Prothymosin alpha protects cardiomyocytes against ischemia-induced apoptosis via preservation of Akt activation View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2013-10

AUTHORS

Alessandro Cannavo, Giuseppe Rengo, Daniela Liccardo, Gianluigi Pironti, Maria Cecilia Scimia, Laura Scudiero, Claudio De Lucia, Marco Ferrone, Dario Leosco, Nicola Zambrano, Walter J. Koch, Bruno Trimarco, Giovanni Esposito

ABSTRACT

The human prothymosin alpha (PTα) gene encodes a 12.5 kDa highly acidic nuclear protein that is widely expressed in mammalian tissues including the heart and importantly, is detectable also in blood serum. During apoptosis or necrosis, PTα changes its nuclear localization and is able to exert an important cytoprotective effect. Since the role of PTα in the heart has never been evaluated, the aim of the present study was to investigate the effects of PTα on cardiomyocytes during ischemic injury. Our data show that seven after myocardial infarction (MI), PTα expression levels are significantly increased both in blood serum and in cardiac tissue, and notably we observe that PTα translocates from the nuclei to cytoplasm and plasma membrane of cardiomyocytes following MI. Furthermore, in vitro experiments in cardiomyocytes, confirm that after 6 h of simulated ischemia (SI), PTα protein levels are upregulated compared to normoxic cells. Importantly, treatment of cardiomyocytes with a recombinant PTα (rPTα), during SI results in a significant decrease in the apoptotic response and in a robust increase in cell survival. Moreover, these effects are accompanied to a significant preservation of the activated levels of the anti-apoptotic serine-threonine kinase Akt. Consistent with our in vitro observation, rPTα-treated MI mice exhibit a strong reduction in infarct size at 24 h, compared to the MI control group and at the molecular level, PTα treatment induces activation of Akt. The present study provides for the first time the demonstration that PTα offers cardioprotection against ischemic injury by an Akt-dependent mechanism. More... »

PAGES

1252-1261

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10495-013-0876-9

DOI

http://dx.doi.org/10.1007/s10495-013-0876-9

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1036945973

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/23857453


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