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Human FKBP1B Protein expressed in Wheat germ - ABIN1354118
Åström-Olsson, Li, Olofsson, Borén, Öhlin, Grip: Impact of hypoxia, simulated ischemia and reperfusion in HL-1 cells on the expression of FKBP12/FKBP12.6 and intracellular calcium dynamics. in Biochemical and biophysical research communications 2012
The heart contraction is controlled by the Ca2+-induced Ca2+ release between L-type Ca2+ channels and ryanodine receptors. RyRs became more sensitive to Ca2+ triggers without FKBP12.6, leading to ventricular arrthymias.
Calstabin2 as a key modulator of cardiac aging.
Sirolimus-FKBP12.6 impairs endothelial barrier function by activation of protein kinase C-alpha and downstream disruption of the p120-VE cadherin interaction in vascular endothelium.
genetic approaches confirm the role of FKBP12.6 in regulating cardiac ryanodine receptors
the impact of simulated ischemia and reperfusion on expression of the calcium handling proteins FKBP12 and FKBP12.6, and intracellular calcium dynamics was investigated.
Transcription factor CHF1/Hey2 regulates EC coupling and heart failure in mice through regulation of FKBP12.6.
Cardiac FKBP12.6 overexpression in the mouse blunts pressure overload-induced maladaptive left ventricular remodelling.
FKBP12.6 removal enhanced, whereas RyR2 gene deletion blocked the hypoxic increase in Ca(2+)(i) in pulmonary artery smooth muscle cells.
Characterize the kinetics of FKBP12/12.6 binding to RyR2 in ventricular myocytes and effects on calcium signaling.
FKBP12.6(-/-) mice displayed hyperinsulinemia, & resistance to high fat diet-induced hyperglycemia, suggesting that FKBP12.6 plays an important role in insulin secretion & blood glucose control.
modulates cardiac excitation-contraction coupling
During exercise, RyR2 phosphorylation by protein kinase A dissociates FKBP12.6 from the channel, increasing Ca(2+) release and cardiac contractility. FKBP12.6(-/-) mice showed exercise-induced arrhythmias.
important role of the FKBP12.6/RyR2 complex in stochastic (spontaneous) and receptor-mediated Ca2+ release in smooth muscle.
spontaneous, transient outward currents (STOCs) and spontaneous Ca(2+) sparks are altered in FKBP12.6 deficient myocytes relative to wild-type and RYR3 null cells
the loss of FKBP12.6 has no significant effect on the conduction and activation of RyR2 or the propensity for spontaneous Ca(2+) release and stress-induced ventricular arrhythmias
FKBP12.6 plays a role in glucose-induced insulin secretion downstream of ATP production, independently of ATP-sensitive K(+) channels, in pancreatic beta-cells.
The increased vulnerability to AF in FKBP12.6-/- mice substantiates the notion that defective SR Ca(2+) release caused by abnormal RyR2 and FKBP12.6 interactions may contribute to the initiation or maintenance of atrial fibrillation.
Dissociation of FKBP12.6 from the RYR2 complex does not play a significant role in beta-adrenergic-stimulated Ca(2+) release in heart cells, whereas this mechanism does underlie the action of cADPR.
Our FRET-based HTS detects RyR binding of accessory proteins calmodulin (CaM) or FKBP12.6...One compound increased FRET and inhibited RyR1, which was only significant at nM [Ca(2+)], and accentuated without CaM present.
Total chemical synthesis, refolding, and crystallographic structure of fully active immunophilin calstabin 2
results suggest that both FKBP12.6 and FKBP12 play critical roles in regulating RyR2 function by facilitating the termination of SOICR.
RyRs have been identified as important targets of FKBP12 and FKBP12.6, members of the immunophilin family
How phosphorylation of RyR affects channel activity and whether proteins such as the FK-506 binding proteins (FKBP12 and FKBP12.6) are involved in heart failure
These data corroborate other studies suggesting that mutations in FKBP12 and FKBP12.6 genes are not commonly related to cardiac diseases.
FKBP12.6-deficient mice with cardiac hypertrophy do not display exercise-induced arrhythmia and/or sudden cardiac death.
analysis of the ryanodine receptor FK506-binding protein subunit
localization of binding site to the NH2-terminal domain of the cardiac Ca2+ release channel
Data show that VTSIP- and ARVD2-associated point mutations influence positively and negatively, respectively, the binding of RyR2 to its gating protein FKBP12.6.
data demonstrate that defective regulation of ryanodine receptor 2 causes altered cellular phenotype via profound perturbations in intracellular calcium signaling and highlight a key modulatory role of FK506 binding protein 12.6
FKBP1B gene is involved in the genetic susceptibility to the AITDs development in the studied family.
novel interaction site for FKBP12.6 may be present at the RyR2 C terminus, proximal to the channel pore, a sterically appropriate location that would enable this protein to play a central role in the modulation of this critical ion channel
FKBP12.6 plays a critical role in Ca channel gating, the R2401H mutation can be expected to alter Ca-induced Ca release and E-C coupling resulting in CPVT.
Enhancing calstabin binding to ryanodine receptors improves cardiac and skeletal muscle function in heart failure.
the redox state of the RyR is intimately connected with FKBP binding affinity.
Data show that K201 abolished spontaneous calcium release in cardiac myocytes, and that treating ventricular myocytes with FK506 to dissociate FKBP12.6 from ryanodine receptor RyR2 did not affect the suppression of spontaneous Ca2+ release by K201.
Results describe abrupt changes in the expression of FKBP12.6, SERCA2a, PKA, and ECE on reperfusion against ischemia, which are responsible for the rapid occurrence of ventricular fibrillation, and their prevention by CPU86017.
Study determined the three-dimensional structure of rabbit RyR2 in complex with the regulatory protein FKBP12.6 in the closed state at 11.8 A resolution using cryo-electron microscopy and built an atomic model of RyR2.
phosphorylation and K201 acted similarly to change the conformation of RyR1/2 and regulate FKBP12/12.6 binding.
Stoichiometry of binding sites and FKBP exchange binding.
The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds the immunosuppressants FK506 and rapamycin. It is highly similar to the FK506-binding protein 1A. Its physiological role is thought to be in excitation-contraction coupling in cardiac muscle. There are two alternatively spliced transcript variants of this gene encoding different isoforms.
FK506 binding protein 12.6
, peptidyl-prolyl cis-trans isomerase FKBP1B
, FK506 binding protein 1B, 12.6 kDa
, 12.6 kDa FK506-binding protein
, 12.6 kDa FKBP
, FK506-binding protein 12.6
, FK506-binding protein 1B
, PPIase FKBP1B
, immunophilin FKBP12.6
, calstabin 2
, Immunophilin FKBP12.6
, PPIase 1B
, Rotamase 1B
, peptidyl-prolyl cis-trans isomerase 1B
, peptidyl-prolyl cis-trans isomerase; PPIase