Selective recapitulation of conserved and nonconserved regions of putative noxa1 protein activation domain confers isoform-specific inhibition of nox1 oxidase and attenuation of endothelial cell migration

Daniel J. Ranayhossaini; Andres I. Rodriguez; Sanghamitra Sahoo; Beibei B. Chen; Rama K. Mallampalli; Eric E. Kelley; Gabor Csanyi; Mark T. Gladwin; Guillermo Romero; Patrick J. Pagano

doi:10.1074/jbc.M113.521344

Selective recapitulation of conserved and nonconserved regions of putative noxa1 protein activation domain confers isoform-specific inhibition of nox1 oxidase and attenuation of endothelial cell migration

Daniel J. Ranayhossaini, Andres I. Rodriguez, Sanghamitra Sahoo, Beibei B. Chen, Rama K. Mallampalli, Eric E. Kelley, Gabor Csanyi, Mark T. Gladwin, Guillermo Romero, Patrick J. Pagano

Research output: Contribution to journal › Article › peer-review

72 Scopus citations

Abstract

Background: Nox1, an oxidant source in colon carcinoma and vascular disease, is activated by NOXA1. Results: A NOXA1 peptide blocked NOXA1-Nox1 binding and inhibited colon carcinoma and endothelial oxidants and migration. Conclusion: The findings identify a NOXA1-Activating domain and an isoform-specific Nox1 inhibitor. Significance: The data provide insight into Nox1 regulation and present a potential therapy for suppressing oxidative stressrelated disease.

Original language	English (US)
Pages (from-to)	36437-36450
Number of pages	14
Journal	Journal of Biological Chemistry
Volume	288
Issue number	51
DOIs	https://doi.org/10.1074/jbc.M113.521344
State	Published - Dec 20 2013
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Molecular Biology
Cell Biology

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Ranayhossaini, D. J., Rodriguez, A. I., Sahoo, S., Chen, B. B., Mallampalli, R. K., Kelley, E. E., Csanyi, G., Gladwin, M. T., Romero, G., & Pagano, P. J. (2013). Selective recapitulation of conserved and nonconserved regions of putative noxa1 protein activation domain confers isoform-specific inhibition of nox1 oxidase and attenuation of endothelial cell migration. Journal of Biological Chemistry, 288(51), 36437-36450. https://doi.org/10.1074/jbc.M113.521344

Selective recapitulation of conserved and nonconserved regions of putative noxa1 protein activation domain confers isoform-specific inhibition of nox1 oxidase and attenuation of endothelial cell migration. / Ranayhossaini, Daniel J.; Rodriguez, Andres I.; Sahoo, Sanghamitra et al.
In: Journal of Biological Chemistry, Vol. 288, No. 51, 20.12.2013, p. 36437-36450.

Research output: Contribution to journal › Article › peer-review

Ranayhossaini, DJ, Rodriguez, AI, Sahoo, S, Chen, BB, Mallampalli, RK, Kelley, EE, Csanyi, G, Gladwin, MT, Romero, G & Pagano, PJ 2013, 'Selective recapitulation of conserved and nonconserved regions of putative noxa1 protein activation domain confers isoform-specific inhibition of nox1 oxidase and attenuation of endothelial cell migration', Journal of Biological Chemistry, vol. 288, no. 51, pp. 36437-36450. https://doi.org/10.1074/jbc.M113.521344

Ranayhossaini DJ, Rodriguez AI, Sahoo S, Chen BB, Mallampalli RK, Kelley EE et al. Selective recapitulation of conserved and nonconserved regions of putative noxa1 protein activation domain confers isoform-specific inhibition of nox1 oxidase and attenuation of endothelial cell migration. Journal of Biological Chemistry. 2013 Dec 20;288(51):36437-36450. doi: 10.1074/jbc.M113.521344

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title = "Selective recapitulation of conserved and nonconserved regions of putative noxa1 protein activation domain confers isoform-specific inhibition of nox1 oxidase and attenuation of endothelial cell migration",

abstract = "Background: Nox1, an oxidant source in colon carcinoma and vascular disease, is activated by NOXA1. Results: A NOXA1 peptide blocked NOXA1-Nox1 binding and inhibited colon carcinoma and endothelial oxidants and migration. Conclusion: The findings identify a NOXA1-Activating domain and an isoform-specific Nox1 inhibitor. Significance: The data provide insight into Nox1 regulation and present a potential therapy for suppressing oxidative stressrelated disease.",

author = "Ranayhossaini, \{Daniel J.\} and Rodriguez, \{Andres I.\} and Sanghamitra Sahoo and Chen, \{Beibei B.\} and Mallampalli, \{Rama K.\} and Kelley, \{Eric E.\} and Gabor Csanyi and Gladwin, \{Mark T.\} and Guillermo Romero and Pagano, \{Patrick J.\}",

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doi = "10.1074/jbc.M113.521344",

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AU - Rodriguez, Andres I.

AU - Sahoo, Sanghamitra

AU - Chen, Beibei B.

AU - Mallampalli, Rama K.

AU - Kelley, Eric E.

AU - Csanyi, Gabor

AU - Gladwin, Mark T.

AU - Romero, Guillermo

AU - Pagano, Patrick J.

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N2 - Background: Nox1, an oxidant source in colon carcinoma and vascular disease, is activated by NOXA1. Results: A NOXA1 peptide blocked NOXA1-Nox1 binding and inhibited colon carcinoma and endothelial oxidants and migration. Conclusion: The findings identify a NOXA1-Activating domain and an isoform-specific Nox1 inhibitor. Significance: The data provide insight into Nox1 regulation and present a potential therapy for suppressing oxidative stressrelated disease.

AB - Background: Nox1, an oxidant source in colon carcinoma and vascular disease, is activated by NOXA1. Results: A NOXA1 peptide blocked NOXA1-Nox1 binding and inhibited colon carcinoma and endothelial oxidants and migration. Conclusion: The findings identify a NOXA1-Activating domain and an isoform-specific Nox1 inhibitor. Significance: The data provide insight into Nox1 regulation and present a potential therapy for suppressing oxidative stressrelated disease.

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Selective recapitulation of conserved and nonconserved regions of putative noxa1 protein activation domain confers isoform-specific inhibition of nox1 oxidase and attenuation of endothelial cell migration

Abstract

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