Decreased S-nitrosation of peptide thiols in the membrane interior. Free Radic Biol Med 2009 Oct 01;47(7):962-8
Date
07/04/2009Pubmed ID
19573593Pubmed Central ID
PMC2874255DOI
10.1016/j.freeradbiomed.2009.06.031Scopus ID
2-s2.0-69249209615 (requires institutional sign-in at Scopus site) 15 CitationsAbstract
It has been proposed that autoxidation of nitric oxide (()NO) stimulates S-nitrosation of thiols located in the hydrophobic milieu. We tested whether thiols located in hydrophobic membranes undergo enhanced S-nitrosation in the presence of ()NO/O(2). The transmembrane cysteinyl peptides C(4) (AcNH-KKACALA(LA)(6)KK-CONH(2)) and C(8) (AcNH-KKALALACALA(LA)(3)KK-CONH(2)) were incorporated into dilauroylphosphatidylcholine bilayers; their location in the membrane was determined by EPR spin labeling. The peptides, C(8) and C(4), and glutathione (GSH; 300 microM) were treated with a ()NO donor, DEA-NONOate, and nitrosothiol formation was determined under various O(2) levels. Surprisingly, the more hydrophobic cysteinyl peptide, C(8), did not yield any S-nitrosated product compared to GSH in the aqueous phase or C(4) peptide in the liposomes in the presence of ()NO/O(2). These data suggest that thiols located deeply in the hydrophobic core of the membrane may be less likely to undergo S-nitrosation in the presence of ()NO/O(2).
Author List
Zhang H, Andrekopoulos C, Xu Y, Joseph J, Hogg N, Feix J, Kalyanaraman BAuthors
Jimmy B. Feix PhD Professor in the Biophysics department at Medical College of WisconsinNeil Hogg PhD Associate Dean, Professor in the Biophysics department at Medical College of Wisconsin
Balaraman Kalyanaraman PhD Professor in the Biophysics department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
Chromatography, High Pressure LiquidLiposomes
Luminescent Measurements
Membranes, Artificial
Nitric Oxide
Nitroso Compounds
Oxygen
Peptides
Sulfhydryl Compounds
Time Factors