GEA3162, a nitric oxide-releasing agent, activates non-store-operated Ca2+ entry and inhibits store-operated Ca2+ entry pathways in neutrophils through thiol oxidation

Hsu, Mei‐Feng; Chen, Yu-San; Huang, Le-Tian; Tsao, Lo‐Ti; Kuo, Sheng‐Chu; Wang, Jih-Pyang

doi:10.1016/j.ejphar.2006.02.013

Cited by 9 publications

(6 citation statements)

References 44 publications

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“…Similar findings about the dual, concentration dependent effects of NO and NOdonors on SOCE were also reported in neutrophils and platelets in 2011 [204,205]. Bolotina and co-workers showed in two successive reports that NO inhibits SOCE in human platelets and proposed an accelerated SERCA pumping rate and consequently faster refilling of the ER-Ca 2+ stores as the molecular mechanism underlying this event [206,207].…”

Section: Reactive Nitrogen Species Effects On Soce and Crac/orai Chansupporting

confidence: 61%

“…Hawkins et al [188] studied redox mediated activation of STIM1 and found that oxidative stress leads to gluthationylation of STIM1's cysteine 56, triggering STIM1 oligomerization and punctae [171][172][173][174][175][176][177][180][181][182][183][184][185][186]189,[192][193][194][195][203][204][205][206][207][208][209][210][211][212][213][214][215][216][217][218] BSO, buthionine sulfoximine; DEANO, 2-(N,N-diethylamino)diazenolate-2-oxide; FRTL-5, fischer rat thyroid low serum 5%; GEA3162, 1,2,3,4,-oxatriazolium, 5-amino-3-(3,4-dichlorophenyl)-chloride; HEK, human embryonic kidney; IP3R, IP3 receptor; Jurkat, human leukemic T cell line; MEF, mouse embryonic fibroblasts; RBL, rat basophilic leukemia; RyR, ryanodine receptor; SH-SY5Y, human neuroblastoma cell line; SNP, sodium nitroprusside; tBHP, tert-butylhydroperoxide.…”

Section: Reactive Oxygen Species Effects On Soce and Crac/orai Channelsmentioning

confidence: 99%

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Redox regulation of calcium ion channels: Chemical and physiological aspects

et al. 2011

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a b s t r a c tReactive oxygen species (ROS) are increasingly recognized as second messengers in many cellular processes. While high concentrations of oxidants damage proteins, lipids and DNA, ultimately resulting in cell death, selective and reversible oxidation of key residues in proteins is a physiological mechanism that can transiently alter their activity and function. Defects in ROS producing enzymes cause disturbed immune response and disease.Changes in the intracellular free Ca 2+ concentration are key triggers for diverse cellular functions. Ca 2+ homeostasis thus needs to be precisely tuned by channels, pumps, transporters and cellular buffering systems. Alterations of these key regulatory proteins by reversible or irreversible oxidation alter the physiological outcome following cell stimulation. It is therefore necessary to understand which proteins are regulated and if this regulation is relevant in a physiological-and/or pathophysiological context. Because ROS are inherently difficult to identify and to measure, we first review basic oxygen redox chemistry and methods of ROS detection with special emphasis on electron paramagnetic resonance (EPR) spectroscopy. We then focus on the present knowledge of redox regulation of Ca 2+ permeable ion channels such as voltage-gated (CaV) Ca 2+ channels, transient receptor potential (TRP) channels and Orai channels.© 2011 Elsevier Ltd. All rights reserved. Basic redox chemistry of oxygenMany chemical processes are linked to the exchange of electrons between two or more molecular entities. The transfer of one (or more) electron(s) is associated with oxidation (loss of electron) and reduction (gain of electron) of the components. Such reactions are also known as redox reactions. The processes of reactive oxygen species (ROS) formation and elimination are exclusively of redox nature.Molecular oxygen is the precursor of all ROS. It contains two unpaired electrons in separate (antibonding) orbitals in its outer electron sphere and is thus, by definition, a radical. Radicals have at least one unpaired electron in their orbital system and usually show high reactivity; transition metal ions also may have unpaired electrons, but are not called radicals. Although having radical character, molecular oxygen is chemically rather inert (luckily!), because high * Corresponding authors at: Institut für Biophysik, Gebäude 58, Universität des Saarlandes, D-66421 Homburg/Saar, Germany. Tel.: +49 6841 1626453; fax: +49 6841 1626060.E-mail addresses: ivan.bogeski@uks.eu (I. Bogeski), barbara.niemeyer@uks.eu (B.A. Niemeyer).

