Redox regulation of platelet-derived-growth-factor-receptor: Role of NADPH-oxidase and c-Src tyrosine kinase

Catarzi, Serena; Biagioni, Chiara; Giannoni, Elisa; Favilli, Franco; Marcucci, Tommaso; Iantomasi, Teresa; Vincenzini, Massimo

doi:10.1016/j.bbamcr.2005.03.004

Cited by 58 publications

(45 citation statements)

References 44 publications

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“…Previous studies have implicated a role for ROS in mediating reversible receptor autophosphorylation in response to such ligands as insulin, epidermal growth factor, and platelet-derived growth factor (70,71,72). In addition, angiotensin IImediated transactivation of the epidermal growth factor receptor and platelet-derived growth factor receptor in vascular smooth muscle cells was shown to be redox-sensitive (73,74).…”

Section: Discussionmentioning

confidence: 99%

NADPH Oxidase Activity Selectively Modulates Vascular Endothelial Growth Factor Signaling Pathways

Abid¹,

Spokes²,

Shih

et al. 2007

Journal of Biological Chemistry

135

125

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Vascular endothelial growth factor (VEGF) and reactive oxygen species (ROS) play critical roles in vascular physiology and pathophysiology. We have demonstrated previously that NADPH oxidase-derived ROS are required for VEGF-mediated migration and proliferation of endothelial cells. The goal of this study was to determine the extent to which VEGF signaling is coupled to NADPH oxidase activity. Human umbilical vein endothelial cells and/or human coronary artery endothelial cells were transfected with short interfering RNA against the p47 phox subunit of NADPH oxidase, treated in the absence or presence of VEGF, and assayed for signaling, gene expression, and function. We show that NADPH oxidase activity is required for VEGF activation of phosphoinositide 3-kinase-Akt-forkhead, and p38 MAPK, but not ERK1/2 or JNK. The permissive role of NADPH oxidase on phosphoinositide 3-kinase-Akt-forkhead signaling is mediated at post-VEGF receptor levels and involves the nonreceptor tyrosine kinase Src. DNA microarrays revealed the existence of two distinct classes of VEGF-responsive genes, one that is ROS-dependent and another that is independent of ROS levels. VEGF-induced, thrombomodulin-dependent activation of protein C was dependent on NADPH oxidase activity, whereas VEGF-induced decay-accelerating factor-mediated protection of endothelial cells against complement-mediated lysis was not. Taken together, these findings suggest that NADPH oxidase-derived ROS selectively modulate some but not all the effects of VEGF on endothelial cell phenotypes.

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Section: Discussionmentioning

confidence: 99%

NADPH Oxidase Activity Selectively Modulates Vascular Endothelial Growth Factor Signaling Pathways

Abid¹,

Spokes²,

Shih

et al. 2007

Journal of Biological Chemistry

135

125

View full text Add to dashboard Cite

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“…An intact Txn system may be necessary to attenuate signaling by surface receptors. In response to ligand binding, NADPH-oxidase enzymes associated with the cytosolic aspect of growth factor receptors generate H 2 O 2 [22][23][24]26,[75][76][77][78][79][80][81][82][83]. A conserved catalytic cysteine at the active site of protein tyrosine phosphatases is oxidized by H 2 O 2 to a sulfenic acid, which further reacts with a backbone nitrogen to form a sulfenylamide [68].…”

Section: Effects On Signalingmentioning

confidence: 99%

Effects of thioredoxin reductase-1 deletion on embryogenesis and transcriptome

Bondareva¹,

Capecchi²,

Iverson³

et al. 2007

Free Radical Biology and Medicine

100

112

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Thioredoxin reductases (Txnrd)1 maintain intracellular redox homeostasis in most organisms. Metazoans Txnrds also participate in signal transduction. Mouse embryos homozygous for a targeted null mutation of the txnrd1 gene, encoding the cytosolic thioredoxin reductase, were viable at embryonic day 8.5 (E8.5) but not at E9.5. Histology revealed that txnrd1 −/− cells were capable of proliferation and differentiation; however, mutant embryos were smaller than wild-type littermates and failed to gastrulate. In situ marker gene analyses indicated primitive streak mesoderm did not form. Microarray analyses on E7.5 txnrd −/− and txnrd +/+ littermates showed similar mRNA levels for peroxiredoxins, glutathione reductases, mitochondrial Txnrd2, and most markers of cell proliferation. Conversely, mRNAs encoding sulfiredoxin, IGF-binding protein 1, carbonyl reductase 3, glutamate cysteine ligase, glutathione S-transferases, and metallothioneins were more abundant in mutants. Many gene expression responses mirrored those in thioredoxin reductase 1-null yeast; however mice exhibited a novel response within the peroxiredoxin catalytic cycle. Thus, whereas yeast induce peroxiredoxin mRNAs in response to thioredoxin reductase disruption, mice induced sulfiredoxin mRNA. In summary, Txnrd1 was required for correct patterning of the early embryo and progression to later development. Conserved responses to Txnrd1 disruption likely allowed proliferation and limited differentiation of the mutant embryo cells.

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“…To analyze the pathway involved in atorvastatindependent Nox2 inhibition, we studied PKC phosphorylation, an upstream signaling for activation of Rac1, a key unit for NADPH oxidase activation. 18 Atorvastatin (1-10 mol/L) dose-dependently decreased AA-induced PKC ( Figure 6C) and Rac1 phosphorylation ( Figure 6D). …”

Section: Effect Of Atorvastatin On Platelet Oxidative Stressmentioning

confidence: 99%

Immediate Antioxidant and Antiplatelet Effect of Atorvastatin via Inhibition of Nox2

et al. 2012

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Background-Statins exert an antithrombotic effect in patients at risk of or with acute thrombosis, but no study has investigated whether this effect is immediate and whether there is an underline mechanism. Methods and Results-Patients with hypercholesterolemia were randomly allocated to a Mediterranean diet with low cholesterol intake (Ͻ300 mg/d; nϭ15) or atorvastatin (40 mg/d; nϭ15). Oxidative stress, as assessed by serum Nox2 and urinary isoprostanes, and platelet activation, as assessed by platelet recruitment, platelet isoprostanes, and thromboxane A 2 , platelet Nox2, Rac1, p47

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Redox regulation of platelet-derived-growth-factor-receptor: Role of NADPH-oxidase and c-Src tyrosine kinase

Cited by 58 publications

References 44 publications

NADPH Oxidase Activity Selectively Modulates Vascular Endothelial Growth Factor Signaling Pathways

NADPH Oxidase Activity Selectively Modulates Vascular Endothelial Growth Factor Signaling Pathways

Effects of thioredoxin reductase-1 deletion on embryogenesis and transcriptome

Immediate Antioxidant and Antiplatelet Effect of Atorvastatin via Inhibition of Nox2

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