Heat shock proteins: protective effect and potential therapeutic use (review).

1998 ◽  
Author(s):  
D S Latchman
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protective Effect ◽  
Therapeutic Use ◽  
Shock Proteins

Kinetics of induction and protective effect of heat-shock proteins after cardioplegic arrest

1996 ◽  
Vol 61 (5) ◽  
pp. 1407-1412 ◽  
Author(s):  
Mohamed Amrani ◽  
Joseph Corbett ◽  
Samuel Y. Boateng ◽  
Michael J. Dunn ◽  
Magdi H. Yacoub
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protective Effect ◽  
Cardioplegic Arrest ◽  
Shock Proteins ◽  
Kinetics Of

Role of heat shock proteins HSP70 and HSP32 in the protective effect of adaptation of cultured HT22 hippocampal cells to oxidative stress

2007 ◽  
Vol 144 (2) ◽  
pp. 174-177 ◽  
Author(s):  
I. P. Khomenko ◽  
L. Yu. Bakhtina ◽  
O. M. Zelenina ◽  
S. V. Kruglov ◽  
E. B. Manukhina ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protective Effect ◽  
Shock Proteins

Abstract 226: Human Cardiomyocytes Are Protected From Stress-induced Stiffening By Binding Of Small Heat Shock Proteins To Titin Spring Elements

2013 ◽  
Vol 113 (suppl_1) ◽  
Author(s):  
Sebastian Kotter ◽  
Andreas Unger ◽  
Nazha Hamdani ◽  
Wolfgang A Linke
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protective Effect ◽  
Small Heat Shock Proteins ◽  
Stress Conditions ◽  
Passive Stiffness ◽  
Human Cardiomyocytes ◽  
Αb Crystallin ◽  
Shock Proteins

Introduction: Small heat-shock proteins (sHSPs) generally participate in cellular protein quality-control mechanisms. They are abundant in cardiomyocytes where they bind under diverse stress conditions preferentially to myofilament proteins. The functional role of this association is unclear. Hypothesis: HSP27 and αB-crystallin bind to human cardiac titin spring elements and exert a protective effect on cardiomyocyte passive stiffness under stress conditions. Methods: Binding of sHSPs to recombinant human titin constructs was characterized by GST-pulldown assay and confirmed by immunofluorescence staining of human donor and failing (DCM) cardiomyocytes. Sedimentation-velocity centrifugation, photometric and chromatographic methods were used to test for titin aggregation and protection from it by sHSPs. Passive force was measured in isolated human cardiomyocytes or single myofibrils, in search for a possible protective effect of sHSPs on mechanical function. Results: HSP27 interacted with distinct domains of the human titin-spring region in vitro and in cardiomyocytes, and independent of the presence of actin filaments in the sarcomeres. The binding sites on the elastic titin segment resemble those for αB-crystallin and include proximal Ig-domains, the N2-B and N2-A regions, but not the PEVK-domain. In-vitro assays revealed a monomeric organization of these titin-spring elements; however, unfolded N2-A domain (mainly composed of Ig-domains) aggregated in pH-6.6 buffer but not in normal-pH buffer, whereas αB-crystallin protected from this effect. The intrinsically disordered N2-Bus titin domain did not aggregate. Single skinned human cardiomyocytes showed greatly increased passive stiffness when pre-stretched under acidic stress (pH 6.6), but αB-crystallin or HSP27 corrected the stiffening. In failing patient heart tissue, both HSP27 and αB-crystallin frequently associated with the elastic I-band region, in contrast to a cytosolic and Z-disk location of these sHSPs in donor heart. Conclusions: In cardiomyocytes sHSPs bind to mechanically active titin domains under stress conditions such as intracellular acidosis ( e.g. , ischemia), protecting the titin springs from aggregation and helping reverse diastolic stiffening.

scholarly journals Heat Shock Proteins and Protection Against Ischemic Injury

1999 ◽  
Vol 7 (1-2) ◽  
pp. 55-57 ◽  
Author(s):  
W. H. Dillmann
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Protective Effect ◽  
Cardiac Myocytes ◽  
Ischemic Injury ◽  
Transgenic Animals ◽  
Cell Types ◽  
Αb Crystallin ◽  
Shock Proteins

Heat shock proteins present a complex family of proteins exerting chaperone-like activities that are classified according to their molecular weight. We especially explored protective functions of inducible heat shock protein 70, the mitochondrial heat shock protein 60 and 10, and the small heat shock proteins HSP27 and αB-crystallin against ischemic, reoxygenation-mediated injury using transgenic animals and hearts under in vivo conditions and in isolated cardiac myocyte-derived cells using adenoviral vectors. We noted with great interest that differential protective effects are exerted by specific hsps. For example, alpha-B-crystallin and constitutive hsp70 markedly protect microtubular structure in cardiac myocytes from ischemia-induced injury. Inducible hsp70, hsp60 and hspl0 when coexpressed, and hsp27 and αB-crystallin have an overall protective effect against ischemic injury as determined by the release of enzymes like creatine kinase and LDH. We did not note inflammatory or immune responses elicited by the expression of hsps in transgenic animals and cardiac myocytes. The specific cell types in which hsps are expressed may contribute to the protective effect of hsps versus their inflammatory and immunogenic effects when expressed in other cell types. Infect. Dis. Obstet. Gynecol. 7:55–57, 1999.

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