Unaltered ryanodine receptor protein levels in ischemic cardiomyopathy

Wolfgang Schillinger, Markus Meyer, Goro Kuwajima, Katsuhiko Mikoshiba, Hanjörg Just, Gerd Hasenfuss

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

Abstract

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 (1) 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.

Original languageEnglish (US)
Pages (from-to)297-302
Number of pages6
JournalMolecular and cellular biochemistry
Volume160-161
DOIs
StatePublished - Oct 19 1996
Externally publishedYes

Keywords

  • Calcium-ATPase
  • Calsequestrin
  • Heart failure
  • Human myocardium
  • Sarcoplasmic reticulum

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