Reversible priming and protein-tyrosyl phosphorylation in human peripheral neutrophils under hypotonic conditions.
Hypotonic shock enhanced both formyl-methionyl-leucyl-phenylalanine (FMLP)-induced superoxide (O2-.) generation and tyrosyl phosphorylation of cellular proteins including 120-, 115-, 83-, 63-, and 54-kDa proteins of human peripheral neutrophils. The time course of the enhancement correlated with that of tyrosyl phosphorylation of the 115-kDa protein. The "primed state" was reversed to the nonprimed resting state by changing the conditions from hypotonic to isotonic, with a concomitant decrease in tyrosyl phosphorylation. Genistein inhibited the increase in both O2-. generation and tyrosyl phosphorylation of the 120-, 115-, 63-, and 54-kDa proteins. These results suggest the involvement of tyrosyl phosphorylation of a cellular protein(s) in hypotonic shock-induced priming of neutrophils.
Edashige
K
K
Institute for Laboratory Animals, Kochi Medical School, Japan.
Watanabe
Y
Y
Sato
E F
EF
Takehara
Y
Y
Utsumi
K
K
D000595:Amino Acid Sequence; D019833:Genistein; D006801:Humans; D007529:Isoflavones / Q000494:pharmacology; D008969:Molecular Sequence Data; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000494:pharmacology; D009504:Neutrophils / Q000187:drug effects / Q000201:enzymology / Q000378:metabolism*; D009997:Osmotic Pressure; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation; D019000:Phosphotyrosine; D011505:Protein-Tyrosine Kinases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013481:Superoxides / Q000378:metabolism*; D014443:Tyrosine / Q000031:analogs & derivatives / Q000378:metabolism
D007529:Isoflavones; D010750:Phosphoproteins; D013481:Superoxides; D019000:Phosphotyrosine; D014443:Tyrosine; D009240:N-Formylmethionine Leucyl-Phenylalanine; D019833:Genistein; D011505:Protein-Tyrosine Kinases