caa a22 4500 477119565 CHVBK 20180405111632.0 cr unu---uuuuu 170330e19960301xx s 000 0 eng 10.1007/BF00240062 doi (NATIONALLICENCE)springer-10.1007/BF00240062 Unaltered ryanodine receptor protein levels in ischemic cardiomvopathy [Elektronische Daten] [Wolfgang Schillinger, Markus Meyer, Goro Kuwajima, Katsuhiko Mikoshiba, Hanjörg Just, Gerd Hasenfuss] Previous studies on sarcoplasmic reticulum calcium release channel (ryanodine receptor) demonstrated that protein levels are unchanged in myocardium from hearts with end-stage failing dilated cardiomyopathy. In ischemic cardiomyopathy, ryanodine receptor mRNA levels were shown to be decreased but no data on protein levels are available. Accordingly, protein levels of ryanodine receptor, calsequestrin, and sarcoplasmic reticulum calcium-ATPase (SR-Ca2+-ATPase) were measured by Western blot analysis in nonfailing human myocardium (n = 7) and in end-stage failing myocardium due to ischemic cardiomyopathy (n = 14). Protein levels of calsequestrin which is the major sarcoplasmic reticulum calcium storage protein were similar in nonfailing myocardium and in myocardium from end-stage failing hearts with ischemic cardiomyopathy. Ryanodine receptor protein levels, normalized to total protein or calsequestrin were also unchanged in ischemic cardiomyopathy. In contrast, protein levels of SR-Ca2+-ATPase normalized to total protein or calsequestrin were decreased by 31 and 30%, respectively (p < 0.05). The data indicate that (I) sarcoplasmic reticulum calcium uptake sites are decreased relative to the release sites in ischemic cardiomyopathy, and (2) alterations of sarcoplasmic proteins are similar in ischemic and dilated cardiomyopathy. Kluwer Academic Publishers, 1996 sarcoplasmic reticulum nationallicence calcium-ATPase nationallicence calsequestrin nationallicence human myocardium nationallicence heart failure nationallicence Schillinger Wolfgang Medizinische Klinik III, Universität Freiburg, Germany aut Meyer Markus Medizinische Klinik III, Universität Freiburg, Germany aut Kuwajima Goro Shionogi Institute for Medical Science, Osaka aut Mikoshiba Katsuhiko Dept. of Molecular Neurobiology, Institute of Medical Science, University of Tokyo, Japan aut Just Hanjörg Medizinische Klinik III, Universität Freiburg, Germany aut Hasenfuss Gerd Medizinische Klinik III, Universität Freiburg, Germany aut Molecular and Cellular Biochemistry Kluwer Academic Publishers; http://www.wkap.nl 160-161/1(1996-03-01), 297-302 0300-8177 160-161:1<297 1996 160-161 11010 https://doi.org/10.1007/BF00240062 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00240062 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Schillinger Wolfgang Medizinische Klinik III, Universität Freiburg, Germany aut NATIONALLICENCE 700 1- Meyer Markus Medizinische Klinik III, Universität Freiburg, Germany aut NATIONALLICENCE 700 1- Kuwajima Goro Shionogi Institute for Medical Science, Osaka aut NATIONALLICENCE 700 1- Mikoshiba Katsuhiko Dept. of Molecular Neurobiology, Institute of Medical Science, University of Tokyo, Japan aut NATIONALLICENCE 700 1- Just Hanjörg Medizinische Klinik III, Universität Freiburg, Germany aut NATIONALLICENCE 700 1- Hasenfuss Gerd Medizinische Klinik III, Universität Freiburg, Germany aut NATIONALLICENCE 773 0- Molecular and Cellular Biochemistry Kluwer Academic Publishers; http://www.wkap.nl 160-161/1(1996-03-01), 297-302 0300-8177 160-161:1<297 1996 160-161 11010 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer