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J. Biol. Chem., Vol. 276, Issue 8, 5452-5458, February 23, 2001
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From the Division of Endocrinology, Department of Pediatrics,
Medical University of South Carolina,
Charleston, South Carolina 29425
Superoxide production contributes to osteoclastic
bone resorption. Evidence strongly indicates that NADPH oxidase is an
enzyme system responsible for superoxide generation in osteoclasts. A membrane-bound subunit, p91, is the catalytic domain of NADPH oxidase.
However, osteoclasts from p91 knockout mice still produce superoxide at
a rate similar to that observed in wild type mice. This unexpected
phenomenon prompted us to examine the osteoclasts for an alternative to
the p91-containing oxidase. In this study, the cloning of a NADPH
oxidase subunit (Nox 4) with 578 amino acids is reported. Nox 4 has
58% similarity in amino acids with the known p91 subunit of NADPH
oxidase. Nox 4 is present and active in osteoclasts. Antisense
oligonucleotides of Nox 4 reduced osteoclastic superoxide generation as
well as resorption pit formation by osteoclasts. This new oxidase
complex was present and functional in osteoclasts from p91 knockout
mice, explaining the normal resorptive activity seen in the osteoclasts
where no p91 is present.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF218723.
A New Superoxide-generating Oxidase in Murine
Osteoclasts*
,
*
This work was supported by GCRC in Medical University of
South Carolina and National Institutes of Health Grant
RO1-AR41463.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.
To whom correspondence should be addressed: 316 CSB, Pediatric
Endocrinology, Medical University of South Carolina, 171 Ashley Ave.,
Charleston, SC 29425. Tel.: 843-792-1346; Fax: 843-792-0548; E-mail: yangs@musc.edu.
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