Alterations of protein expression of phospholamban, ZASP and plakoglobin in human atria in Accepted subgroups of seniors

Ulrich Gergs*, Winnie Mangold, Frank Langguth, Mechthild Hatzfeld, Steffen Hauptmann, Hasan Bushnaq, Andreas Simm, Rolf-Edgar Silber, Joachim Neumann

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

3 Citations (Web of Science)

Abstract

The mature mammalian myocardium contains composite junctions (areae compositae) that comprise proteins of adherens junctions as well as desmosomes. Mutations or deficiency of many of these proteins are linked to heart failure and/or arrhythmogenic cardiomyopathy in patients. We firstly wanted to address the question whether the expression of these proteins shows an age-dependent alteration in the atrium of the human heart. Right atrial biopsies, obtained from patients undergoing routine bypass surgery for coronary heart disease were subjected to immunohistology and/or western blotting for the plaque proteins plakoglobin (gamma-catenin) and plakophilin 2. Moreover, the Z-band protein cypher 1(Cypher/ZASP) and calcium handling proteins of the sarcoplasmic reticulum (SR) like phospholamban, SERCA and calsequestrin were analyzed. We noted expression of plakoglobin, plakophilin 2 and Cypher/ZASP in these atrial preparations on western blotting and/or immunohistochemistry. There was an increase of Cypher/ZASP expression with age. The present data extend our knowledge on the expression of anchoring proteins and SR regulatory proteins in the atrium of the human heart and indicate an age-dependent variation in protein expression. It is tempting to speculate that increased expression of Cypher/ZASP may contribute to mechanical changes in the aging human myocardium.

Original languageEnglish
Article number5610
Number of pages10
JournalScientific Reports
Volume9
DOIs
Publication statusPublished - 4 Apr 2019

Keywords

  • RIGHT-VENTRICULAR CARDIOMYOPATHY
  • SARCOPLASMIC-RETICULUM
  • DILATED CARDIOMYOPATHY
  • SEVERE FORM
  • PLAKOPHILIN-2
  • RAT
  • MUTATIONS
  • CALCIUM
  • CYPHER
  • PHOSPHORYLATION

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