<?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%">Vafiadaki, E.</style></author><author><style face="normal" font="default" size="100%">Papalouka, V.</style></author><author><style face="normal" font="default" size="100%">Arvanitis, DA</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%">The role of SERCA2a/PLN complex, Ca(2+) homeostasis, and anti-apoptotic proteins in determining cell fate</style></title><secondary-title><style face="normal" font="default" size="100%">Pflugers ArchPflugers ArchPflugers Arch</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Pflugers Archiv : European journal of physiology</style></alt-title><short-title><style face="normal" font="default" size="100%">Pflugers Archiv : European journal of physiologyPflugers Archiv : European journal of physiology</style></short-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">*Homeostasis</style></keyword><keyword><style  face="normal" font="default" size="100%">Adaptor Proteins, Signal Transducing</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals, Genetically Modified</style></keyword><keyword><style  face="normal" font="default" size="100%">Apoptosis Regulatory Proteins/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Calcium-Binding Proteins/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Calcium/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Heart Failure/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Multiprotein Complexes/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Myocytes, Cardiac/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Proteins/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Proto-Oncogene Proteins c-bcl-2/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Sarcoplasmic Reticulum Calcium-Transporting ATPases/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Sarcoplasmic Reticulum/metabolism</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2009</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Jan</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">457</style></volume><pages><style face="normal" font="default" size="100%">687-700</style></pages><isbn><style face="normal" font="default" size="100%">0031-6768 (Print)0031-6768 (Linking)</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Intracellular calcium is a major coordinator of numerous aspects of cellular physiology, including muscle contractility and cell survival. In cardiac muscle, aberrant Ca(2+) cycling has been implicated in a range of pathological conditions including cardiomyopathies and heart failure. The sarco(endo)plasmic reticulum Ca(2+) transport adenosine triphosphatase (SERCA2a) and its regulator phospholamban (PLN) have a central role in modulating Ca(2+) homeostasis and, therefore, cardiac function. Herein, we discuss the mechanisms through which SERCA2a and PLN control cardiomyocyte function in health and disease. Emphasis is placed on our newly identified PLN-binding partner HS-1-associated protein X-1 (HAX-1), which has an anti-apoptotic function and presents with numerous similarities to Bcl-2. Recent evidence indicates that proteins of the Bcl-2 family can influence ER Ca(2+) content, a critical determinant of cellular sensitivity to apoptosis. The discovery of the PLN/HAX-1 interaction therefore unveils an important new link between Ca(2+) homeostasis and cell survival, with significant therapeutic potential.</style></abstract><accession-num><style face="normal" font="default" size="100%">18415121</style></accession-num><notes><style face="normal" font="default" size="100%">Vafiadaki, ElizabethPapalouka, VasilikiArvanitis, Demetrios AKranias, Evangelia GSanoudou, DespinaengHL26057/HL/NHLBI NIH HHS/HL64018/HL/NHLBI NIH HHS/HL77101/HL/NHLBI NIH HHS/Research Support, N.I.H., ExtramuralResearch Support, Non-U.S. Gov'tReviewGermany2008/04/17 09:00Pflugers Arch. 2009 Jan;457(3):687-700. doi: 10.1007/s00424-008-0506-5. Epub 2008 Apr 16.</style></notes><auth-address><style face="normal" font="default" size="100%">Molecular Biology Division, Biomedical Research Foundation, Academy of Athens, Soranou Efesiou 4, Athens 115 27, Greece.</style></auth-address></record></records></xml>