Different interactions of cardiac and skeletal muscle ryanodine receptors with FK-506 binding protein isoforms.

@article{Barg1997DifferentIO,
  title={Different interactions of cardiac and skeletal muscle ryanodine receptors with FK-506 binding protein isoforms.},
  author={Sascha Barg and Julio A. Copello and Sidney Fleischer},
  journal={The American journal of physiology},
  year={1997},
  volume={272 5 Pt 1},
  pages={C1726-33}
}
In the present study, we compare functional consequences of dissociation and reconstitution of binding proteins FKBP12 and FKBP12.6 with ryanodine receptors from cardiac (RyR2) and skeletal muscle (RyR1). The skeletal muscle RyR1 channel became activated on removal of endogenously bound FKBP12, consistent with previous reports. Both FKBP12 and FKBP12.6 rebind to FKBP-depleted RyR1 and restore its quiescent channel behavior by altering ligand sensitivity, as studied by single-channel recordings… CONTINUE READING

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