The DOI matches its Crossref record; 39 of the 39 references it cites were found in a registry or an index.
Distinct Subcellular Localizations of Nox1 and Nox4 in Vascular Smooth Muscle Cells
Abstract
Objective— Reactive oxygen species (ROS) that act as signaling molecules in vascular smooth muscle cells (VSMC) and contribute to growth, hypertrophy, and migration in atherogenesis are produced by multi-subunit NAD(P)H oxidases. Nox1 and Nox4, two homologues to the phagocytic NAD(P)H subunit gp91 phox , both generate ROS in VSMC but differ in their response to growth factors. We hypothesize that the opposing functions of Nox1 and Nox4 are reflected in their differential subcellular locations. Methods and Results— We used immunofluorescence to visualize the NAD(P)H subunits Nox1, Nox4, and p22 phox in cultured rat and human VSMC. Optical sectioning using confocal microscopy showed that Nox1 is co-localized with caveolin in punctate patches on the surface and along the cellular margins, whereas Nox4 is co-localized with vinculin in focal adhesions. These immunocytochemical distributions are supported by membrane fractionation experiments. Interestingly, p22 phox , a membrane subunit that interacts with the Nox proteins, is found in surface labeling and in focal adhesions in patterns similar to Nox1 and Nox4, respectively. Conclusions— The differential roles of Nox1 and Nox4 in VSMC may be correlated with their differential compartmentalization in specific signaling domains in the membrane and focal adhesions.
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“NOX1 is found in caveolae and signalosomes of vascular cells (423, 431, 652).”
From Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation (2019) · cites this paper as [431]
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Cites
1 retracted
Ushio‐Fukai, M., Hilenski, L. L., Santanam, N., Becker, P. L., Ma, Y., Griendling, K. K., & Alexander, R. W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105901200 · Cited by 204
Self-citationRetractedFree Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
Giancotti, F. G., & Ruoslahti, E. (1999) · Science · doi:10.1126/science.285.5430.1028 · Cited by 3,869
NAD(P)H Oxidase: Role in Cardiovascular Biology and Disease
Griendling, K. K., Sorescu, D., & Ushio-Fukai, M. (2000) · Circulation Research · doi:10.1161/01.res.86.5.494 · Cited by 2,886
Self-citationCaveolin, a protein component of caveolae membrane coats
Rothberg, K. G., Heuser, J. E., Donzell, W. C., Ying, Y., Glenney, J. R., & Anderson, R. G. W. (1992) · Cell · doi:10.1016/0092-8674(92)90143-z · Cited by 2,259
BABIOR, B. M. (1999) · Blood · doi:10.1182/blood.v93.5.1464 · Cited by 2,147
FOCAL ADHESIONS, CONTRACTILITY, AND SIGNALING
Burridge, K., & Chrzanowska‐Wodnicka, M. (1996) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.12.1.463 · Cited by 1,957
Okamoto, T., Schlegel, A., Scherer, P. E., & Lisanti, M. P. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.10.5419 · Cited by 1,496
Cell transformation by the superoxide-generating oxidase Mox1
Suh, Y.-A., Arnold, R. S., Lassegue, B., Shi, J., Xu, X., Sorescu, D., Chung, A. B., Griendling, K. K., & Lambeth, J. D. (1999) · Nature · doi:10.1038/43459 · Cited by 1,480
Self-citationKilling activity of neutrophils is mediated through activation of proteases by K+ flux
Reeves, E. P., Lu, H., Jacobs, H. L., Messina, C. G. M., Bolsover, S., Gabella, G., Potma, E. O., Warley, A., Roes, J., & Segal, A. W. (2002) · Nature · doi:10.1038/416291a · Cited by 1,153
Vascular NAD(P)H oxidases: specific features, expression, and regulation
Lassegue, B. P., & Clempus, R. E. (2003) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00758.2002 · Cited by 1,026
Self-citationCaveolins, Liquid-Ordered Domains, and Signal Transduction
Smart, E. J., Graf, G. A., McNiven, M. A., Sessa, W. C., Engelman, J. A., Scherer, P. E., Okamoto, T., & Lisanti, M. P. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.11.7289 · Cited by 1,005
Identification of Renox, an NAD(P)H oxidase in kidney
Geiszt, M., Kopp, J. B., Várnai, P., & Leto, T. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.130135897 · Cited by 840
Lassègue, B., Sorescu, D., Szöcs, K., Yin, Q., Akers, M., Zhang, Y., Grant, S. L., Lambeth, J. D., & Griendling, K. K. (2001) · Circulation Research · doi:10.1161/hh0901.090299 · Cited by 839
Self-citationHomologs of gp91 phox : cloning and tissue expression of Nox3, Nox4, and Nox5
Cheng, G., Cao, Z., Xu, X., Meir, E. G. V., & Lambeth, J. D. (2001) · Gene · doi:10.1016/s0378-1119(01)00449-8 · Cited by 820
Self-citationA detergent-free method for purifying caveolae membrane from tissue culture cells.
