Thyroid hormone downregulates the expression and function of sarcoplasmic reticulum-associated CaM kinase II in the rabbit heart

American Journal of Physiology. Heart and Circulatory Physiology
Mao JiangN Narayanan

Abstract

Phosphorylation of sarcoplasmic reticulum (SR) Ca2+-cycling proteins by a membrane-associated Ca2+/calmodulin-dependent protein kinase II (CaM kinase II) is a well-documented physiological mechanism for regulation of transmembrane Ca2+ fluxes and the cardiomyocyte contraction-relaxation cycle. The present study investigated the effects of L-thyroxine-induced hyperthyroidism on protein expression of SR CaM kinase II and its substrates, endogenous CaM kinase II-mediated SR protein phosphorylation, and SR Ca2+ pump function in the rabbit heart. Membrane vesicles enriched in junctional SR (JSR) or longitudinal SR (LSR) isolated from euthyroid and hyperthyroid rabbit hearts were utilized. Endogenous CaM kinase II-mediated phosphorylation of ryanodine receptor-Ca2+ release channel (RyR-CRC), Ca2+-ATPase, and phospholamban (PLN) was significantly lower (30-70%) in JSR and LSR vesicles from hyperthyroid than from euthyroid rabbit heart. Western immunoblotting analysis revealed significantly higher (approximately 40%) levels of sarco(endo)plasmic reticulum Ca2+-ATPase isoform 2 (SERCA2) in JSR, but not in LSR, from hyperthyroid than from euthyroid rabbit heart. Maximal velocity of Ca2+ uptake was significantly increased in JSR (130%) an...Continue Reading

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Citations

Sep 10, 2010·International Journal of Biological Sciences·Scott A HelmsJeanne Y Wei
Jul 13, 2012·Canadian Journal of Physiology and Pharmacology·Angel Zarain-HerzbergJorge Fragoso-Medina
Apr 2, 2014·Clinical and Experimental Pharmacology & Physiology·Brent J F Hill, Edwin Muldrew
Sep 9, 2011·IUBMB Life·Angel Zarain-HerzbergRafael Estrada-Avilés
Oct 25, 2017·PLoS Genetics·Shannon N RomanoDaniel A Gorelick

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