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Blood, Vol. 95 No. 11 (June 1), 2000:
pp. 3541-3547
Pleiotropic role of lyn kinase in leukotriene
B4-induced eosinophil activation
Oonagh T. Lynch,
Mark A. Giembycz,
Ian Daniels,
Peter J. Barnes, and
Mark A. Lindsay
From Thoracic Medicine, Imperial College School of Medicine at the
National Heart and Lung Institute, London, and Medical Research Centre,
City Hospital, Nottingham, United Kingdom.
The authors have examined the role of the src-family of protein
tyrosine kinases in leukotriene B4
(LTB4)-induced activation of guinea-pig eosinophils.
Western blot analysis identified the src-like protein tyrosine kinases
p53lyn, p56lyn, p56/59hck,
p55fgr, and p56lck whereas p60src,
p62yes, p55blk, and p59fyn were not
detected. LTB4 promoted a rapid increase in
p53/56lyn activity in eosinophils, which peaked at 5 seconds and remained elevated at 60 seconds; hck, fgr, and lck were not
activated. A role for p53/56lyn in eosinophil activation
was investigated with the use of the src-selective inhibitor
PP1 (1 µmol/L to 10 µmol/L), which attenuated LTB4-stimulated
p53/56lyn activity and the phosphorylation of extracellular
signal-regulated kinase-2 in intact cells. At comparable
concentrations, PP1 was also shown to attenuate
LTB4-induced nicotinamide adenine dinucleotide phosphate
(reduced form) (NADPH) oxidase activation, chemotaxis, and
Ca++-dependent [3H]arachidonic acid (AA)
release. Moreover, an inhibitor of mitogen-activated protein kinase
kinase-1, PD 098059, significantly inhibited LTB4-induced chemotaxis but had no effect on oxidant production or
[3H]AA release. Collectively, these results implicate lyn
kinase in LTB4-induced eosinophil activation through the
recruitment of divergent cell-signaling pathways.
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