scholarly journals Heat Shock Proteins and Mitogen-activated Protein Kinases in Steatotic Livers Undergoing Ischemia-Reperfusion: Some Answers

2006 ◽  
Vol 168 (5) ◽  
pp. 1474-1485 ◽  
Author(s):  
Marta Massip-Salcedo ◽  
Araní Casillas-Ramirez ◽  
Rosah Franco-Gou ◽  
Ramón Bartrons ◽  
Ismail Ben Mosbah ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Protein Kinases ◽  
Ischemia Reperfusion ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein ◽  
Shock Proteins

Lipid Peroxidation Activates Mitogen-Activated Protein Kinases in Testicular Ischemia-Reperfusion Injury

2006 ◽  
Vol 176 (4) ◽  
pp. 1666-1672 ◽  
Author(s):  
Pietro Antonuccio ◽  
Letteria Minutoli ◽  
Carmelo Romeo ◽  
Piero Antonio Nicòtina ◽  
Alessandra Bitto ◽  
...  
Keyword(s):  
Lipid Peroxidation ◽  
Reperfusion Injury ◽  
Protein Kinases ◽  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein ◽  
Testicular Ischemia

Short-term exercise training can improve myocardial tolerance to I/R without elevation in heat shock proteins

2001 ◽  
Vol 281 (3) ◽  
pp. H1346-H1352 ◽  
Author(s):  
Karyn L. Hamilton ◽  
Scott K. Powers ◽  
Takao Sugiura ◽  
Sunjoo Kim ◽  
Shannon Lennon ◽  
...  
Keyword(s):  
Lipid Peroxidation ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Ischemia Reperfusion ◽  
Left Ventricular ◽  
Antioxidant Defenses ◽  
Control Group ◽  
Shock Proteins ◽  
Mnsod Activity ◽  
Over Time

We examined the effects of 3 days of exercise in a cold environment on the expression of left ventricular (LV) heat shock proteins (HSPs) and contractile performance during in vivo ischemia-reperfusion (I/R). Sprague-Dawley rats were divided into the following three groups ( n = 12/group): 1) control, 2) exercise (60 min/day) at 4°C (E-Cold), and 3) exercise (60 min/day) at 25°C (E-Warm). Left anterior descending coronary occlusion was maintained for 20 min, followed by 30 min of reperfusion. Compared with the control group, both the E-Cold and E-Warm groups maintained higher ( P < 0.05) LV developed pressure, first derivative of pressure development over time (+dP/d t), and pressure relaxation over time (−dP/d t) throughout I/R. Relative levels of HSP90, HSP72, and HSP40 were higher ( P < 0.05) in E-Warm animals compared with both control and E-Cold. HSP10, HSP60, and HSP73 did not differ between groups. Exercise increased manganese superoxide dismutase (MnSOD) activity in both E-Warm and E-Cold hearts ( P < 0.05). Protection against I/R-induced lipid peroxidation in the LV paralleled the increase in MnSOD activity whereas lower levels of lipid peroxidation were observed in both E-Warm and E-Cold groups compared with control. We conclude that exercise-induced myocardial protection against a moderate duration I/R insult is not dependent on increases in myocardial HSPs. We postulate that exercise-associated cardioprotection may depend, in part, on increases in myocardial antioxidant defenses.

Abstract 340: Heat Shock Proteins HSP90 and HSP70 Mediate Opioid- and GSK3β-induced Cardioprotection

2014 ◽  
Vol 115 (suppl_1) ◽  
Author(s):  
Sarah K Jimenez ◽  
Bryce A Small ◽  
Anna K Hsu ◽  
Garrett J Gross ◽  
Eric R Gross
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Infarct Size ◽  
Glycogen Synthase ◽  
Ischemia Reperfusion ◽  
Myocardial Salvage ◽  
Sequence Motif ◽  
Protein Partners ◽  
Gsk 3Β ◽  
Shock Proteins

