Protein kinase C-independent pathway for NADPH oxidase activation in guinea pig peritoneal polymorphonuclear leukocytes by cytochalasin D

Imagawa, Naoki; Nagasawa, Kohei; Nagai, Katsutoshi; Kawakami-Honda, Naoko; Fujimoto, Sadaki

doi:10.1016/j.abb.2005.04.003

Cited by 7 publications

(3 citation statements)

References 38 publications

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“…Protein kinase C has been shown to play a role in NADPH oxidase regulation in both phagocytes and nonphagocytes (8,20). Cytochalasin D-induced O 2 ·Ϫ production, however, is protein kinase C independent in phagocytes (22). Our findings in endothelial cells suggest that cytochalasin D does induce ROS/O 2 ·Ϫ production (Figs.…”

Section: Discussionsupporting

confidence: 56%

“…These novel observations may reveal the mechanisms of this mechanical-biochemical interaction, which has pathological implications for atherogenesis. The regulation of NADPH oxidase has been mostly studied in phagocytes where disruption of actin polymerization potentiates O 2 ·Ϫ production (22). Activation of phagocytic NADPH oxidase requires serine phosphorylation of the cytosolic p47 phox , p67 phox , and p40 phox components, assembly of the phosphorylated subunits with Rac2, and translocation to the phagosomes for association with cytochrome b 558 reductase, which consists of p22 phox and gp91 phox (Nox2) (45).…”

Section: Discussionmentioning

confidence: 99%

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Endothelial actin depolymerization mediates NADPH oxidase-superoxide production during flow reversal

Choy

Yang

et al. 2014

American Journal of Physiology-Heart and Circulatory Physiology

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Slow moving blood flow and changes in flow direction, e.g., negative wall shear stress, can cause increased superoxide (O2 ·Ϫ ) production in vascular endothelial cells. The mechanism by which shear stress increases O2·Ϫ production, however, is not well established. We tested the hypothesis that actin depolymerization, which occurs during flow reversal, mediates O2 ·Ϫ production in vascular endothelial cells via NADPH oxidase, and more specifically, the subunit p47 phox . Using a swine model, we created complete blood flow reversal in one carotid artery, while the contralateral vessel maintained forward blood flow as control. We measured actin depolymerization, NADPH oxidase activity, and reactive oxygen species (ROS) production in the presence of various inhibitors. Flow reversal was found to induce actin depolymerization and a 3.9 Ϯ 1.0-fold increase in ROS production as compared with forward flow. NADPH oxidase activity was 1.4 Ϯ 0.2 times higher in vessel segments subjected to reversed blood flow when measured by a direct enzyme assay. The NADPH oxidase subunits gp91 phox (Nox2) and p47 phox content in the vessels remained unchanged after 4 h of flow reversal. In contrast, p47 phox phosphorylation was increased in vessels with reversed flow. The response caused by reversed flow was reduced by in vivo treatment with jasplakinolide, an actin stabilizer (only a 1.7 Ϯ 0.3-fold increase). Apocynin (an antioxidant) prevented reversed flow-induced ROS production when the animals were treated in vivo. Cytochalasin D mimicked actin depolymerization in vitro and caused a 5.2 Ϯ 3.0-fold increase in ROS production. These findings suggest that actin filaments play an important role in negative shear stress-induced ROS production by potentiating NADPH oxidase activity, and more specifically, the p47 phox subunit in vascular endothelium.endothelial cells

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Section: Discussionsupporting

confidence: 56%

Section: Discussionmentioning

confidence: 99%

Endothelial actin depolymerization mediates NADPH oxidase-superoxide production during flow reversal

Choy

Yang

et al. 2014

American Journal of Physiology-Heart and Circulatory Physiology

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“…Noh and Koh (2000) revealed that overloading cortical neurons and astrocytes with zinc activates NADPH oxidase via protein kinase C (PKC) activation. It has been reported that activation of phosphatidylinositol 3 0 -kinase (PI3K) and the small G-protein Rac play regulatory roles of PKC in NADPH oxidase activation (DeLeo and Quinn, 1996;Imagawa et al, 2005). In microglial chemotaxis, the motility of microglia via P234/P2Y12 receptor activation by ATP/ADP was demonstrated to be mediated by activation of PI3K (Honda et al, 2001) and Rac (Ohsawa, 2007).…”

Section: Introductionmentioning

confidence: 99%

Microglial zinc uptake via zinc transporters induces ATP release and the activation of microglia

Higashi

Segawa

Matsuo

et al. 2011

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Previously, we demonstrated that extracellular zinc plays a key role in transient global ischemia-induced microglial activation through sequential activation of NADPH oxidase and poly(ADP-ribose) polymerase (PARP)-1. However, it remains unclear how zinc causes the sequential activation of microglia. Here, we examined whether transporter-mediated zinc uptake is necessary for microglial activation. Administration of zinc to microglia activated them through reactive oxygen species (ROS) generation and poly(ADP-ribose) (PAR) formation, which were suppressed by intracellular zinc chelation with 25 μM TPEN (N,N,N',N'-tetrakis(2-pyridylmethyl)ethylenediamine) or 2 μM BAPTA-AM (1,2-bis(2-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid-acetoxymethyl ester). The (65)Zn uptake by microglia was temperature- and dose-dependent, and it was blocked by metal cations, but not by L-type calcium channel blockers nifedipine and nimodipine. Expression of Zrt-Irt-like protein (ZIP)1, a plasma membrane-type zinc transporter, was detected in microglia, and nickel, a relatively sensitive substrate/inhibitor of ZIP1, showed cis- and trans-inhibitory effects on the (65)Zn uptake. Exposure of microglia to zinc increased the extracellular ATP concentration, which was suppressed by intracellular zinc chelation and inhibition of hemichannels. mRNA expression of several types of P2 receptors was detected in microglia, and periodate-oxidized ATP, a selective P2×7 receptor antagonist, attenuated the zinc-induced microglial activation via NADPH oxidase and PARP-1. Exogenous ATP and 2'(3')-O-(4-benzoyl-benzoyl) ATP also caused microglial activation through ROS generation and PAR formation. These findings demonstrate that ZIP1-mediated uptake of zinc induces ATP release and autocrine/paracrine activation of P2X(7) receptors, and then activates microglia, suggesting that zinc transporter-mediated uptake of zinc is a trigger for microglial activation via the NADPH oxidase and PARP-1 pathway. © 2011 Wiley-Liss, Inc.

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Mechanobiology

Kassab

2024

Coronary Circulation

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Protein kinase C-independent pathway for NADPH oxidase activation in guinea pig peritoneal polymorphonuclear leukocytes by cytochalasin D

Cited by 7 publications

References 38 publications

Endothelial actin depolymerization mediates NADPH oxidase-superoxide production during flow reversal

Endothelial actin depolymerization mediates NADPH oxidase-superoxide production during flow reversal

Microglial zinc uptake via zinc transporters induces ATP release and the activation of microglia

Mechanobiology

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