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J Biol Chem, Vol. 274, Issue 7, 3994-3999, February 12, 1999
From the Institut für Pharmakologie,
Universitätsklinikum Essen, D-45122 Essen, Germany
Sphingosine-1-phosphate (SPP) produced from
sphingosine by sphingosine kinase has recently been reported to act as
intracellular second messenger for a number of plasma membrane
receptors. In the present study, we investigated whether the
sphingosine kinase/SPP pathway is involved in cellular signaling of the
Gi protein-coupled formyl peptide receptor in myeloid
differentiated human leukemia (HL-60) cells. Receptor activation
resulted in rapid and transient production of SPP by sphingosine
kinase, which was abolished after pertussis toxin treatment. Direct
activation of heterotrimeric G proteins by
AlF4
also rapidly increased SPP
formation in intact HL-60 cells. In cytosolic preparations of HL-60
cells, sphingosine kinase activity was stimulated by the stable GTP
analog, guanosine 5'-O-(3-thiotriphosphate). Inhibition of
sphingosine kinase by
DL-threo-dihydrosphingosine and
N,N-dimethylsphingosine did not affect
phospholipase C stimulation and superoxide production but markedly
inhibited receptor-stimulated Ca2+ mobilization and enzyme
release. We conclude that the formyl peptide receptor stimulates
through Gi-type G proteins SPP production by sphingosine
kinase, that the enzyme is also stimulated by direct G protein
activation, and that the sphingosine kinase/SPP pathway apparently
plays an important role in chemoattractant signaling in myeloid
differentiated HL-60 cells.
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