<?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%">Arvanitis, DA</style></author><author><style face="normal" font="default" size="100%">Vafiadaki, E.</style></author><author><style face="normal" font="default" size="100%">Fan, G. C.</style></author><author><style face="normal" font="default" size="100%">Mitton, B. A.</style></author><author><style face="normal" font="default" size="100%">Gregory, K. N.</style></author><author><style face="normal" font="default" size="100%">Del Monte, F.</style></author><author><style face="normal" font="default" size="100%">Kontrogianni-Konstantopoulos, A.</style></author><author><style face="normal" font="default" size="100%">Sanoudou, D.</style></author><author><style face="normal" font="default" size="100%">Kranias, EG</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Histidine-rich Ca-binding protein interacts with sarcoplasmic reticulum Ca-ATPase</style></title><secondary-title><style face="normal" font="default" size="100%">Am J Physiol Heart Circ PhysiolAm J Physiol Heart Circ PhysiolAm J Physiol Heart Circ Physiol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">American journal of physiology. Heart and circulatory physiology</style></alt-title><short-title><style face="normal" font="default" size="100%">American journal of physiology. Heart and circulatory physiologyAmerican journal of physiology. Heart and circulatory physiology</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/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Calcium/pharmacology</style></keyword><keyword><style  face="normal" font="default" size="100%">Carrier Proteins/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Cells, Cultured</style></keyword><keyword><style  face="normal" font="default" size="100%">Dose-Response Relationship, Drug</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Intracellular Signaling Peptides and Proteins</style></keyword><keyword><style  face="normal" font="default" size="100%">Mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Muscle Proteins/metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Myocytes, Cardiac/cytology/*metabolism</style></keyword><keyword><style  face="normal" font="default" size="100%">Sarcoplasmic Reticulum Calcium-Transporting ATPases/*metabolism</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2007</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Sep</style></date></pub-dates></dates><number><style face="normal" font="default" size="100%">3</style></number><volume><style face="normal" font="default" size="100%">293</style></volume><pages><style face="normal" font="default" size="100%">H1581-9</style></pages><isbn><style face="normal" font="default" size="100%">0363-6135 (Print)0363-6135 (Linking)</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Depressed cardiac Ca cycling by the sarcoplasmic reticulum (SR) has been associated with attenuated contractility, which can progress to heart failure. The histidine-rich Ca-binding protein (HRC) is an SR component that binds to triadin and may affect Ca release through the ryanodine receptor. HRC overexpression in transgenic mouse hearts was associated with decreased rates of SR Ca uptake and delayed relaxation, which progressed to hypertrophy with aging. The present study shows that HRC may mediate part of its regulatory effects by binding directly to sarco(endo)plasmic reticulum Ca-ATPase type 2 (SERCA2) in cardiac muscle, which is confirmed by coimmunostaining observed under confocal microscopy. This interaction involves the histidine- and glutamic acid-rich domain of HRC (320-460 aa) and the part of the NH(2)-terminal cation transporter domain of SERCA2 (74-90 aa) that projects into the SR lumen. The SERCA2-binding domain is upstream from the triadin-binding region in human HRC (609-699 aa). Specific binding between HRC and SERCA was verified by coimmunoprecipitation and pull-down assays using human and mouse cardiac homogenates and by blot overlays using glutathione S-transferase and maltose-binding protein recombinant proteins. Importantly, increases in Ca concentration were associated with a significant reduction of HRC binding to SERCA2, whereas they had opposite effects on the HRC-triadin interaction in cardiac homogenates. Collectively, our data suggest that HRC may play a key role in the regulation of SR Ca cycling through its direct interactions with SERCA2 and triadin, mediating a fine cross talk between SR Ca uptake and release in the heart.</style></abstract><accession-num><style face="normal" font="default" size="100%">17526652</style></accession-num><notes><style face="normal" font="default" size="100%">Arvanitis, Demetrios AVafiadaki, ElizabethFan, Guo-ChangMitton, Bryan AGregory, Kimberly NDel Monte, FedericaKontrogianni-Konstantopoulos, AikateriniSanoudou, DespinaKranias, Evangelia GengHL-26057/HL/NHLBI NIH HHS/HL-64018/HL/NHLBI NIH HHS/HL-77101/HL/NHLBI NIH HHS/Research Support, N.I.H., ExtramuralResearch Support, Non-U.S. Gov't2007/05/29 09:00Am J Physiol Heart Circ Physiol. 2007 Sep;293(3):H1581-9. doi: 10.1152/ajpheart.00278.2007. Epub 2007 May 25.</style></notes><auth-address><style face="normal" font="default" size="100%">Molecular Biology Division, Center for Basic Research, Foundation for Biomedical Research of the Academy of Athens, Athens, Greece.</style></auth-address></record></records></xml>