Echinochrome A regulates phosphorylation of phospholamban Ser16 and Thr17 suppressing cardiac SERCA2A Ca2+ reuptake View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2015-10

AUTHORS

Hyoung Kyu Kim, Jae Boum Youm, Seung Hun Jeong, Sung Ryul Lee, In-Sung Song, Tae Hee Ko, Julius Ryan Pronto, Kyung Soo Ko, Byoung Doo Rhee, Nari Kim, Bernd Nilius, Natalia P. Mischchenko, Sergey A. Fedoreyev, Valentin A. Stonik, Jin Han

ABSTRACT

Echinochrome A (Ech A), a marine bio-product isolated from sea urchin eggs, is known to have cardioprotective effects through its strong antioxidant and ATP-sparing capabilities. However, the effects of Ech A on cardiac excitation-contraction (E-C) are not known. In this study, we investigated the effects of Ech A on cardiac contractility and Ca(2+) handling in the rat heart. In ex vivo Langendorff hearts, Ech A (3 μM) decreased left ventricular developing pressure to 77.7 ± 6.5 % of basal level. In isolated ventricular myocytes, Ech A reduced the fractional cell shortening from 3.4 % at baseline to 2.1 %. Ech A increased both diastolic and peak systolic intracellular Ca(2+) ([Ca(2+)]i). However, the ratio of peak [Ca]i to resting [Ca]i was significantly decreased. Ech A did not affect the L-type Ca(2+) current. Inhibiting the Na(+)/Ca(2+) exchanger with either NiCl2 or SEA400 did not affect the Ech A-dependent changes in Ca(2+) handling. Our data demonstrate that treatment with Ech A results in a significant reduction in the phosphorylation of phospholamban at both serine 16 and threonine 17 leading to a significant inhibition of SR Ca(2+)-ATPase 2A (SERCA2A) and subsequent reduced Ca(2+) uptake into the intracellular Ca(2+) store. Taken together, our data show that Ech A negatively regulates cardiac contractility by inhibiting SERCA2A activity, which leads to a reduction in internal Ca(2+) stores. More... »

PAGES

2151-2163

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s00424-014-1648-2

DOI

http://dx.doi.org/10.1007/s00424-014-1648-2

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1045666440

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/25410495


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