Smart, E. J., Ying, Y. S., Mineo, C., & Anderson, R. G. W. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.22.10104 · Cited by 728
Angiotensin II Stimulation of NAD(P)H Oxidase Activity
Seshiah, P., Weber, D. S., Ročić, P., Valppu, L., Taniyama, Y., & Griendling, K. K. (2002) · Circulation Research · doi:10.1161/01.res.0000033523.08033.16 · Cited by 711
Self-citationUshio‐Fukai, M., Alexander, R. W., Akers, M., & Griendling, K. K. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.24.15022 · Cited by 648
Self-citationMalhotra, S. K. (1983) · Cited by 556
Upregulation of Nox-Based NAD(P)H Oxidases in Restenosis After Carotid Injury
Szöcs, K., Lassegue, B. P., Sorescu, D., Hilenski, L. L., Valppu, L., Couse, T. L., Wilcox, J. N., Quinn, M. T., Lambeth, J. D., & Griendling, K. K. (2002) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/hq0102.102189 · Cited by 443
Self-citationReactive oxygen species as mediators of angiotensin II signaling
Griendling, K. K., & Ushio‐Fukai, M. (2000) · Regulatory Peptides · doi:10.1016/s0167-0115(00)00136-1 · Cited by 417
Self-citationLi, J., & Shah, A. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110073200 · Cited by 390
Lambeth, J. D., Cheng, G., Arnold, R. S., & Edens, W. A. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01658-3 · Cited by 355
Self-citationDugina, V. B., Fontao, L., Chaponnier, C., Vasiliev, J. M., & Gabbiani, G. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.18.3285 · Cited by 309
Angiotensin II Type 1 Receptor
Ishizaka, N., Griendling, K. K., Lassegue, B. P., & Alexander, R. W. (1998) · Hypertension · doi:10.1161/01.hyp.32.3.459 · Cited by 225
Self-citationKarlsson, A., Nixon, J. B., & McPhail, L. C. (2000) · Journal of Leukocyte Biology · doi:10.1002/jlb.67.3.396 · Cited by 220
Benna, J. E., Ruedi, J. M., & BABIOR, B. M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37436-7 · Cited by 192
Jesaitis, A. J., Buescher, E. S., Harrison, D. J., Quinn, M. T., Parkos, C. A., Livesey, S. A., & Linner, J. G. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114509 · Cited by 148
Self-citationWoodman, R. C., Ruedi, J. M., Jesaitis, A. J., Okamura, N., Quinn, M. T., Smith, R. M., Curnutte, J. T., & BABIOR, B. M. (1991) · Journal of Clinical Investigation · doi:10.1172/jci115138 · Cited by 146
Self-citationBrown, G. E., Stewart, M. Q., Liu, H., Ha, V.-L., & Yaffe, M. B. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00005-4 · Cited by 139
Identification of intracellular sites of superoxide production in stimulated neutrophils
Kobayashi, T., Robinson, J. M., & Seguchi, H. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.1.81 · Cited by 129
Nuclear and cytoplasmic localizations of the adenomatous polyposis coli protein
Neufeld, K. L., & White, R. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.7.3034 · Cited by 122
Griendling, K. K., Taubman, M. B., Akers, M., et al. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98644-8 · Cited by 97
Self-citationRegulation of Src Family Tyrosine Kinase Activities in Adherent Human Neutrophils
Yan, S. R., & Berton, G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.38.23464 · Cited by 91
NAD(P)H Oxidases and Their Relevance to Atherosclerosis
Sorescu, D. (2001) · Trends in Cardiovascular Medicine · doi:10.1016/s1050-1738(01)00097-4 · Cited by 91
Yan, S. R., Fumagalli, L., Dusi, S., et al. (1995) · Journal of Leukocyte Biology · doi:10.1002/jlb.58.5.595 · Cited by 64
Benna, J. E., Dang, P. M., Andrieu, V., Vergnaud, S., Dewas, C., Cachia, O., Fay, M., Morel, F., Chollet‐Martin, S., Hakim, J., et al. (1999) · Journal of Leukocyte Biology · doi:10.1002/jlb.66.6.1014 · Cited by 54
Neutrophils with a License to Kill
Finkel, T. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00023-6 · Cited by 8
Miyazaki, T., Inoue, Y., & Takano, K. (1995) · ACTA HISTOCHEMICA ET CYTOCHEMICA · doi:10.1267/ahc.28.365 · Cited by 3
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Metadata
- Authors
- Hilenski, L. L., Clempus, R. E., Quinn, M. T., Lambeth, J. D., & Griendling, K. K.
- Affiliations
- Emory University (US)
- Venue
- Arteriosclerosis, Thrombosis, and Vascular Biology
- Published
- 2004-04
- Volume
- 24
- Issue
- 4
- Pages
- 677-683
- ISSN
- 1079-5642 (ISSN-L)
- 1524-4636
- OpenAlex
- W2115239727
- Cited by
- 573
- References
- 39
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 5 · 2023: 15 · 2022: 9 · 2021: 13 · 2020: 14 · 2019: 21 · 2018: 22 · 2017: 25 · 2016: 17 · 2015: 23 · 2014: 36 · 2013: 39 · 2012: 53
- FWCI
- 16.48
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Arteriosclerosis Thrombosis and Vascular Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Heart, Lung, and Blood Institute (HL 58000, HL38206, HL58863, P01HL058000, R01HL058863)
- Topics
- Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- NOX1, NOX4, NADPH oxidase, reactive oxygen species, vascular smooth muscle cells, subcellular localization, p22phox, caveolin, focal adhesions, vinculin, membrane compartmentalization, atherogenesis
- MeSH terms
- NADPH Oxidase 1, NADPH Oxidase 4, Animals, Cell Division, Cell Fractionation, Cells, Cultured, Cytoskeleton, Humans, Male, Microscopy, Fluorescence, Muscle, Smooth, Vascular, NADH, NADPH Oxidoreductases, NADPH Dehydrogenase, Oxidation-Reduction, Phosphoproteins, Vinculin, Cellular Senescence, Rats, Sprague-Dawley, Reactive Oxygen Species, Microscopy, Confocal, NADPH Oxidases, Protein Subunits, Caveolae, Focal Adhesions, Caveolins, Membrane Transport Proteins, Myocytes, Smooth Muscle, Macromolecular Substances, Caveolin 1, Rats
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