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J Biol Chem, Vol. 274, Issue 46, 32672-32679, November 12, 1999
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From the Recently, we identified the two myeloid related
protein-8 (MRP8) (S100A8) and MRP14 (S100A9) as fatty acid-binding
proteins (Klempt, M., Melkonyan, H., Nacken, W., Wiesmann, D.,
Holtkemper, U., and Sorg, C. (1997) FEBS Lett. 408, 81-84). Here we present data that the S100A8/A9 protein complex
represents the exclusive arachidonic acid-binding proteins in human
neutrophils. Binding and competition studies revealed evidence that (i)
fatty acid binding was dependent on the calcium concentration; (ii)
fatty acid binding was specific for the protein complex formed by
S100A8 and S100A9, whereas the individual components were unable to
bind fatty acids; (iii) exclusively polyunsaturated fatty acids were bound by S100A8/A9, whereas saturated (palmitic acid, stearic acid) and
monounsaturated fatty acids (oleic acid) as well as arachidonic
acid-derived eicosanoids (15-hydroxyeicosatetraenoic acid, prosta-
glandin E2, thromboxane B2, leukotriene
B4) were poor competitors. Stimulation of neutrophil-like
HL-60 cells with phorbol 12-myristate 13-acetate led to the secretion
of S100A8/A9 protein complex, which carried the released arachidonic
acid. When elevation of intracellular calcium level was induced by
A23187, release of arachidonic acid occurred without secretion of
S100A8/A9. In view of the unusual abundance in neutrophilic cytosol
(approximately 40% of cytosolic protein) our findings assign an
important role for S100A8/A9 as mediator between calcium signaling and
arachidonic acid effects. Further investigations have to explore the
exact function of the S100A8/A9-arachidonic acid complex both inside and outside of neutrophils.
Institut für Experimentelle
Dermatologie, Institut für
Molekularpharmakologie,
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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