Tags

Type your tag names separated by a space and hit enter

A comparison of the NADPH oxidase in human sperm and white blood cells.
Int J Androl 2002; 25(4):223-9IJ

Abstract

The mechanism of reactive oxygen species (ROS) generation in human sperm has recently been found to depend upon a novel NADPH-oxidase (NOX5) resembling the multicomponent NADPH-oxidase of white blood cells (WBCs). The purpose of our study was to compare the ROS producing activity of NOX5 in sperm and NADPH-oxidase of WBCs, and to investigate the role of protein kinase C (PKC) in NOX5 activation. A combination of electron paramagnetic resonance (EPR), chemiluminescence (CL), and nitroblue tetrazolium (NBT) dye reduction were used to monitor ROS production by sperm. The involvement of PKC in NOX5 activation was investigated using myristate acetate (PMA), and the PKC inhibitor GF-109203X. The presence of b cytochrome in NOX5 was investigated by spectrophotometry. PMA-stimulated WBCs produced superoxide dismutase -- inhibitable EPR signals for both superoxide and hydroxyl radicals. Sperm did not produce these spectra with or without PMA stimulation. WBCs generated significantly increased levels of CL and reduced NBT after PMA stimulation; whereas sperm did not increase the CL response or reduce NBT. Adenosine triphosphate (ATP) levels in WBCs were significantly reduced after PMA stimulation, whereas sperm ATP levels did not change. The characteristic spectra of b cytochrome observed after dithionite reduction of WBCs was not observed with sperm under similar conditions. These results indicate that the ROS producing activity of NOX5 is significantly lower than the WBC NADPH-oxidase, and suggest that the activation mechanism of NOX5 in sperm is independent of PKC.

Authors+Show Affiliations

Department of Biochemistry, Emory University School of Medicine, Atlanta, GA, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Comparative Study
Journal Article

Language

eng

PubMed ID

12121572

Citation

Armstrong, Jeffrey S., et al. "A Comparison of the NADPH Oxidase in Human Sperm and White Blood Cells." International Journal of Andrology, vol. 25, no. 4, 2002, pp. 223-9.
Armstrong JS, Bivalacqua TJ, Chamulitrat W, et al. A comparison of the NADPH oxidase in human sperm and white blood cells. Int J Androl. 2002;25(4):223-9.
Armstrong, J. S., Bivalacqua, T. J., Chamulitrat, W., Sikka, S., & Hellstrom, W. J. (2002). A comparison of the NADPH oxidase in human sperm and white blood cells. International Journal of Andrology, 25(4), pp. 223-9.
Armstrong JS, et al. A Comparison of the NADPH Oxidase in Human Sperm and White Blood Cells. Int J Androl. 2002;25(4):223-9. PubMed PMID: 12121572.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A comparison of the NADPH oxidase in human sperm and white blood cells. AU - Armstrong,Jeffrey S, AU - Bivalacqua,Trinity J, AU - Chamulitrat,Walee, AU - Sikka,Suresh, AU - Hellstrom,Wayne J G, PY - 2002/7/18/pubmed PY - 2002/12/4/medline PY - 2002/7/18/entrez SP - 223 EP - 9 JF - International journal of andrology JO - Int. J. Androl. VL - 25 IS - 4 N2 - The mechanism of reactive oxygen species (ROS) generation in human sperm has recently been found to depend upon a novel NADPH-oxidase (NOX5) resembling the multicomponent NADPH-oxidase of white blood cells (WBCs). The purpose of our study was to compare the ROS producing activity of NOX5 in sperm and NADPH-oxidase of WBCs, and to investigate the role of protein kinase C (PKC) in NOX5 activation. A combination of electron paramagnetic resonance (EPR), chemiluminescence (CL), and nitroblue tetrazolium (NBT) dye reduction were used to monitor ROS production by sperm. The involvement of PKC in NOX5 activation was investigated using myristate acetate (PMA), and the PKC inhibitor GF-109203X. The presence of b cytochrome in NOX5 was investigated by spectrophotometry. PMA-stimulated WBCs produced superoxide dismutase -- inhibitable EPR signals for both superoxide and hydroxyl radicals. Sperm did not produce these spectra with or without PMA stimulation. WBCs generated significantly increased levels of CL and reduced NBT after PMA stimulation; whereas sperm did not increase the CL response or reduce NBT. Adenosine triphosphate (ATP) levels in WBCs were significantly reduced after PMA stimulation, whereas sperm ATP levels did not change. The characteristic spectra of b cytochrome observed after dithionite reduction of WBCs was not observed with sperm under similar conditions. These results indicate that the ROS producing activity of NOX5 is significantly lower than the WBC NADPH-oxidase, and suggest that the activation mechanism of NOX5 in sperm is independent of PKC. SN - 0105-6263 UR - https://www.unboundmedicine.com/medline/citation/12121572/A_comparison_of_the_NADPH_oxidase_in_human_sperm_and_white_blood_cells_ L2 - https://onlinelibrary.wiley.com/resolve/openurl?genre=article&sid=nlm:pubmed&issn=0105-6263&date=2002&volume=25&issue=4&spage=223 DB - PRIME DP - Unbound Medicine ER -