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M111078200v1
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Papers In Press, published online ahead of print May 30, 2002
J. Biol. Chem, 10.1074/jbc.M111078200
Submitted on November 19, 2001
Revised on May 28, 2002
Accepted on May 29, 2002

Phospholipase D activation by sphingosine-1-phosphate regulates interleukin-8 secretion in human bronchial epithelial cells

Rhett J. Cummings, Narasimham L. Parinandi, Ari Zaiman, Lixin Wang, Peter V. Usatyuk, Joe G. N. Garcia, and Viswanathan Natarajan

Medicine/Pulmonary & Critical Care, Johns Hopkins University School of Medicine, Baltimore, MD 21224

Corresponding Author: vnatara1{at}jhmi.edu

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 (HBEp) 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 phosphotidylbutanol 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 (PKC) and Rho kinase also attenuated S1P-induced IL-8 secretion. Our data suggest that PLD-derived PA, PKC and Rho are important signaling components in S1P-mediated IL-8 secretion by human bronchial epithelial cells.


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