%0 Journal Article %1 Gyoer_2007_1758 %A Gy�rke, Sandor %A Hagen, Brian M %A Terentyev, Dmitry %A Lederer, W. Jonathan %D 2007 %J J. Clin. Invest. %K Animals; Calcium Calsequestrin; Channel; Humans; Myocardium; Receptor Release Ryanodine Signaling; Tachycardia, Ventricular %N 7 %P 1758--1762 %R 10.1172/JCI32496 %T Chain-reaction Ca$^2+$ signaling in the heart. %U http://dx.doi.org/10.1172/JCI32496 %V 117 %X Mutations in Ca$^2+$ -handling proteins in the heart have been linked to exercise-induced sudden cardiac death. The best characterized of these have been mutations in the cardiac Ca$^2+$ release channel known as the ryanodine receptor type 2 (RyR2). RyR2 mutations cause "leaky" channels, resulting in diastolic Ca$^2+$ leak from the sarcoplasmic reticulum (SR) that can trigger fatal cardiac arrhythmias during stress. In this issue of the JCI, Song et al. show that mutations in the SR Ca$^2+$-binding protein calsequestrin 2 (CASQ2) in mice result not only in reduced CASQ2 expression but also in a surprising, compensatory elevation in expression of both the Ca$^2+$-binding protein calreticulin and RyR2, culminating in premature Ca$^2+$ release from cardiac myocytes and stress-induced arrhythmia (see the related article beginning on page 1814). In the context of these findings and other recent reports studying CASQ2 mutations, we discuss how CASQ2 influences the properties of Ca$^2+$-dependent regulation of RyR2 and how this contributes to cardiac arrhythmogenesis.

@article{Gyoer_2007_1758, abstract = {Mutations in {C}a$^{2+}$ -handling proteins in the heart have been linked to exercise-induced sudden cardiac death. The best characterized of these have been mutations in the cardiac {C}a$^{2+}$ release channel known as the ryanodine receptor type 2 (RyR2). RyR2 mutations cause "leaky" channels, resulting in diastolic {C}a$^{2+}$ leak from the sarcoplasmic reticulum (SR) that can trigger fatal cardiac arrhythmias during stress. In this issue of the JCI, Song et al. show that mutations in the SR {C}a$^{2+}$-binding protein calsequestrin 2 (CASQ2) in mice result not only in reduced CASQ2 expression but also in a surprising, compensatory elevation in expression of both the {C}a$^{2+}$-binding protein calreticulin and RyR2, culminating in premature {C}a$^{2+}$ release from cardiac myocytes and stress-induced arrhythmia (see the related article beginning on page 1814). In the context of these findings and other recent reports studying CASQ2 mutations, we discuss how CASQ2 influences the properties of {C}a$^{2+}$-dependent regulation of RyR2 and how this contributes to cardiac arrhythmogenesis.}, added-at = {2009-06-03T11:20:58.000+0200}, author = {Gy�rke, Sandor and Hagen, Brian M and Terentyev, Dmitry and Lederer, W. Jonathan}, biburl = {https://www.bibsonomy.org/bibtex/26d94b58af059094c0396cd010a0c25e8/hake}, description = {The whole bibliography file I use.}, doi = {10.1172/JCI32496}, file = {Gyoer_2007_1758.pdf:Gyoer_2007_1758.pdf:PDF}, institution = {Department of Physiology and Cell Biology and OSU Dorothy M Davis Heart and Lung Research Institute, The Ohio State University, Columbus, OH, USA.}, interhash = {c4f8a1e2dd37474227091363dedadb67}, intrahash = {6d94b58af059094c0396cd010a0c25e8}, journal = {J. Clin. Invest.}, keywords = {Animals; Calcium Calsequestrin; Channel; Humans; Myocardium; Receptor Release Ryanodine Signaling; Tachycardia, Ventricular}, month = Jul, number = 7, pages = {1758--1762}, pmid = {17607353}, timestamp = {2009-06-03T11:21:13.000+0200}, title = {Chain-reaction {C}a$^{2+}$ signaling in the heart.}, url = {http://dx.doi.org/10.1172/JCI32496}, volume = 117, year = 2007 }