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Am J Physiol Lung Cell Mol Physiol 285: L1184-L1189, 2003; doi:10.1152/ajplung.00281.2003
1040-0605/03 $5.00
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Regulation of ion channel structure and function by reactive oxygen-nitrogen species

Sadis Matalon,1,2 Karin M. Hardiman,1,3 Lucky Jain,4 Douglas C. Eaton,5 Michael Kotlikoff,6 Jerry P. Eu,7 Junhui Sun,7 Gerhard Meissner,8 and Jonathan S. Stamler7,9

Departments of 1Physiology and Biophysics and 2Anesthesiology and the 3Medical Scientists Training Program, University of Alabama at Birmingham, Birmingham Alabama 35233; Departments of 4Pediatrics and 5Physiology and the Center for Cell and Molecular Signaling, Emory University School of Medicine, Atlanta, Georgia 30322; 6Department of Biomedical Sciences, College of Veterinary Medicine, Cornell University, Ithaca, New York 14853-6401; Departments of 7Medicine and 9Biochemistry and Howard Hughes Medical Institute, Duke University Medical Center, Durham 27710; and 8Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599-7260

Ion channels subserve diverse cellular functions. Reactive oxygen and nitrogen species modulate ion channel function by a number of mechanisms including 1) transcriptional regulation of gene expression, 2) posttranslational modifications of channel proteins, i.e. nitrosylation, nitration, and oxidation of key amino acid residues, 3) by altering the gain in other signaling pathways that may in turn lead to changes in channel activity or channel gene expression, and 4) by modulating trafficking or turnover of channel proteins, as typified by oxygen radical activation of NF-kB, with subsequent changes in proteasomal degradation of channel degradation. Regardless of the mechanism, as was discussed in a symposium at the 2003 Experimental Biology Meeting in San Diego, CA, changes in the cellular level of reactive oxygen and nitrogen species can have profound effects on the activity of ion channels and cellular function.

calcium channels; potassium channels; sodium channels; chloride channels; nitric oxide; cystic fibrosis transmembrane conductance regulator


Address for reprint requests and other correspondence: S. Matalon, Dept. of Anesthesiology, Univ. of Alabama at Birmingham, Rm. 224, BMR II, 901 S. 19th St., Birmingham, AL 35205-3703 (E-mail: Sadis{at}uab.edu).




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