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Section: Reactive Nitrogen Species Effects On Soce and Crac/orai Chansupporting

confidence: 61%

Section: Reactive Oxygen Species Effects On Soce and Crac/orai Channelsmentioning

confidence: 99%

Redox regulation of calcium ion channels: Chemical and physiological aspects

et al. 2011

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“…Interestingly, Wang et al showed that NO donor GEA3162 and NEM could induce calcium entry through a non-store-operated mechanism via direct sulfhydryl modification in resting rat neutrophils which were performed in suspension [22]–[24]. Gill et al also reported that NO donors and NEM caused non-store-operated calcium entry through sulfhydryl modification in DDT 1 MF-2 cells [25]–[27].…”

Section: Discussionmentioning

confidence: 99%

“…For resting rat neutrophils, Wang et al demonstrated that alkylating agent NEM and NO donor 5-amino-3-(3,4-dichlorophenyl)-1,2,3,4-oxatriazolium (GEA3162) just stimulated calcium entry through a non-store-operated pathway via direct sulfhydryl modification [22]–[24]. In addition, Gill et al reported that NEM and membrane-permeant NO donors could activate non-store-operated calcium entry through sulfhydryl modification in DDT 1 MF-2 cells [25]–[27].…”

Section: Introductionmentioning

confidence: 99%

Sulfhydryl Modification Induces Calcium Entry through IP3-Sensitive Store-Operated Pathway in Activation-Dependent Human Neutrophils

et al. 2011

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As the first line of host defense, neutrophils are stimulated by pro-inflammatory cytokines from resting state, facilitating the execution of immunomodulatory functions in activation state. Sulfhydryl modification has a regulatory role in a wide variety of physiological functions through mediation of signaling transductions in various cell types. Recent research suggested that two kinds of sulfhydryl modification, S-nitrosylation by exogenous nitric oxide (NO) and alkylation by N-ethylmaleimide (NEM), could induce calcium entry through a non-store-operated pathway in resting rat neutrophils and DDT1MF-2 cells, while in active human neutrophils a different process has been observed by us. In the present work, data showed that NEM induced a sharp rising of cytosolic calcium concentration ([Ca2+]c) without external calcium, followed by a second [Ca2+]c increase with readdition of external calcium in phorbol 12-myristate 13-acetate (PMA)-activated human neutrophils. Meanwhile, addition of external calcium did not cause [Ca2+]c change of Ca2+-free PMA-activated neutrophils before application of NEM. These data indicated that NEM could induce believable store-operated calcium entry (SOCE) in PMA-activated neutrophils. Besides, we found that sodium nitroprusside (SNP), a donor of exogenous NO, resulted in believable SOCE in PMA-activated human neutrophils via S-nitrosylation modification. In contrast, NEM and SNP have no effect on [Ca2+]c of resting neutrophils which were performed in suspension. Furthermore, 2-Aminoethoxydiphenyl borate, a reliable blocker of SOCE and an inhibitor of inositol 1,4,5-trisphosphate (IP3) receptor, evidently abolished SNP and NEM-induced calcium entry at 75 µM, while preventing calcium release in a concentration-dependent manner. Considered together, these results demonstrated that NEM and SNP induced calcium entry through an IP3-sensitive store-operated pathway of human neutrophils via sulfhydryl modification in a PMA-induced activation-dependent manner.

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“…The dual effects of GEA3162 on the regulation of the external Ca 2+ entry are mainly through the thiol modification of target protein(s) residing on the outside of the plasma membrane [72].…”

Section: 234-oxatriazolium-5-aminidesmentioning

confidence: 99%