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J. Biol. Chem., Vol. 260, Issue 6, 3321-3329, Mar, 1985
EL Thomas, MB Grisham, DF Melton and MM Jefferson
Production of hydrogen peroxide and secretion of myeloperoxidase by
stimulated neutrophils resulted in myeloperoxidase-catalyzed oxidation of
chloride to hypochlorous acid (HOCl), the reaction of HOCl with taurine to
yield taurine monochloramine (TauNHCl), and accumulation of TauNHCl in the
extracellular medium. When erythrocytes were present, the yield of TauNHCl
was lower as the result of uptake of TauNHCl into erythrocytes. The
zwitterion taurine was not taken up, but the anion TauNHCl and other
anionic oxidants including taurine dichloramine (TauNCl2) and L-alanine
chloramines were transported into erythrocytes by the anion-transport
system. Oxidation of intracellular components such as glutathione (GSH) by
taurine chloramines resulted in reduction of the chloramines and trapping
of taurine within erythrocytes. At high oxidant:erythrocyte ratios, TauNHCl
also oxidized hemoglobin (Hb) and depleted ATP, but caused little lysis.
TauNCl2 was much more effective as a lytic agent. At low
oxidant:erythrocyte ratios, the chloramines caused net loss of GSH when no
glucose was provided, but Hb was not oxidized and GSH content returned to
normal when glucose was added. Therefore, anionic chloramines may mediate
oxidative toxicity when the neutrophil:erythrocyte ratio is high. Under
more physiologic conditions, chlorination of taurine by neutrophils and the
uptake and reduction of TauNHCl by erythrocytes prevents accumulation of
oxidants and may protect blood cells, plasma components, and tissues
against oxidative toxicity.
Evidence for a role of taurine in the in vitro oxidative toxicity of neutrophils toward erythrocytes
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