 are also described. Data on the possible involvement of Hsp20 in regulation of platelet aggregation and glucose transport are presented and analyzed. Special attention is paid to literature data describing probable regulatory effect of Hsp20 on contraction of smooth muscle. Two hypotheses postulating direct effect of Hsp20 on actomyosin interaction or its effect on cytoskeleton are compared and analyzed. The most recent data on the effect of Hsp20 on apoptosis and contractile activity of cardiomyocytes are also presented.

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supporting

confidence: 89%

Structure, Properties, and Probable Physiological Role of Small Heat Shock Protein with Molecular Mass 20 kD (Hsp20, HspB6)

Gusev

Bukach

Marston

2005

Biochemistry (Moscow)

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“…10 Stable overexpression of Hsp20 in Chinese hamster ovary (CHO) cells resulted in enhanced survival, after a heat shock, similar to ␣B-crystallin. 12 Furthermore, heat pretreatment of swine carotid artery was associated with increased Hsp20 levels and its phosphorylation at Ser16. 13 The significance of upregulation of Hsp20 is unclear, but it could represent a cytoprotective response to stress.…”

mentioning

confidence: 98%

Small Heat-Shock Protein Hsp20 Phosphorylation Inhibits β-Agonist-Induced Cardiac Apoptosis

Fan

Chu

Mitton

et al. 2004

Circulation Research

112

144

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Abstract-Activation of the sympathetic nervous system is a common compensatory feature in heart failure, but sustained ␤-adrenergic activation induces cardiomyocyte death, leading to cardiac remodeling and dysfunction. In mouse cardiomyocytes, we recently reported that prolonged exposure to ␤-agonists is associated with transient increases in expression and phosphorylation of a small heat-shock protein, Hsp20. To determine the functional significance of Hsp20, we overexpressed this protein and its constitutively phosphorylated (S16D) or nonphosphorylated (S16A) mutant in adult rat cardiomyocytes. Hsp20 protected cardiomyocytes from apoptosis triggered by activation of the cAMP-PKA pathway, as indicated by decreases in the number of pyknotic nuclei, terminal deoxynucleotidyltransferase-mediated dUTP nick-end labeling, and DNA laddering, which were associated with inhibition of caspase-3 activity. These protective effects were further increased by the constitutively phosphorylated Hsp20 mutant (S16D), which conferred full protection from apoptosis. In contrast, the nonphosphorylatable mutant (S16A) exhibited no antiapoptotic properties. Immunostaining studies and immunoprecipitations with Hsp20 or actin antibodies demonstrated that Hsp20 translocated to cytoskeleton and associated with actin on isoproterenol stimulation. These findings suggest that Hsp20 and its phosphorylation at Ser16 may provide cardioprotection against ␤-agonist-induced apoptosis. Thus, Hsp20 may represent a novel therapeutic target in the treatment of heart failure.

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“…16 It provides resistance to heat treatment in Chinese hamster ovary cells, 17 and its expression levels are elevated on heat pretreatment of swine carotid artery, 18 insulin exposure of skeletal muscle, 19 and ␤-agonist stimulation of cardiomyocytes. 20 Interestingly, Hsp20 has been shown to regulate vasodilation 21 and suppress platelet aggregation.…”

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confidence: 99%

Novel Cardioprotective Role of a Small Heat-Shock Protein, Hsp20, Against Ischemia/Reperfusion Injury

et al. 2005

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Background-Heat-shock proteins (Hsps) have been shown to render cardioprotection from stress-induced injury; however, little is known about the role of another small heat-shock protein, Hsp20, which regulates activities of vasodilation and platelet aggregation, in cardioprotection against ischemia injury. We recently reported that increased expression of Hsp20 in cardiomyocytes was associated with improved contraction and protection against ␤-agonistinduced apoptosis. Methods and Results-To investigate whether overexpression of Hsp20 exerts protective effects in both ex vivo and in vivo ischemia/reperfusion (I/R) injury, we generated a transgenic (TG) mouse model with cardiac-specific overexpression of Hsp20 (10-fold). TG and wild-type (WT) hearts were then subjected to global no-flow I/R (45 minutes/120 minutes) using the Langendorff preparation. TG hearts exhibited improved recovery of contractile performance over the whole reperfusion period. This improvement was accompanied by a 2-fold decrease in lactate dehydrogenase released from the TG hearts. The extent of infarction and apoptotic cell death was also significantly decreased, which was associated with increased protein ratio of Bcl-2/Bax and reduced caspase-3 activity in TG hearts. Furthermore, in vivo experiments of 30-minute myocardial ischemia, via coronary artery occlusion, followed by 24-hour reperfusion, showed that the infarct region-to-risk region ratio was 8.1Ϯ1.1% in TG hearts (nϭ7), compared with 19.5Ϯ2.1% in WT hearts (nϭ11, PϽ0.001). Conclusions-Our data demonstrate that increased Hsp20 expression in the heart protects against I/R injury, resulting in improved recovery of cardiac function and reduced infarction. Thus, Hsp20 may constitute a new therapeutic target for ischemic heart diseases.

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Rat Hsp20 Confers Thermoresistance in a Clonal Survival Assay, but Fails to Protect Coexpressed Luciferase in Chinese Hamster Ovary Cells

Cited by 23 publications

References 24 publications

Structure, Properties, and Probable Physiological Role of Small Heat Shock Protein with Molecular Mass 20 kD (Hsp20, HspB6)

Structure, Properties, and Probable Physiological Role of Small Heat Shock Protein with Molecular Mass 20 kD (Hsp20, HspB6)

Small Heat-Shock Protein Hsp20 Phosphorylation Inhibits β-Agonist-Induced Cardiac Apoptosis

Novel Cardioprotective Role of a Small Heat-Shock Protein, Hsp20, Against Ischemia/Reperfusion Injury

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