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Heat Shock Protein 70 Protects the Heart from IschemiaReperfusion Injury through Inhibition of p38 MAPK Signaling
Joint Authors
Meng, Xiao-wen
Peng, Ke
Ji, Fu-hai
Liu, Hua-yue
Song, Nan
Ma, Jiao
Liu, Hong
Wang, Hui
Song, Shao-yong
Chen, Qing-cai
Zhang, Juan
Source
Oxidative Medicine and Cellular Longevity
Issue
Vol. 2020, Issue 2020 (31 Dec. 2020), pp.1-19, 19 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2020-03-21
Country of Publication
Egypt
No. of Pages
19
Main Subjects
Abstract EN
Background.
Heat shock protein 70 (Hsp70) has been shown to exert cardioprotection.
Intracellular calcium ([Ca2+]i) overload induced by p38 mitogen-activated protein kinase (p38 MAPK) activation contributes to cardiac ischemia/reperfusion (I/R) injury.
However, whether Hsp70 interacts with p38 MAPK signaling is unclear.
Therefore, this study investigated the regulation of p38 MAPK by Hsp70 in I/R-induced cardiac injury.
Methods.
Neonatal rat cardiomyocytes were subjected to oxygen-glucose deprivation for 6 h followed by 2 h reoxygenation (OGD/R), and rats underwent left anterior artery ligation for 30 min followed by 30 min of reperfusion.
The p38 MAPK inhibitor (SB203580), Hsp70 inhibitor (Quercetin), and Hsp70 short hairpin RNA (shRNA) were used prior to OGD/R or I/R.
Cell viability, lactate dehydrogenase (LDH) release, serum cardiac troponin I (cTnI), [Ca2+]i levels, cell apoptosis, myocardial infarct size, mRNA level of IL-1β and IL-6, and protein expression of Hsp70, phosphorylated p38 MAPK (p-p38 MAPK), sarcoplasmic/endoplasmic reticulum Ca2+-ATPase2 (SERCA2), phosphorylated signal transducer and activator of transcription3 (p-STAT3), and cleaved caspase3 were assessed.
Results.
Pretreatment with a p38 MAPK inhibitor, SB203580, significantly attenuated OGD/R-induced cell injury or I/R-induced myocardial injury, as evidenced by improved cell viability and lower LDH release, resulted in lower serum cTnI and myocardial infarct size, alleviation of [Ca2+]i overload and cell apoptosis, inhibition of IL-1β and IL-6, and modulation of protein expressions of p-p38 MAPK, SERCA2, p-STAT3, and cleaved-caspase3.
Knockdown of Hsp70 by shRNA exacerbated OGD/R-induced cell injury, which was effectively abolished by SB203580.
Moreover, inhibition of Hsp70 by quercetin enhanced I/R-induced myocardial injury, while SB203580 pretreatment reversed the harmful effects caused by quercetin.
Conclusions.
Inhibition of Hsp70 aggravates [Ca2+]i overload, inflammation, and apoptosis through regulating p38 MAPK signaling during cardiac I/R injury, which may help provide novel insight into cardioprotective strategies.
American Psychological Association (APA)
Song, Nan& Ma, Jiao& Meng, Xiao-wen& Liu, Hong& Wang, Hui& Song, Shao-yong…[et al.]. 2020. Heat Shock Protein 70 Protects the Heart from IschemiaReperfusion Injury through Inhibition of p38 MAPK Signaling. Oxidative Medicine and Cellular Longevity،Vol. 2020, no. 2020, pp.1-19.
https://search.emarefa.net/detail/BIM-1204382
Modern Language Association (MLA)
Song, Nan…[et al.]. Heat Shock Protein 70 Protects the Heart from IschemiaReperfusion Injury through Inhibition of p38 MAPK Signaling. Oxidative Medicine and Cellular Longevity No. 2020 (2020), pp.1-19.
https://search.emarefa.net/detail/BIM-1204382
American Medical Association (AMA)
Song, Nan& Ma, Jiao& Meng, Xiao-wen& Liu, Hong& Wang, Hui& Song, Shao-yong…[et al.]. Heat Shock Protein 70 Protects the Heart from IschemiaReperfusion Injury through Inhibition of p38 MAPK Signaling. Oxidative Medicine and Cellular Longevity. 2020. Vol. 2020, no. 2020, pp.1-19.
https://search.emarefa.net/detail/BIM-1204382
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-1204382