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Arrhythmogenic properties of dismantling cadherin-mediated adhesion in murine hearts

Hongjun Zhu1, Hegui Wang, Xiwen Zhang

  • 1Department of Cardiology, the First Affiliated Hospital of Nanjing Medical University, Nanjing 210029, Jiangsu Province, China.

Journal of Biomedical Research
|April 5, 2013
PubMed
Abstract

Insights

Recombinant mouse aminopeptidase N (rmAPN) disrupts cardiac cell adhesion, leading to gap junction remodeling and increased risk of ventricular arrhythmias in mice. This suggests proteolytic enzymes may contribute to heart rhythm disorders.

Area of Science:

  • Cardiology
  • Molecular Biology
  • Biochemistry

Background:

  • Cadherin-mediated adhesion is crucial for cardiomyocyte integrity.
  • Proteolytic enzymes can disrupt cell-cell junctions.
  • Understanding these disruptions is key to addressing cardiac arrhythmias.

Purpose of the Study:

  • To investigate the arrhythmogenic effects of recombinant mouse aminopeptidase N (rmAPN).
  • To evaluate rmAPN's impact on cadherin-mediated adhesion in cardiac tissue.

Main Methods:

  • Incubation of rmAPN with cultured cardiomyocytes and infusion into adult mice.
  • Laser confocal microscopy to observe cell-cell connections.
  • Western blot and immunofluorescence to detect N-cadherin (N-cad) disruption.
  • Electrophysiological studies to assess arrhythmia risk.

Main Results:

  • rmAPN disrupted cell-cell contact in cardiomyocytes.
  • N-cadherin N-terminal loss and altered connexin 43 (Cx43) distribution were observed in rmAPN-infused mouse hearts.
  • Prolonged QRS duration and increased ventricular tachycardia inducibility were noted.

Conclusions:

  • rmAPN-induced N-cadherin disruption contributes to gap junction remodeling.
  • These changes may elicit arrhythmogenic effects.
  • Proteolytic enzyme-mediated disruption of adherent junctions may be significant in cardiac disease mechanisms.
Keywords:
N-cadherinadherence junctiongap junctionrecombinant mouse aminopeptidase Nventricular tachyarrhythmia

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