Previously, opioids were established to reduce myocardial injury in an ischemic preconditioning (IPC)-like manner, involving a central and downstream role of glycogen synthase kinase-3 beta (GSK-3β) inhibition. However, the mechanism of GSK-3β inhibition mediating cardioprotection and the protein partners involved has not been fully elucidated. Hence, we used a non-biased sequence scan of the proteome to determine potential GSK-3β protein partners and tested whether two candidate proteins, heat shock proteins (HSP) 70 and 90, are involved in the mechanism of opioid-induced cardioprotection. A non-biased BLAST search was performed for putative GSK-3β target substrates, based upon the sequence motif S/T-X-X-X-S/T. Approximately 700 proteins were identified to have this moiety, including many of the HSP protein class, including HSP70 and HSP90. To determine whether HSP70 or HSP90 are indeed important in opioid-induced cardioprotection, rats were subjected to an in vivo myocardial ischemia-reperfusion protocol consisting of 30 minutes of ischemia and 2 hours of reperfusion of the left anterior descending coronary artery followed by infarct size assessment. Either morphine (0.3mg/kg) or inhibition of GSK-3β using SB216763 (0.6mg/kg), reduced infarct size compared to control (42.21±1*% and 41.09±2*%, respectively versus control 60.38±1.2, *P<0.01). Inhibition of HSP70 using desoxysperguanalin (DSG), or HSP90 using radicicol (RAD), abrogated morphine-induced protection (56.09±2 and 58.64±1, respectively). Either DSG or RAD partially inhibited protection in the presence of GSK-3β (47.28±1.071 and 49.88±3.09). Our results suggest that morphine-induced cardioprotection occurs by a HSP70 and HSP90- dependent mechanism, with this HSP machinery partially required for GSK3β-inhibition-induced cardioprotection. Further understanding of this mechanism is important, considering many agents targeting HSP are currently in development as novel cancer treatments, which may have detrimental effects on the myocardial salvage mediated by opioids or by GSK3β-inhibition.

scholarly journals Mitogen Activated Protein Kinases in Steatotic and Non-Steatotic Livers Submitted to Ischemia-Reperfusion

2019 ◽  
Vol 20 (7) ◽  
pp. 1785 ◽  
Author(s):  
Jiménez-Castro ◽  
Cornide-Petronio ◽  
Gracia-Sancho ◽  
Casillas-Ramírez ◽  
Peralta
Keyword(s):  
Risk Factor ◽  
Clinical Practice ◽  
Protein Kinases ◽  
Hepatic Steatosis ◽  
Ischemic Preconditioning ◽  
Liver Surgery ◽  
Clinical Studies ◽  
Ischemia Reperfusion ◽  
Mitogen Activated Protein Kinases ◽  
Mitogen Activated Protein

: We analyzed the participation of mitogen-activated protein kinases (MAPKs), namely p38, JNK and ERK 1/2 in steatotic and non-steatotic livers undergoing ischemia-reperfusion (I-R), an unresolved problem in clinical practice. Hepatic steatosis is a major risk factor in liver surgery because these types of liver tolerate poorly to I-R injury. Also, a further increase in the prevalence of steatosis in liver surgery is to be expected. The possible therapies based on MAPK regulation aimed at reducing hepatic I-R injury will be discussed. Moreover, we reviewed the relevance of MAPK in ischemic preconditioning (PC) and evaluated whether MAPK regulators could mimic its benefits. Clinical studies indicated that this surgical strategy could be appropriate for liver surgery in both steatotic and non-steatotic livers undergoing I-R. The data presented herein suggest that further investigations are required to elucidate more extensively the mechanisms by which these kinases work in hepatic I-R. Also, further researchers based in the development of drugs that regulate MAPKs selectively are required before such approaches can be translated into clinical liver surgery.

Protective role of TAT-HSP70 after myocardial I/R injury

2017 ◽  
Vol 5 (3) ◽  
pp. 279-284
Author(s):  
Martin A. Meenakshi ◽  
Erik G. Seth
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion ◽  
Protective Role ◽  
Inflammatory Mechanism ◽  
Myocardial Ischemia Reperfusion Injury ◽  
Myocardial Ischemia Reperfusion ◽  
Shock Proteins

Myocardial ischemia reperfusion injury I/R adversely affects cardiac function. Heat shock proteins (HSPs) are a highly conserved family of proteins with diverse functions expressed by all cells exposed to environmental stress including myocardila injury. We investigated release of small constitutive heat shock proteins (HSPs) from mouse myocardium and the effects of TAT-HSP70 after myocardial I/R via occluding the left coronary artery (LAD). The results support the hypothesis that elevated HSPs in myocardium after ischemia and reperfusion and contributes to the inflammatory mechanism of myocardial functional injury. Further investigation of the significance of HSPs accumulation to the evolution of myocardial injury.

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