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

Barg, Sebastian LU ; Copello, J A and Fleischer, S (1997) In American Journal of Physiology: Cell Physiology 272(5). p.1726-1733
Abstract
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 in planar lipid bilayers, and macroscopic behavior of the channels (ryanodine binding and net energized Ca2- uptake). By contrast, removal of FKBP12.6 from the cardiac RyR2 did not modulate the function of the channel using the same types of assays... (More)
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 in planar lipid bilayers, and macroscopic behavior of the channels (ryanodine binding and net energized Ca2- uptake). By contrast, removal of FKBP12.6 from the cardiac RyR2 did not modulate the function of the channel using the same types of assays as for RyR1. FKBP12 or FKBP12.6 had no effect on channel activity of FKBP12.6-depleted cardiac RyR2, although FKBP12.6 rebinds. Our studies reveal important differences between the two ryanodine receptor isoforms with respect to their functional interaction with FKBP12 and FKBP12.6. (Less)
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published
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in
American Journal of Physiology: Cell Physiology
volume
272
issue
5
pages
1726 - 1733
publisher
American Physiological Society
external identifiers
  • pmid:9176165
  • scopus:0030927915
ISSN
1522-1563
language
English
LU publication?
yes
id
a75a1e58-b743-48c0-a9e8-2627c428e477 (old id 1111605)
alternative location
http://ajpcell.physiology.org/cgi/reprint/272/5/C1726
date added to LUP
2016-04-01 16:30:28
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2020-09-16 15:47:40
@article{a75a1e58-b743-48c0-a9e8-2627c428e477,
  abstract     = {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 in planar lipid bilayers, and macroscopic behavior of the channels (ryanodine binding and net energized Ca2- uptake). By contrast, removal of FKBP12.6 from the cardiac RyR2 did not modulate the function of the channel using the same types of assays as for RyR1. FKBP12 or FKBP12.6 had no effect on channel activity of FKBP12.6-depleted cardiac RyR2, although FKBP12.6 rebinds. Our studies reveal important differences between the two ryanodine receptor isoforms with respect to their functional interaction with FKBP12 and FKBP12.6.},
  author       = {Barg, Sebastian and Copello, J A and Fleischer, S},
  issn         = {1522-1563},
  language     = {eng},
  number       = {5},
  pages        = {1726--1733},
  publisher    = {American Physiological Society},
  series       = {American Journal of Physiology: Cell Physiology},
  title        = {Different interactions of cardiac and skeletal muscle ryanodine receptors with FK-506 binding protein isoforms},
  url          = {http://ajpcell.physiology.org/cgi/reprint/272/5/C1726},
  volume       = {272},
  year         = {1997},
}