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Specific transport of S ‐nitrosocysteine in human red blood cells: Implications for formation of S ‐nitrosothiols and transport of NO bioactivity within the vasculature
Author(s) -
Sandmann Jörg,
Schwedhelm Kathrin S.,
Tsikas Dimitrios
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.06.040
Subject(s) - s nitrosoglutathione , cysteine , chemistry , cytosol , platelet , biochemistry , transporter , serine , glutathione , incubation , phosphorylation , biology , immunology , gene , enzyme
The transport of various S ‐nitrosothiols, NO and NO donors in human red blood cells (RBC) and the formation of erythrocytic S ‐nitrosoglutathione were investigated. Of the NO species tested only S ‐nitrosocysteine was found to form S ‐nitrosoglutathione in the RBC cytosol. l ‐Serine, l ‐cysteine and l ‐lysine inhibited formation of S ‐nitrosoglutathione. Incubation of RBC pre‐incubated with S ‐[ 15 N]nitroso‐ l ‐cysteine with native plasma or platelet‐rich plasma led to formation of S ‐[ 15 N]nitrosoalbumin and inhibited platelet aggregation, respectively. The specific transporter system of S ‐nitroso‐ l ‐cysteine in the RBC membrane may have implications for formation of S ‐nitrosoalbumin and S ‐nitrosohemoglobin and for transport of NO bioactivity within the vasculature.