R. Rezzonico et al., INTERLEUKIN-6 STIMULATES IS A TYROSINE KINASE-ACTIVITY POTENTIALLY INVOLVED IN MOUSE HYBRIDOMA CELL-GROWTH, Cytokine, 9(2), 1997, pp. 93-100
In this report the authors describe the characterization of a cytosoli
c tyrosine kinase activity (IL-6PTK) stimulated by interleukin 6 (IL-6
), IL-6PTK appears 6 h after IL-6 addition and is inhibited by tyrphos
tin but not genistein, It is active under its phosphorylated form alth
ough it is not immunoprecipitated by antiphosphotyrosine antibodies, s
uggesting that autophosphorylation occurs on residues other than tyros
ine. Using the ATP-binding site covalent label, 5'-p-fluorosulfonylben
zoyladenosine (FSBA), two phosphoproteins have been identified of 52 a
nd 59 kDa respectively, that could potentially harbour IL-6PTK activit
y, The intracellular elevation of cAMP, which inhibits 7TD1 cell proli
feration, decreases as the same time IL-6PTK activity suggesting that
the cAMP-dependent kinase could act as a negative regulator of this ty
rosine kinase species, Taken together the results strongly suggest tha
t a tyrosine kinase (IL-6PTK) might be involved in the cascade of even
ts leading to the proliferation of 7TD1 cells under IL-6 stimulation.
(C) 1997 Academic Press Limited.