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A Ca(2+)-activated NADPH oxidase in testis, spleen, and lymph nodes.
J Biol Chem 2001; 276(40):37594-601JB

Abstract

Superoxide and its derivatives are increasingly implicated in the regulation of physiological functions from oxygen sensing and blood pressure regulation to lymphocyte activation and sperm-oocyte fusion. Here we describe a novel superoxide-generating NADPH oxidase referred to as NADPH oxidase 5 (NOX5). NOX5 is distantly related to the gp91(phox) subunit of the phagocyte NADPH oxidase with conserved regions crucial for the electron transport (NADPH, FAD and heme binding sites). However, NOX5 has a unique N-terminal extension that contains three EF hand motifs. The mRNA of NOX5 is expressed in pachytene spermatocytes of testis and in B- and T-lymphocyte-rich areas of spleen and lymph nodes. When heterologously expressed, NOX5 was quiescent in unstimulated cells. However, in response to elevations of the cytosolic Ca(2+) concentration it generated large amounts of superoxide. Upon Ca(2+) activation, NOX5 also displayed a second function: it became a proton channel, presumably to compensate charge and pH alterations due to electron export. In summary, we have identified a novel NADPH oxidase that generates superoxide and functions as a H(+) channel in a Ca(2+)-dependent manner. NOX5 is likely to be involved in Ca(2+)-activated, redox-dependent processes of spermatozoa and lymphocytes such as sperm-oocyte fusion, cell proliferation, and cytokine secretion.

Authors+Show Affiliations

Biology of Aging Laboratory, Department of Geriatrics, Geneva University Hospitals, Ch. du Petit-Bel-Air 2, CH-1225 Geneva, Switzerland.No 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, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

11483596

Citation

Bánfi, B, et al. "A Ca(2+)-activated NADPH Oxidase in Testis, Spleen, and Lymph Nodes." The Journal of Biological Chemistry, vol. 276, no. 40, 2001, pp. 37594-601.
Bánfi B, Molnár G, Maturana A, et al. A Ca(2+)-activated NADPH oxidase in testis, spleen, and lymph nodes. J Biol Chem. 2001;276(40):37594-601.
Bánfi, B., Molnár, G., Maturana, A., Steger, K., Heged슩s, B., Demaurex, N., & Krause, K. H. (2001). A Ca(2+)-activated NADPH oxidase in testis, spleen, and lymph nodes. The Journal of Biological Chemistry, 276(40), pp. 37594-601.
Bánfi B, et al. A Ca(2+)-activated NADPH Oxidase in Testis, Spleen, and Lymph Nodes. J Biol Chem. 2001 Oct 5;276(40):37594-601. PubMed PMID: 11483596.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A Ca(2+)-activated NADPH oxidase in testis, spleen, and lymph nodes. AU - Bánfi,B, AU - Molnár,G, AU - Maturana,A, AU - Steger,K, AU - Heged슩s,B, AU - Demaurex,N, AU - Krause,K H, Y1 - 2001/08/01/ PY - 2001/8/3/pubmed PY - 2002/1/5/medline PY - 2001/8/3/entrez SP - 37594 EP - 601 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 276 IS - 40 N2 - Superoxide and its derivatives are increasingly implicated in the regulation of physiological functions from oxygen sensing and blood pressure regulation to lymphocyte activation and sperm-oocyte fusion. Here we describe a novel superoxide-generating NADPH oxidase referred to as NADPH oxidase 5 (NOX5). NOX5 is distantly related to the gp91(phox) subunit of the phagocyte NADPH oxidase with conserved regions crucial for the electron transport (NADPH, FAD and heme binding sites). However, NOX5 has a unique N-terminal extension that contains three EF hand motifs. The mRNA of NOX5 is expressed in pachytene spermatocytes of testis and in B- and T-lymphocyte-rich areas of spleen and lymph nodes. When heterologously expressed, NOX5 was quiescent in unstimulated cells. However, in response to elevations of the cytosolic Ca(2+) concentration it generated large amounts of superoxide. Upon Ca(2+) activation, NOX5 also displayed a second function: it became a proton channel, presumably to compensate charge and pH alterations due to electron export. In summary, we have identified a novel NADPH oxidase that generates superoxide and functions as a H(+) channel in a Ca(2+)-dependent manner. NOX5 is likely to be involved in Ca(2+)-activated, redox-dependent processes of spermatozoa and lymphocytes such as sperm-oocyte fusion, cell proliferation, and cytokine secretion. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/11483596/A_Ca_2+__activated_NADPH_oxidase_in_testis_spleen_and_lymph_nodes_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=11483596 DB - PRIME DP - Unbound Medicine ER -