<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Wang, H. S.</style></author><author><style face="normal" font="default" size="100%">Arvanitis, DA</style></author><author><style face="normal" font="default" size="100%">Dong, M.</style></author><author><style face="normal" font="default" size="100%">Niklewski, P. J.</style></author><author><style face="normal" font="default" size="100%">Zhao, W.</style></author><author><style face="normal" font="default" size="100%">Lam, C. K.</style></author><author><style face="normal" font="default" size="100%">Kranias, EG</style></author><author><style face="normal" font="default" size="100%">Sanoudou, D.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">SERCA2a superinhibition by human phospholamban triggers electrical and structural remodeling in mouse hearts</style></title><secondary-title><style face="normal" font="default" size="100%">Physiol GenomicsPhysiol GenomicsPhysiol Genomics</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Physiological genomics</style></alt-title><short-title><style face="normal" font="default" size="100%">Physiological genomicsPhysiological genomics</style></short-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Calcium-Binding Proteins/genetics/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Calcium/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Computational Biology</style></keyword><keyword><style  face="normal" font="default" size="100%">Electrophysiology</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Immunoblotting</style></keyword><keyword><style  face="normal" font="default" size="100%">In Vitro Techniques</style></keyword><keyword><style  face="normal" font="default" size="100%">inhibitors/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Male</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Models, Theoretical</style></keyword><keyword><style  face="normal" font="default" size="100%">Myocytes, Cardiac/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Oligonucleotide Array Sequence Analysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Sarcoplasmic Reticulum Calcium-Transporting ATPases/antagonists &amp;</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2011</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Apr 12</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">7</style></number><volume><style face="normal" font="default" size="100%">43</style></volume><pages><style face="normal" font="default" size="100%">357-64</style></pages><isbn><style face="normal" font="default" size="100%">1531-2267 (Electronic)1094-8341 (Linking)</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Phospholamban (PLN), the reversible inhibitor of the sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA2a), is a key regulator of myocyte Ca(2+) cycling with a significant role in heart failure. We previously showed that the single amino acid difference between human and mouse PLN results in increased inhibition of Ca(2+) cycling and cardiac remodeling and attenuated stress responses in transgenic mice expressing the human PLN (hPLN) in the null background. Here we dissect the molecular and electrophysiological processes triggered by the superinhibitory hPLN in the mouse. Using a multidisciplinary approach, we performed global gene expression analysis, electrophysiology, and mathematical simulations on hPLN mice. We identified significant changes in a series of Na(+) and K(+) homeostasis genes/proteins (including Kcnd2, Scn9a, Slc8a1) and ionic conductance (including L-type Ca(2+) current, Na(+)/Ca(2+) exchanger, transient outward K(+) current). Simulation analysis suggests that this electrical remodeling has a critical role in rescuing cardiac function by improving sarcoplasmic reticulum Ca(2+) load and overall Ca(2+) dynamics. Furthermore, multiple structural and transcription factor gene expression changes indicate an ongoing structural remodeling process, favoring hypertrophy and myogenesis while suppressing apoptosis and progression to heart failure. Our findings expand current understanding of the hPLN function and provide additional insights into the downstream implications of SERCA2a superinhibition in the mammalian heart.</style></abstract><accession-num><style face="normal" font="default" size="100%">21266500</style></accession-num><notes><style face="normal" font="default" size="100%">Wang, Hong-ShengArvanitis, Demetrios ADong, MinNiklewski, Paul JZhao, WenLam, Chi KeungKranias, Evangelia GSanoudou, DespinaengES-017263/ES/NIEHS NIH HHS/HL-084539/HL/NHLBI NIH HHS/HL-26057/HL/NHLBI NIH HHS/HL-64018/HL/NHLBI NIH HHS/Research Support, N.I.H., ExtramuralResearch Support, Non-U.S. Gov't2011/01/27 06:00Physiol Genomics. 2011 Apr 12;43(7):357-64. doi: 10.1152/physiolgenomics.00032.2010. Epub 2011 Jan 25.</style></notes><custom2><style face="normal" font="default" size="100%">3092331</style></custom2><auth-address><style face="normal" font="default" size="100%">Department of Pharmacology, College of Medicine, University of Cincinnati, Cincinnati, Ohio 45267-0575, USA. wanghs@uc.edu</style></auth-address></record></records></xml>