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J. Biol. Chem., Vol. 276, Issue 40, 37594-37601, October 5, 2001
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From the 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 gp91phox 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 Ca2+
concentration it generated large amounts of superoxide. Upon Ca2+ 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 Ca2+-dependent
manner. NOX5 is likely to be involved in Ca2+-activated,
redox-dependent processes of spermatozoa and lymphocytes such as sperm-oocyte fusion, cell proliferation, and cytokine secretion.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF353088, AF325189, AF353089, and AF325190.
A Ca2+-activated NADPH Oxidase in Testis,
Spleen, and Lymph Nodes*
§,
,,¶¶
Biology of Aging Laboratory,
Department of Geriatrics, Geneva University Hospitals, Ch. du
Petit-Bel-Air 2, CH-1225 Geneva, Switzerland, the ¶ Department of
Physiology and the Foundation for Medical Research, Geneva
Medical School, Rue de Michel-Servet 1, CH-1211 Geneva, Switzerland,
the § Department of Physiology, Semmelweis University,
Puskin utca 9, H-1444 Budapest 8, Hungary, the ** Institute
of Veterinary Anatomy, Frankfurter Strasse 98, D-35392 Giessen,
Germany, and the Department of Biological
Physics, Eotvos University, Pazmany Peter Setany 1A, H-1117
Budapest, Hungary
*
This research was supported by Swiss National Foundation
Grants 31-55344.98 and 31-56802.99; by a grant allocated by the
Swiss Foundation of Aging Research (AETAS), and the foundation Hans Wilsdorf, Geneva; and by United States Public Health Service, National
Institutes of Health Grants AI20866 and AG19519.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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