Abstract
Heat shock proteins (HSPs), highly conserved in all organisms, act as molecular chaperones activated by several stresses. The HSP70 class of stress-induced proteins is the most studied subtype in cardiovascular and inflammatory disease. Because of the high similarity between plant and mammalian HSP70, the aim of this work was to evaluate whether recombinant HSP70 of plant origin (r-AtHSP70) was able to protect rat cardiac and hepatic function under ischemic and sepsis conditions. We demonstrated for the first time that, in ex vivo isolated and perfused rat heart, exogenous r-AtHSP70 exerted direct negative inotropic and lusitropic effects via Akt/endothelial nitric oxide synthase pathway, induced post-conditioning cardioprotection via Reperfusion Injury Salvage Kinase and Survivor Activating Factor Enhancement pathways, and did not cause hepatic damage. In vivo administration of r-AtHSP70 protected both heart and liver against lipopolysaccharide-dependent sepsis, as revealed by the reduced plasma levels of interleukin-1β, tumour necrosis factor alpha, aspartate aminotransferase and alanine aminotransferase. These results suggest exogenous r-AtHSP70 as a molecular modulator able to protect myocardial function and to prevent cardiac and liver dysfunctions during inflammatory conditions.
Highlights
Heat shock proteins (HSPs) represent a family of highly conserved molecular chaperones, classified according to their molecular sizes, whose main function consists in preventing misfolding and aggregation of nascent polypeptides or facilitating protein folding in both eukaryotic and prokaryotic organisms [1, 2]
Transfection of pET27-AtHSP70 in BL21 cells resulted in the accumulation of recombinant protein
To evaluate the possibility of r-AtHSP70 to counteract E. coli LPS (SigmaAldrich) -induced sepsis, animals were divided in three groups: (i) treatment (i.p.) with a placebo of saline solution; (ii) treatment by a single dose (i.p.) of LPS (5 mg/kgbw); (iii) treatment with a single dose of LPS plus rAtHSP70 (5 mg/kgbw)
Summary
Heat shock proteins (HSPs) represent a family of highly conserved molecular chaperones, classified according to their molecular sizes, whose main function consists in preventing misfolding and aggregation of nascent polypeptides or facilitating protein folding in both eukaryotic and prokaryotic organisms [1, 2]. They protect proteins during exposure to stressful situations such as heat shock, which causes proteins unfolding [3, 4]. Journal of Cellular and Molecular Medicine published by John Wiley & Sons Ltd and Foundation for Cellular and Molecular Medicine
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