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NOX5 in human spermatozoa: expression, function, and regulation.
J Biol Chem 2012; 287(12):9376-88JB

Abstract

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.

Authors+Show Affiliations

Department of Molecular Biophysics and Physiology, Rush University Medical Center, Chicago, Illinois 60612, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

22291013

Citation

Musset, Boris, et al. "NOX5 in Human Spermatozoa: Expression, Function, and Regulation." The Journal of Biological Chemistry, vol. 287, no. 12, 2012, pp. 9376-88.
Musset B, Clark RA, DeCoursey TE, et al. NOX5 in human spermatozoa: expression, function, and regulation. J Biol Chem. 2012;287(12):9376-88.
Musset, B., Clark, R. A., DeCoursey, T. E., Petheo, G. L., Geiszt, M., Chen, Y., ... El Jamali, A. (2012). NOX5 in human spermatozoa: expression, function, and regulation. The Journal of Biological Chemistry, 287(12), pp. 9376-88. doi:10.1074/jbc.M111.314955.
Musset B, et al. NOX5 in Human Spermatozoa: Expression, Function, and Regulation. J Biol Chem. 2012 Mar 16;287(12):9376-88. PubMed PMID: 22291013.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - NOX5 in human spermatozoa: expression, function, and regulation. AU - Musset,Boris, AU - Clark,Robert A, AU - DeCoursey,Thomas E, AU - Petheo,Gabor L, AU - Geiszt,Miklos, AU - Chen,Yumin, AU - Cornell,John E, AU - Eddy,Carlton A, AU - Brzyski,Robert G, AU - El Jamali,Amina, Y1 - 2012/01/30/ PY - 2012/2/1/entrez PY - 2012/2/1/pubmed PY - 2012/6/13/medline SP - 9376 EP - 88 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 287 IS - 12 N2 - 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. SN - 1083-351X UR - https://www.unboundmedicine.com/medline/citation/22291013/NOX5_in_human_spermatozoa:_expression_function_and_regulation_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=22291013 DB - PRIME DP - Unbound Medicine ER -