scholarly journals Over-expression of FK506-binding protein FKBP12.6 alters excitation-contraction coupling in adult rabbit cardiomyocytes

2004 ◽  
Vol 556 (3) ◽  
pp. 919-934 ◽  
Author(s):  
C. M. Loughrey ◽  
T. Seidler ◽  
S. L. W. Miller ◽  
J. Prestle ◽  
K. E. MacEachern ◽  
...  
Keyword(s):  
Binding Protein ◽  
Adult Rabbit ◽  
Excitation Contraction Coupling ◽  
Over Expression ◽  
Contraction Coupling ◽  
Fk506 Binding Protein

scholarly journals Modification of sarcoplasmic reticulum (SR) Ca2+ release by FK506 induces defective excitation-contraction coupling only when SR Ca2+ recycling is disturbed

2005 ◽  
Vol 83 (4) ◽  
pp. 357-366 ◽  
Author(s):  
Shu Yoshihara ◽  
Hiroshi Satoh ◽  
Masao Saotome ◽  
Hideki Katoh ◽  
Hajime Terada ◽  
...  
Keyword(s):  
Steady State ◽  
Sarcoplasmic Reticulum ◽  
Normal Condition ◽  
Binding Protein ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Cell Shortening ◽  
Fk506 Binding Protein ◽  
Ec Coupling ◽  
Protein Dissociation

This study examined whether the effects of FK506-binding protein dissociation from sarcoplasmic reticulum (SR) Ca2+ release channels on excitation-contraction (EC) coupling changed when SR Ca2+ reuptake and (or) the trans-sarcolemmal Ca2+ extrusion were altered. The steady-state twitch Ca2+ transient (CaT), cell shortening, post-rest caffeine-induced CaT, and Ca2+ sparks were measured in rat ventricular myocytes using laser-scanning confocal microscopy. In the normal condition, 50 µmol FK506/L significantly increased steady-state CaT, cell shortening, and post-rest caffeine-induced CaT. When the cells were solely perfused with thapsigargin, FK506 did not reduce any of the states, but when low [Ca2+]0 (0.1 mmol/L) was perfused additionally, FK506 reduced CaT and cell shortening, and accelerated the reduction of post-rest caffeine-induced CaT. FK506 significantly increased Ca2+ spark frequency in the normal condition, whereas it mainly prolonged duration of individual Ca2+ sparks under the combination of thapsigargin and low [Ca2+]0 perfusion. Modification of SR Ca2+ release by FK506 impaired EC coupling only when released Ca2+ could not be taken back into the SR and was readily extruded to the extracellular space. Our findings could partly explain the controversy regarding the contribution of FK506-binding protein dissociation to defective EC coupling.Key words: FK506, ryanodine receptor, sarcoplasmic reticulum Ca2+-ATPase, Na+/Ca2+ exchange, excitation-contraction coupling

scholarly journals Overexpression of FK-506–Binding Protein 12.0 Modulates Excitation–Contraction Coupling in Adult Rabbit Ventricular Cardiomyocytes

2007 ◽  
Vol 101 (10) ◽  
pp. 1020-1029 ◽  
Author(s):  
Tim Seidler ◽  
Christopher M. Loughrey ◽  
Darya Zibrova ◽  
Sarah Kettlewell ◽  
Nils Teucher ◽  
...  
Keyword(s):  
Binding Protein ◽  
Adult Rabbit ◽  
Fk 506 ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Ventricular Cardiomyocytes

Effects of Na+/Ca2+-exchanger Overexpression on Excitation–contraction Coupling in Adult Rabbit Ventricular Myocytes

2002 ◽  
Vol 34 (4) ◽  
pp. 389-400 ◽  
Author(s):  
Hardeep K. Ranu ◽  
Cesare M.N. Terracciano ◽  
Kerry Davia ◽  
Elena Bernobich ◽  
Babar Chaudhri ◽  
...  
Keyword(s):  
Ventricular Myocytes ◽  
Adult Rabbit ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Rabbit Ventricular Myocytes

scholarly journals CYTOCHEMICAL LOCALIZATION OF CHOLINESTERASE ACTIVITY IN ADULT RABBIT HEART

1971 ◽  
Vol 19 (6) ◽  
pp. 376-381 ◽  
Author(s):  
MARTIN HAGOPIAN ◽  
VIRGINIA M. TENNYSON
Keyword(s):  
Sarcoplasmic Reticulum ◽  
Papillary Muscle ◽  
Cholinesterase Activity ◽  
Acetylcholinesterase Activity ◽  
Rabbit Heart ◽  
Adult Rabbit ◽  
Cytochemical Localization ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
T System

The papillary muscle of the adult rabbit heart was studied by a modification of the Koelle-Friedenwald copper thiocholine technique for the localization of cholinesterase activity. Butyrylcholinesterase (BuChE), identified by its substrate and inhibitor specificity, is found mainly in the terminal sacs of the sarcoplasmic reticulum adjacent to the T system. The localization of the reaction product in this particular site suggests that BuChE may play a role in excitation-contraction coupling in the adult rabbit heart. The present findings are also discussed in comparison with our previous work on the localization of acetylcholinesterase activity in the embryonic rabbit heart.

scholarly journals Myosin-Binding Protein C Corrects an Intrinsic Non-Uniformity in Cardiac Excitation-Contraction Coupling

2015 ◽  
Vol 108 (2) ◽  
pp. 362a
Author(s):  
Michael J. Previs ◽  
Benjamin L. Prosser ◽  
Ji Young Mun ◽  
Samantha Beck Previs ◽  
James Gulick ◽  
...  
Keyword(s):  
Protein C ◽  
Binding Protein ◽  
Excitation Contraction Coupling ◽  
Contraction Coupling ◽  
Myosin Binding Protein ◽  
Myosin Binding Protein C ◽  
Myosin Binding ◽  
Cardiac Excitation

scholarly journals Effects of calsequestrin over-expression on excitation–contraction coupling in isolated rabbit cardiomyocytes

2005 ◽  
Vol 67 (4) ◽  
pp. 667-677 ◽  
Author(s):  
S MILLER ◽  
S CURRIE ◽  
C LOUGHREY ◽  
S KETTLEWELL ◽  
T SEIDLER ◽  
...  
Keyword(s):  
Excitation Contraction Coupling ◽  
Over Expression ◽  
Contraction Coupling
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