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J. Biol. Chem., Vol. 277, Issue 33, 30227-30235, August 16, 2002
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From the Department of Medicine, Division of Pulmonary and Critical
Care Medicine, The Johns Hopkins University,
Baltimore, Maryland 21224
Sphingosine 1-phosphate (S1P), a potent bioactive
sphingolipid, has been implicated in many critical cellular events,
including a regulatory role in the pathogenesis of airway inflammation. We investigated the participation of S1P as an inflammatory mediator by
assessing interleukin-8 (IL-8) secretion and phospholipase D (PLD)
activation in human bronchial epithelial cells (Beas-2B). S1P1, S1P3, S1P4,
S1P5, and weak S1P2 receptors were detected in
Beas-2B and primary human bronchial epithelial cells. S1P stimulated a
rapid activation of PLD, which was nearly abolished by pertussis toxin
(PTX) treatment, consistent with S1P receptor/Gi protein coupling. S1P also markedly induced Beas-2B secretion of IL-8, a
powerful neutrophil chemoattractant and activator, in a PTX-sensitive manner. This S1P-mediated response was dependent on transcription as
indicated by a strong induction of IL-8 promoter-mediated luciferase activity in transfected Beas-2B cells and a complete inhibition by
actinomycin D. Beas-2B exposure to 1-butanol, which converts the
PLD-generated phosphatidic acid (PA) to phosphatidylbutanol by a
transphosphatidylation reaction, significantly attenuated the
S1P-induced IL-8 secretion, indicating the involvement of PLD-derived
PA in the signaling pathway. Inhibition of
12-O-tetradecanoyl-phorbol-13-acetate-stimulated IL-8
production by 1-butanol further strengthened this observation. Blocking
protein kinase C and Rho kinase also attenuated S1P-induced IL-8
secretion. Our data suggest that PLD-derived PA, protein kinase C, and
Rho are important signaling components in S1P-mediated IL-8 secretion
by human bronchial epithelial cells.
Phospholipase D Activation by Sphingosine
1-Phosphate Regulates Interleukin-8 Secretion in Human Bronchial
Epithelial Cells*
*
This work was supported by National Institutes of Health
Grants HL47671 and HL71152 (to V. N.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: The Johns Hopkins
Asthma and Allergy Center, Division of Pulmonary and Critical Care
Medicine, 5501 Hopkins Bayview Circle, Baltimore, MD 21224. Tel.:
410-550-7748; Fax: 410-550-2612; E-mail: vnatara1@jhmi.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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