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J. Biol. Chem., Vol. 276, Issue 38, 35258-35264, September 21, 2001
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From the Sphingolipids have been implicated
in the regulation of cell growth, differentiation, and programmed cell
death. Sphingosine 1-phosphate (SPP) has recently emerged as an
important lipid messenger and a ligand for the endothelial
differentiation gene receptor family of proteins through which it
mediates its biologic effects. Recent studies in Saccharomyces
cerevisiae in our laboratory implicated the yeast oligomycin
resistance gene (YOR1), a member of the ATP binding cassette family of
proteins, in the transport of SPP. The cystic fibrosis transmembrane
regulator is a unique member of the ATP binding cassette transporter
family and has high homology with YOR1. We therefore set out to
investigate if this member of the family can regulate SPP transport. We
demonstrate that C127/cystic fibrosis transmembrane regulator (CFTR)
cells, expressing wild type CFTR, exhibited significantly higher uptake
of sphingosine 1-phosphate than either cells expressing a mutant CFTR
C127/
Cystic Fibrosis Transmembrane Regulator Regulates Uptake of
Sphingoid Base Phosphates and Lysophosphatidic Acid
MODULATION OF CELLULAR ACTIVITY OF SPHINGOSINE 1-PHOSPHATE*
§,
,§§
Division of General Internal
Medicine, Ralph H. Johnson Veterans Administration Hospital,
Charleston, South Carolina 29401-5799, the Departments of
¶ Medicine and ** Biochemistry and Molecular Biology and
the Division of Pediatric Gastroenterology and Nutrition,
Medical University of South Carolina, Charleston, South Carolina 29425, and the Department of Internal Medicine, Duke University Medical
Center, Durham, North Carolina 27710
F508 or C127/mock-transfected cells. This effect was specific,
dose-dependent, and competed off by dihydrosphingosine
1-phosphate and lysophosphatidic acid. There was no difference in
uptake of sphingosine, C16-ceramide, sphingomyelin,
lysophingomyelin, phosphatidylcholine, lysophosphatidylcholine, or
phosphatidic acid among the different cell lines. Pretreatment with
forskolin or isobutylmethylxanthine to stimulate cAMP did not affect
the uptake in any of the cell lines. Moreover, we found that
mitogen-activated protein kinase activation by SPP was less responsive
in C127/CFTR as compared with C127/mock-transfected cells, suggesting
that uptake of SPP by CFTR may divert it from interacting with its cell
surface receptors and attenuate signaling functions. Taken together,
these data implicate CFTR in uptake of SPP and the related
phosphorylated lipids dihydrosphingosine 1-phosphate and
lysophosphatidic acid. This uptake influences the availability of SPP
to modulate biologic activity via endothelial differentiation gene
receptors. These studies may have important implications to
cystic fibrosis.
*
This work was supported by National Institutes of Health
Grants R01-GM43825 (to Y. A. H.) and R01-GM62887 (to L. M. O.).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.
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