Transcriptional regulation of the NADPH oxidase isoform, Nox1, in colon epithelial cells: Role of GATA-binding factor(s)

Brewer, Alison C.; Sparks, Emma; Shah, Ajay M.

doi:10.1016/j.freeradbiomed.2005.08.022

Cited by 42 publications

(29 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Although a putative GATA-binding site in mouse Nox1 promoter was reported (Brewer et al, 2006), the detailed regulatory mechanism of Nox1 expression and in vivo involvement of GATA-6 in the regulation of Nox1 promoter were not defined. Furthermore, no other study has revealed the phosphorylationdependent regulatory mechanism for GATA-6.…”

Section: Discussionmentioning

confidence: 99%

Oncogenic Ras upregulates NADPH oxidase 1 gene expression through MEK-ERK-dependent phosphorylation of GATA-6

et al. 2008

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 99%

Oncogenic Ras upregulates NADPH oxidase 1 gene expression through MEK-ERK-dependent phosphorylation of GATA-6

et al. 2008

View full text Add to dashboard Cite

“…These results are consistent with those reported on human phagocytes and vascular smooth muscle cells. 35,36 Brewer et al 37 reported that the NADPHox isoform, NOX1, is transcriptionally regulated by GATA-binding factors in human colon epithelial Caco-2 cells. Little is known about the effect of AP-1 on the regulation of NADPHox.…”

Section: Discussionmentioning

confidence: 99%

AP-1–Dependent Transcriptional Regulation of NADPH Oxidase in Human Aortic Smooth Muscle Cells

Manea¹,

Manea²,

Gafencu³

et al. 2008

ATVB

102

View full text Add to dashboard Cite

Objective-NADPH oxidase (NADPHox) is the major source of reactive oxygen species in vascular diseases; the mechanisms of enzyme activation are not completely elucidated. AP-1 controls the expression of many genes linked to vascular smooth muscle cells (SMCs) dysfunction. In this study we searched for the role of AP-1 in the regulation of NADPHox expression and function in human aortic SMCs exposed to proinflammatory conditions. Methods and Results-Cultured SMCs were exposed to either angiotensin II (Ang II) or tumor necrosis factor (TNF)-␣.The lucigenin-enhanced chemiluminescence assay and real-time polymerase chain reaction analysis revealed that AP-1 and mitogen-activated protein kinase inhibitors reduced both Ang II or TNF-␣-dependent upregulation of NADPHox activity and mRNA expression (NOX1, NOX4, p67 phox , p47 phox , p22 phox ). n cardiovascular disorders such as hypertension, atherosclerosis, heart failure, and diabetes the generation of reactive oxygen species (ROS) is increased in the vasculature primarily through the activation of NADPH oxidase 1,2 (NADPHox), a group of multi-subunit enzymes expressed by endothelial cells, smooth muscle cells (SMCs), pericytes, adventitial fibroblasts, and cardiac myocytes. 3,4 Hypertension, a major risk factor for cardiovascular diseases, is associated with functional-structural changes of blood vessels and in particular with vascular SMC hypertrophy, synthesis of excess extracellular matrix, and inflammatory cytokines. 5,6 Evidence exists that angiotensin II (Ang II) plays an important role in the pathogenesis of hypertensionrelated cardiovascular diseases. Besides its vasoactive action, Ang II stimulates NADPHox-derived ROS production, and exerts hypertrophic and hyperplasic effects by activating various intracellular signal transduction pathways. The latter include mitogen-activated protein kinase (MAPK) family members, extracellular signal-regulated protein kinase (ERK)1/2, c-Jun amino terminal kinase (JNK), p38 MAPK, and transcription factors such as nuclear factor kB (NF-kB) and activator protein-1 (AP-1). [7][8][9][10] Also, NADPHox-resulting ROS activate AP-1, which regulates cell growth and transformation, inflammation, innate immune response, and apoptosis. In vivo, evidence supports a key role of AP-1 in the vascular response to injury. [7][8][9][10][11][12][13][14][15] The NADPHox complex, the major source of superoxide in the vascular wall, 16 consists of 5 subunits: a membraneassociated cytochrome b 558 containing gp91 phox and p22 phox and a cytosolic complex of p40 phox , p47 phox , p67 phox17 . Besides gp91 phox (NOX2), NOX1 and NOX4 were identified in cardiovascular cells 3,4 and all require p22 phox for their activity. 6,18,19 The increased expression of oxidase subunits correlates with an enhanced vascular superoxid production in human atherosclerotic arteries and in hypertension 18,20 ; although important, the transcriptional regulatory mechanisms of NADPHox components are not entirely elucidated.Because proinflammatory stimuli activate both AP-1...

show abstract

“…Introduction of mutations at the AP-1 site consistently abolished prostanoidinduced transcriptional activation of the Nox1 promoter in a luciferase assay in vascular smooth muscle cells (Cevik et al, 2008). Several lines of study have shown that Nox1 gene transcription in nonphagocytic cells is modulated by members of the GATA family transcription factors, especially GATA-6 (Brewer et al, 2006;Adachi et al, 2008;Valente et al, 2008). Moreover, there is evidence that Nox4 transcription in smooth muscle cells is modulated by the transcription factor E2F, a critical protein in driving cell cycle progression and promoting cell proliferation .…”

Section: A Up-regulation Of Expressionmentioning

confidence: 99%

NADPH Oxidase-Mediated Redox Signaling: Roles in Cellular Stress Response, Stress Tolerance, and Tissue Repair

Jiang

Zhang

Dusting

2011

Pharmacological Reviews

514

381

View full text Add to dashboard Cite

Transcriptional regulation of the NADPH oxidase isoform, Nox1, in colon epithelial cells: Role of GATA-binding factor(s)

Cited by 42 publications

References 50 publications

Oncogenic Ras upregulates NADPH oxidase 1 gene expression through MEK-ERK-dependent phosphorylation of GATA-6

Oncogenic Ras upregulates NADPH oxidase 1 gene expression through MEK-ERK-dependent phosphorylation of GATA-6

AP-1–Dependent Transcriptional Regulation of NADPH Oxidase in Human Aortic Smooth Muscle Cells

NADPH Oxidase-Mediated Redox Signaling: Roles in Cellular Stress Response, Stress Tolerance, and Tissue Repair

Contact Info

Product

Resources

About