Effects of sulfur amino acids on tyrosyl or serine/threonine phosphorylation and translocation of cytosolic compounds to cell membrane in stimulus-treated human neutrophils.
We investigated the effects of various sulfur amino acids on the phosphorylation of proteins and the translocation of cytosolic compounds to cell membrane in stimulus-treated human neutrophils using specific monoclonal antibodies. D,L-homocysteine and D,L-homocysteine-thiolactone enhanced fMLP-induced tyrosyl phosphorylation of proteins and the translocation of p47phox, p67phox, and rac to the cell membrane in a concentration-dependent manner. L-cystathionine, NAc-L-cysteine and carboxymethylcysteine suppressed the tyrosyl phophorylation and translocation of cytosolic compounds to the cell membrane. L-cystathionine, L-cysteine and NAc-L-cysteine suppressed PMA-induced serine/threonine phosphorylation and the translocation of cytosolic compounds to the cell membrane. L-cysteine, NAc-L-cysteine and D,L-homocysteine enhanced AA-induced serine/threonine phosphorylation and the translocation of cytosolic compounds to the cell membrane, but L-cystathionine had opposite effects. These results indicated that the effects of sulfur amino acids on tyrosyl or serine/threonine phosphorylation and the translocation of p47phox, p67phox, and rac to the cell membrane in the stimulus-treated human neutrophils were in parallel with those of the stimulus-induced superoxide generation reported in previous paper. L-cysteine, D,L-homocysteine and L-cystathionine weakly inhibited lipid peroxidation, but the other sulfur amino acids tested had no effect.
Abe
Hidehiro
H
Department of Anesthesiology and Critical Care Medicine, Kochi Medical School, Nankoku, Kochi, Japan.
Liu
Gang
G
Chi
Haidong
H
He
Wenfei
W
Kitaoka
Noriko
N
Yamashita
Koichi
K
Kodama
Hiroyuki
H
D000603:Amino Acids, Sulfur / Q000494:pharmacology*; D000818:Animals; D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism*; D002478:Cells, Cultured; D006801:Humans; D015227:Lipid Peroxidation; D019255:NADPH Oxidases / Q000378:metabolism; D009504:Neutrophils / Q000166:cytology / Q000187:drug effects* / Q000378:metabolism; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation; D016897:Respiratory Burst; D012694:Serine / Q000378:metabolism*; D013481:Superoxides / Q000378:metabolism; D013912:Threonine / Q000378:metabolism*; D014443:Tyrosine / Q000378:metabolism*; D020744:rac GTP-Binding Proteins / Q000378:metabolism
D000603:Amino Acids, Sulfur; D010750:Phosphoproteins; C079789:neutrophil cytosol factor 67K; D013481:Superoxides; D013912:Threonine; D014443:Tyrosine; D012694:Serine; D019255:NADPH Oxidases; C060505:neutrophil cytosolic factor 1; D020744:rac GTP-Binding Proteins