Stimulation of intracellular Ca2+ elevation in neutrophils by thiol-oxidizing phenylarsine oxide

Wang, Jih-Pyang; Tsai, Jaw‐Ji; Chen, Yu-San; Hsu, Mei‐Feng

doi:10.1016/j.bcp.2005.01.013

Cited by 12 publications

(7 citation statements)

References 48 publications

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“…In addition to enzymes whose active sites contain redox-active dithiols, these redox-sensitive sites are found in a variety of proteins involved in the regulation of cellular processes. They include proteins that regulate neutrophil function (23,280) including NADPH neutrophil oxidase activity (73,151,161), platelet function (257), protein tyrosine phosphatase (45), and a variety of other proteins (110,212,216). Vicinal thiols are found on cell surfaces (71,80,244), with at least 10 to 12 vicinal thiol-containing proteins found on the surface of endothelial or fibrosarcoma cells (71).…”

Section: E Vicinal Thiolsmentioning

confidence: 99%

Redox Control of Platelet Function

Essex¹

2009

Antioxidants & Redox Signaling

102

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There has recently been a dramatic expansion in research in the area of redox biology with systems that utilize thiols to perform redox chemistry being central to redox control. Thiol-based reactions occur in proteins involved in platelet function, including extracellular platelet proteins. The alphaIIbbeta3 fibrinogen receptor contains free thiols that are required for the activation of this receptor to a fibrinogen-binding conformation. This process is under enzymatic control, with protein disulfide isomerase playing a central role in the activation of alphaIIbbeta3. Other integrins, such as the alpha2beta1 collagen receptor on platelets, are also regulated by protein disulfide isomerase and thiol metabolism. Low molecular weight thiols that are found in blood regulate these processes by converting redox sensitive disulfide bonds to thiols and by providing the appropriate redox potential for these reactions. Additional mechanisms of redox control of platelets involve nitric oxide that inhibits platelet responses, and reactive oxygen species that potentiate platelet thrombus formation. Specific nitrosative or oxidative modifications of thiol groups in platelets may modulate platelet function. Since many biologic processes are regulated by redox reactions that involve surface thiols, the extracellular redox state can have an important influence on health and disease status and may be a target for therapeutic intervention.

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Section: E Vicinal Thiolsmentioning

confidence: 99%

Redox Control of Platelet Function

Essex¹

2009

Antioxidants & Redox Signaling

102

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“…Although there are lots of research works on the effect of chemical compound on cytokine release of human neutrophils, such as catecholamine, thiol‐oxidizing phenylarsine oxide, lipopolysaccharide, etc., few researchers pay attention on the implanted foreign material effect to the neurtrophils function 14–16. Kamazawa et al17, 18 and Tamura et al19 examined the effect of Ti and other metals particles and ions on function and morphology of the human neutrophils in vitro ; the results showed that the cytotoxicity of Ti particles is size‐dependent, which is for the implants evaluation.…”

Section: Introductionmentioning

confidence: 99%

“…As we know, the Ca 2+ signals have been implicated in many cellular functions of neutrophils. The intracellular Ca 2+ rise stimulated by phenylarsine oxide in rat neutrophils was examined by Wang et al,16 whether the Ca ions released from the foreign materials affect the neutrophils function or not is unknown. In our study, the biodegraded nHA‐based materials were used to investigate this effect, although the high biocompatible materials were considered to slight reactions.…”

Section: Introductionmentioning

confidence: 99%

Human neutrophils reaction to the biodegraded nano‐hydroxyapatite/collagen and nano‐hydroxyapatite/collagen/poly(L‐lactic acid) composites

Liao

Tamura

Zhu

et al. 2005

J Biomedical Materials Res

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The impact of biodegraded nano-hydroxyapatite/collagen (nHAC) composite and nano-hydroxyapatite/collagen/poly(L-lactic acid) (nHAC/PLA) scaffold composite on neutrophils reaction was evaluated in vitro. Neutrophils were separated from human peripheral blood of healthy subjects. The nHAC and nHAC/PLA materials were immersed in the D-Hanks' Balanced Salt Solution (D-HBSS) for 1 day, 7 days and 2, 4, 8 weeks (37 degrees C) as testing solution, which mixed with the neutrophils for 1 h. Both of the nHAC and nHAC/PLA materials were shown the same cell survival rate as blank control, but the lactate dehydrogenase (LDH) and tumor necrosis factor alpha (TNF-alpha) released from the neutrophils were increased significantly after the 2 weeks in nHAC sample. The possible reason relied on the high concentration of calcium due to the quick biodegradation of the nHAC material. Before 2 weeks, the LDH value of nHAC/PLA is higher than that of nHAC sample that corresponded to the initial PLA degradation in vitro. This study provided the biocompatibility test of neutrophils other than common methods, such as osteoblastic cells for biomimetic materials. Moreover, it demonstrated the calcium concentration stimulating effect for cytokine release from neutrophils.

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“…Inhibitors were applied after platelets spreading on rRHO substrates and were treated at least 20 min for further image recording. Concentrations of reagents used: BSA 5%, fibrinogen 20 lg/ ml, rRHO 40 nM, thapsigargin (TG) 300 nM [35], [ethylenebis (oxyethylenenitrilo)] tetraacetic acid (EGTA) 1 mM, A3P5P 250 lM, wortmannin 100 nM, apyrase 1 unit/ml, U73122 3 lM [36], staurosporine 1 lM [37].…”

Section: Calcium Imagingmentioning

confidence: 99%

PI3-kinase is essential for ADP-stimulated integrin αIIbβ3-mediated platelet calcium oscillation, implications for P2Y receptor pathways in integrin αIIbβ3-initiated signaling cross-talks

Sun

Lo²,

Tsai

et al. 2005

J Biomed Sci

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Phosphatidylinositol 3-kinase (PI3K) pathway is important for platelet activation. Recent studies showed that PI3K and oscillative calcium could cross talk to each other and positively regulate integrin alpha (IIb)beta3-mediated outside-in signaling. However, the mechanism of this feedback regulation remains to be further characterized. Here we found that treatments of both PI3K inhibitor wortmannin and P2Y1 inhibitor A3P5P could inhibit granular secretion in platelets. Additionally, when RGD-substrate adherent platelets were treated with the ADP scavenger apyrase to deplete the granular-released ADP, their attachments in engaging with substrates became looser and the frequency of calcium oscillation decreased. Since it is known that ADP stimulates the PI3K and calcium signal primarily through P2Y12 and P2Y1 receptors respectively, our data indicated that integrin alpha(IIb)beta3 downstream PI3K and calcium activation might be not completely coupled to integrin associated signaling complex, but in part through feedback stimulation by granular released ADP. Our data indicates the important roles of PI3K and granular released ADP in coordinating the feedback regulations in integrin alpha(IIb)beta3-mediated platelet activation.

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Stimulation of intracellular Ca2+ elevation in neutrophils by thiol-oxidizing phenylarsine oxide

Cited by 12 publications

References 48 publications

Redox Control of Platelet Function

Redox Control of Platelet Function

Human neutrophils reaction to the biodegraded nano‐hydroxyapatite/collagen and nano‐hydroxyapatite/collagen/poly(L‐lactic acid) composites

PI3-kinase is essential for ADP-stimulated integrin αIIbβ3-mediated platelet calcium oscillation, implications for P2Y receptor pathways in integrin αIIbβ3-initiated signaling cross-talks

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