scholarly journals Methods for studying store-operated calcium entry

Methods ◽  
2008 ◽  
Vol 46 (3) ◽  
pp. 204-212 ◽  
Author(s):  
Gary S. Bird ◽  
Wayne I. DeHaven ◽  
Jeremy T. Smyth ◽  
James W. Putney
Keyword(s):  
Calcium Entry ◽  
Store Operated Calcium Entry

scholarly journals A CRITICAL ROLE OF TRPC1-ORAI1-STIM1 MEDIATED STORE OPERATED CALCIUM ENTRY IN CARDIAC HYPERTROPHY

2015 ◽  
Vol 65 (10) ◽  
pp. A902
Author(s):  
Senthil Selvaraj ◽  
Brij Singh ◽  
Christian Bollensdorff ◽  
Jassim Al Suwaidi ◽  
Magdi Yacoub
Keyword(s):  
Cardiac Hypertrophy ◽  
Critical Role ◽  
Calcium Entry ◽  
Store Operated Calcium Entry

scholarly journals Synthesis and Characterization of Store-Operated Calcium Entry Inhibitors Active in the Submicromolar Range

2020 ◽  
Vol 21 (24) ◽  
pp. 9777
Author(s):  
Camille Le Guilcher ◽  
Tomas Luyten ◽  
Jan B. Parys ◽  
Mathieu Pucheault ◽  
Olivier Dellis
Keyword(s):  
Cell Activation ◽  
Interleukin 2 ◽  
Calcium Entry ◽  
Ip3 Receptors ◽  
Excitable Cells ◽  
Cellular Targets ◽  
Entry Inhibitors ◽  
The Past ◽  
Store Operated Calcium Entry

The store-operated calcium entry, better known as SOCE, forms the main Ca2+ influx pathway in non-excitable cells, especially in leukocytes, where it is required for cell activation and the immune response. During the past decades, several inhibitors were developed, but they lack specificity or efficacy. From the non-specific SOCE inhibitor 2-aminoethyl diphenylborinate (2-APB), we synthetized 16 new analogues by replacing/modifying the phenyl groups. Among them, our compound P11 showed the best inhibitory capacity with a Ki ≈ 75 nM. Furthermore, below 1 µM, P11 was devoid of any inhibitory activity on the two other main cellular targets of 2-APB, the IP3 receptors, and the SERCA pumps. Interestingly, Jurkat T cells secrete interleukin-2 under phytohemagglutinin stimulation but undergo cell death and stop IL-2 synthesis when stimulated in the presence of increasing P11 concentrations. Thus, P11 could represent the first member of a new and potent family of immunosuppressors.

Store-operated calcium entry compensates fast ER calcium loss in resting hippocampal neurons

Cell Calcium ◽  
2015 ◽  
Vol 58 (2) ◽  
pp. 147-159 ◽  
Author(s):  
Samira Samtleben ◽  
Britta Wachter ◽  
Robert Blum
Keyword(s):  
Hippocampal Neurons ◽  
Calcium Entry ◽  
Store Operated Calcium Entry ◽  
Calcium Loss ◽  
Er Calcium

scholarly journals Hydrogen peroxide attenuates store-operated calcium entry and enhances calcium extrusion in thyroid FRTL-5 cells

2000 ◽  
Vol 351 (1) ◽  
pp. 47 ◽  
Author(s):  
Kid TÖRNQUIST ◽  
Petri J. VAINIO ◽  
Sonja BJÖRKLUND ◽  
Alexey TITIEVSKY ◽  
Benoit DUGUÉ ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Calcium Entry ◽  
Store Operated Calcium Entry ◽  
Calcium Extrusion

scholarly journals Serine/threonine phosphatase 5 (PP5C/PPP5C) regulates the ISOC channel through a PP5C-FKBP51 axis

2017 ◽  
Vol 8 (1) ◽  
pp. 204589321775315 ◽  
Author(s):  
Caleb L. Hamilton ◽  
Kevin A. Abney ◽  
Audrey A. Vasauskas ◽  
Mikhail Alexeyev ◽  
Li Ni ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Endothelial Cell ◽  
Heat Shock Protein 90 ◽  
Calcium Entry ◽  
Hek293 Cells ◽  
Wide Field ◽  
Cell Fractionation ◽  
Gap Formation ◽  
Tetratricopeptide Repeats ◽  
Store Operated Calcium Entry

Pulmonary endothelial cells express a store-operated calcium entry current ( Isoc), which contributes to inter-endothelial cell gap formation. Isoc is regulated by a heterocomplex of proteins that includes the immunophilin FKBP51. FKBP51 inhibits Isoc by mechanisms that are not fully understood. In pulmonary artery endothelial cells (PAECs) we have shown that FKBP51 increases microtubule polymerization, an event that is critical for Isoc inhibition by FKBP51. In neurons, FKBP51 promotes microtubule stability through facilitation of tau dephosphorylation. However, FKBP51 does not possess phosphatase activity. Protein phosphatase 5 (PP5C/PPP5C) can dephosphorylate tau, and similar to FKBP51, PP5C possesses tetratricopeptide repeats (TPR) that mediate interaction with heat shock protein-90 (HSP90) chaperone/scaffolding complexes. We therefore tested whether PP5C contributes to FKBP51-mediated inhibition of Isoc. Both siRNA-mediated suppression of PP5C expression in PAECs and genetic disruption of PP5C in HEK293 cells attenuate FKBP51-mediated inhibition of Isoc. Reintroduction of catalytically competent, but not catalytically inactive PP5C, restored FKBP51-mediated inhibition of Isoc. PAEC cell fractionation studies identified both PP5C and the ISOC heterocomplex in the same membrane fractions. Further, PP5C co-precipitates with TRPC4, an essential subunit of ISOC channel. Finally, to determine if PP5C is required for FKBP51-mediated inhibition of calcium entry-induced inter-endothelial cell gap formation, we measured gap area by wide-field microscopy and performed biotin gap quantification assay and electric cell-substrate impedance sensing (ECIS®). Collectively, the data presented indicate that suppression of PP5C expression negates the protective effect of FKBP51. These observations identify PP5C as a novel member of the ISOC heterocomplex that is required for FKBP51-mediated inhibition of Isoc.

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