scholarly journals Intra-renal transfection of heat shock protein 90 alpha or beta (Hsp90  or Hsp90 ) protects against ischemia/reperfusion injury

2013 ◽  
Vol 29 (2) ◽  
pp. 301-312 ◽  
Author(s):  
J. Barrera-Chimal ◽  
R. Perez-Villalva ◽  
J. A. Ortega ◽  
N. Uribe ◽  
G. Gamba ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Reperfusion Injury ◽  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion ◽  
Heat Shock Protein 90

IS HEAT SHOCK PROTEIN A POTENTIAL PROTECTIVE MECHANISM AGAINST ISCHEMIA-REPERFUSION INJURY?

1999 ◽  
Vol 103 (1) ◽  
pp. 336-337 ◽  
Author(s):  
Sean Lille ◽  
Ching-Yuan Su ◽  
Michael Neumeister ◽  
Robert C. Russell ◽  
Chen-Ching Lai
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Reperfusion Injury ◽  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion ◽  
Protein A ◽  
Protective Mechanism

scholarly journals Heat Shock Protein 72 Enhances Manganese Superoxide Dismutase Activity During Myocardial Ischemia-Reperfusion Injury, Associated With Mitochondrial Protection and Apoptosis Reduction

Circulation ◽  
2002 ◽  
Vol 106 (12_suppl_1) ◽  
Author(s):  
Ken Suzuki ◽  
Bari Murtuza ◽  
Ivan A. Sammut ◽  
Najma Latif ◽  
Jay Jayakumar ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Reperfusion Injury ◽  
Manganese Superoxide Dismutase ◽  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion ◽  
Left Ventricular ◽  
Heat Shock Protein 72 ◽  
Manganese Superoxide

Background Heat shock protein 72 (HSP72) is known to provide myocardial protection against ischemia-reperfusion injury by its chaperoning function. Target molecules of this effect are presumed to include not only structural proteins but also other self-preservation proteins. The details, however, remain unknown. Manganese superoxide dismutase (Mn-SOD) is an enzyme that preserves mitochondria, a key organelle for cellular respiration, from reperfusion injury and limits mitochondria-related apoptosis. We hypothesized that Mn-SOD would play a role in HSP72-mediated cardioprotection. Methods and Results Rat hearts were transfected with human HSP72 by intra-coronary infusion of Hemagglutinating Virus of Japan-liposome, resulting in global myocardial overexpression of HSP72. After ischemia-reperfusion injury, cardiac function (left ventricular systolic pressure, maximum dP/dt, minimum dP/dt, and coronary flow) was improved in the HSP72-transfected hearts compared with control-transfected ones, corresponding with less leakage of creatine kinase and mitochondrial aspartate aminotransferase. Postischemic Mn-SOD content and activity in the HSP72-transfected hearts were enhanced in comparison with the controls (content: 96.9±4.1 versus 85.5±2.5% to the preischemic level, P =0.038; activity: 93.9±2.2 versus 82.2±3.7%, P =0.022), associated with improved mitochondrial respiratory function (postischemic percent respiratory control index; NAD + -linked: 81.3±3.8 versus 18.5±4.4%; FAD-linked: 71.8±5.5 versus 20.7±5.3%, P <0.001). In addition, incidence of postischemic cardiomyocyte apoptosis was attenuated in the HSP72-transfected hearts (4.0±1.1 versus 10.3±3.3%, P =0.036), correlating with an increased Bcl-2 level and reduced up-regulation of caspase-3. Conclusions These data suggest that the enhanced Mn-SOD activity during ischemia-reperfusion injury, which is associated with mitochondrial protection and apoptosis reduction, is a possible mechanism of HSP72-induced cardioprotection.

Gene transfer of heat shock protein 70 protects lung grafts from ischemia-reperfusion injury

1999 ◽  
Vol 67 (5) ◽  
pp. 1421-1427 ◽  
Author(s):  
Masafumi Hiratsuka ◽  
Bassem N Mora ◽  
Motoki Yano ◽  
Thalachallour Mohanakumar ◽  
G.Alexander Patterson
Keyword(s):  
Heat Shock ◽  
Gene Transfer ◽  
Heat Shock Protein ◽  
Reperfusion Injury ◽  
Heat Shock Protein 70 ◽  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion
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