| ARTICLES |
|
| Year : 2001 | Volume
: 3
| Issue : 11 | Page : 49--64 |
The influence of superoxide dismutase and glutathione peroxidase deficiencies on noise induced hearing loss in mice
Sandra L McFadden1, Kevin K Ohlemiller2, Dalian Ding1, Marlene Shero1, Richard J Salvi2
1 Center for Hearing and Deafness, University at Buffalo, Buffalo, NY 14214, USA
2 Central Institute for the Deaf, St. Louis, MO 63110, USA
Correspondence Address:
Sandra L McFadden
Center for Hearing and Deafness, University at Buffalo, Buffalo, NY 14214
USA
 Source of Support: None, Conflict of Interest: None  | Check |
PMID: 12689448 
One consequence of noise exposure is increased production of reactive oxygen species (ROS), such as superoxide, hydrogen peroxide, and hydroxyl radicals, in the cochlea. ROS can cause oxidative damage to diverse cellular components, including membranes, proteins, and DNA, if they are not "neutralised" by antioxidant defences. Two important enzymes of the cochlear antioxidant defense system are cytosolic copper/zinc superoxide dismutase (SOD1) and selenium-dependent glutathione peroxidase (GPx1). These metalloenzymes work together to regulate ROS production in virtually every cell in the body, and they may be important for limiting cochlear damage associated with aging and acoustic overexposure. In this chapter, we describe a series of experiments using mice with targeted deletions of Sod1 or Gpx1, the mouse genes that code for SOD1 and GPx1, respectively, to study the cellular mechanisms underlying noise-induced hearing loss (NIHL). The results from Sod1 and Gpx1 knockout mice provide insights into the link between endogenous levels of antioxidant enzymes and susceptibility to NIHL.
[FULL TEXT] [PDF]*
|
Search Pubmed for
