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Rapid modification of ribosomal S6 kinase II (S6KII) in rabbit peritoneal neutrophils stimulated with chemotactic factor fMet‐Leu‐Phe
Author(s) -
Huang ChiKuang,
Coleman Herman,
Stevens Tim,
Liang Li
Publication year - 1994
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1002/jlb.55.4.430
Subject(s) - tyrosine phosphorylation , biology , phosphorylation , chemotaxis , microbiology and biotechnology , protein kinase c , cytochalasin b , ribosomal protein s6 , tyrosine kinase , tyrosine , biochemistry , phorbol , protein kinase a , protein phosphorylation , signal transduction , receptor , in vitro
The ribosomal S6 kinase II (S6KII) in rabbit neutrophils was studied by immunoblotting with antibodies prepared against recombinant S6KII. A protein with apparent molecular weight of 80,000 Da in SDS‐gel was recognized by the antibodies. A shift of the apparent molecular weight to 84,000 Da in SDS‐gel was observed in cells stimulated with the chemotactic factor fMet‐Leu‐Phe. Cytochalasin B and phorbol 12‐myristate 13‐acetate, but not A23187, stimulated both the tyrosine phosphorylation of p41 mapk and the change of the mobility of S6KII. Pretreatment of the cells with quin 2/AM inhibited almost completely the tyrosine phosphorylation of p41 mapk induced by fMet‐Leu‐Phe, but only partially the change in mobility of S6KII. Under various conditions, near maximum conversion of S6KII was observed even if only about 40% of the maximum level of tyrosine phosphorylation of p41 mapk was achieved. The results suggest that rapid modification of S6KII occurs in chemotactic factor‐stimulated neutrophils. Furthermore, the modification of S6KII induced by fMet‐Leu‐Phe requires either only partial tyrosine phosphorylation of p41 mapk or the activation of kinase(s) other than the p41 mapk isoform. J. Lcukoc. Biol . 55: 430–436; 1994.