FKBP12.6 and cADPR regulation of Ca release in smooth muscle cells
نویسندگان
چکیده
Yong-Xiao Wang, Yun-Min Zheng, Qi-Bing Mei, Qinq-Song Wang, Mei Lin Collier, Sidney Fleischer, Hong-Bo Xin, and Michael I. Kotlikoff Center for Cardiovascular Sciences, Albany Medical College, Albany, New York 12208; Department of Animal Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104; Department of Biological Sciences, Vanderbilt University, Nashville, Tennessee 37235; and Department of Biomedical Sciences, Cornell University, Ithaca, New York 14853
منابع مشابه
Role of FKBP12.6 in cADPR-induced activation of reconstituted ryanodine receptors from arterial smooth muscle.
cADP ribose (cADPR) serves as second messenger to activate the ryanodine receptors (RyRs) of the sarcoplasmic reticulum (SR) and mobilize intracellular Ca(2+) in vascular smooth muscle cells. However, the mechanisms mediating the effect of cADPR remain unknown. The present study was designed to determine whether FK-506 binding protein 12.6 (FKBP12.6), an accessory protein of the RyRs, plays a r...
متن کاملCa(2+) release induced by cADP-ribose is mediated by FKBP12.6 proteins in mouse bladder smooth muscle.
We examined the role and molecular mechanism of cADPR action on Ca(2+) spark properties in mouse bladder smooth muscle. Dialysis of cADPR with patch pipettes increased frequency and amplitude of spontaneous transient out currents (STOCs) to 6.1+/-0.87 currents/min from 1.2+/-0.36 currents/min (control) and to 179.8+/-48.7pA from 36.4+/-22.6pA (control), respectively, in wildtype (WT) cells, and...
متن کاملFKBP12.6 and cADPR regulation of Ca2+ release in smooth muscle cells.
Intracellular Ca2+ release through ryanodine receptors (RyRs) plays important roles in smooth muscle excitation-contraction coupling, but the underlying regulatory mechanisms are poorly understood. Here we show that FK506 binding protein of 12.6 kDa (FKBP12.6) associates with and regulates type 2 RyRs (RyR2) in tracheal smooth muscle. FKBP12.6 binds to RyR2 but not other RyR or inositol 1,4,5-t...
متن کاملDissociation of FKBP12.6 from ryanodine receptor type 2 is regulated by cyclic ADP-ribose but not beta-adrenergic stimulation in mouse cardiomyocytes.
AIMS Beta-adrenergic augmentation of Ca(2+) sparks and cardiac contractility has been functionally linked to phosphorylation-dependent dissociation of FK506 binding protein 12.6 (FKBP12.6) regulatory proteins from ryanodine receptors subtype 2 (RYR2). We used FKBP12.6 null mice to test the extent to which the dissociation of FKBP12.6 affects Ca(2+) sparks and mediates the inotropic action of is...
متن کاملCyclic ADP-ribose increases Ca2+ removal in smooth muscle.
Ca2+ release via ryanodine receptors (RyRs) is vital in cell signalling and regulates diverse activities such as gene expression and excitation-contraction coupling. Cyclic ADP ribose (cADPR), a proposed modulator of RyR activity, releases Ca2+ from the intracellular store in sea urchin eggs but its mechanism of action in other cell types is controversial. In this study, caged cADPR was used to...
متن کاملDissociation of FKBP 12.6 from Ryanodine Receptor Type 2 Is Regulated by Cyclic ADP-ribose but not β-Adrenergic Stimulation in Mouse Cardiomyocytes
AIMS: β-adrenergic augmentation of Ca 2+ sparks and cardiac contractility has been functionally linked to phosphorylation–dependent dissociation of FK506 binding protein 12.6 (FKBP12.6) regulatory proteins from ryanodine receptors subtype 2 (RYR2). We used FKBP12.6 null mice to test the extent to which the dissociation of FKBP12.6 affects Ca 2+ sparks and mediates the inotropic action of isopro...
متن کامل