The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
NOX5 in Human Spermatozoa
Open accessAbstract
Physiological and pathological processes in spermatozoa involve the production of reactive oxygen species (ROS), but the identity of the ROS-producing enzyme system(s) remains a matter of speculation. We provide the first evidence that NOX5 NADPH oxidase is expressed and functions in human spermatozoa. Immunofluorescence microscopy detected NOX5 protein in both the flagella/neck region and the acrosome. Functionally, spermatozoa exposed to calcium ionophore, phorbol ester, or H(2)O(2) exhibited superoxide anion production, which was blocked by addition of superoxide dismutase, a Ca(2+) chelator, or inhibitors of either flavoprotein oxidases (diphenylene iododonium) or NOX enzymes (GKT136901). Consistent with our previous overexpression studies, we found that H(2)O(2)-induced superoxide production by primary sperm cells was mediated by the non-receptor tyrosine kinase c-Abl. Moreover, the H(V)1 proton channel, which was recently implicated in spermatozoa motility, was required for optimal superoxide production by spermatozoa. Immunoprecipitation experiments suggested an interaction among NOX5, c-Abl, and H(V)1. H(2)O(2) treatment increased the proportion of motile sperm in a NOX5-dependent manner. Statistical analyses showed a pH-dependent correlation between superoxide production and enhanced sperm motility. Collectively, our findings show that NOX5 is a major source of ROS in human spermatozoa and indicate a role for NOX5-dependent ROS generation in human spermatozoa motility.
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Cites
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A Ca2+-activated NADPH Oxidase in Testis, Spleen, and Lymph Nodes
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Mechanism of Ca2+ Activation of the NADPH Oxidase 5 (NOX5)
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Self-citationNovel Mechanism of Activation of NADPH Oxidase 5
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Nox5 mediates PDGF-induced proliferation in human aortic smooth muscle cells
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Cited by
Nox family NADPH oxidases: Molecular mechanisms of activation
Brandes, R. P., Weissmann, N., & Schröder, K. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.07.046 · Cited by 673
Sources of Vascular Nitric Oxide and Reactive Oxygen Species and Their Regulation
Tejero, J., Shiva, S., & Gladwin, M. T. (2019) · Physiological Reviews · doi:10.1152/physrev.00036.2017 · Cited by 541
Evolution of nadph oxidase inhibitors: Selectivity and mechanisms for target engagement
Altenhöfer, S., Radermacher, K. A., Kleikers, P. W. M., Wingler, K., & Schmidt, H. H. H. W. (2015) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5814 · Cited by 521
Causes and consequences of oxidative stress in spermatozoa
Aitken, R. J., Gibb, Z., Baker, M. A., Drevet, J., & Gharagozloo, P. (2015) · Reproduction, Fertility and Development · doi:10.1071/rd15325 · Cited by 428
The Quest for Selective Nox Inhibitors and Therapeutics: Challenges, Triumphs and Pitfalls
Cifuentes-Pagano, E., Meijles, D. N., & Pagano, P. J. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5620 · Cited by 84
Metadata
- Authors
- Musset, B., Clark, R. A., DeCoursey, T. E., Petheo, G. L., Geiszt, M., Chen, Y., Cornell, J. E., Eddy, C. A., Brzyski, R. G., & El Jamali, A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2012-03
- Volume
- 287
- Issue
- 12
- Pages
- 9376-9388
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1968206606
- Cited by
- 168
- References
- 9
- FWCI
- 12.43
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Musset, B., Clark, R. A., DeCoursey, T. E., Petheo, G. L., Geiszt, M., Chen, Y., Cornell, J. E., Eddy, C. A., Brzyski, R. G., & El Jamali, A. (2012). NOX5 in Human Spermatozoa. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m111.314955
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