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J. Biol. Chem., Vol. 278, Issue 13, 10879-10884, March 28, 2003
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From the INSERM U454, Department of Respiratory Disease, Centre
Hospitalier Universitaire Arnaud de Villeneuve, 34295 Montpellier Cedex
05, France
Lipoxins are biologically active
eicosanoids possessing anti-inflammatory properties. Using a
calcium imaging system we investigated the effect of lipoxin
A4 (LXA4) on intracellular
[Ca2+] ([Ca2+]i) of human
bronchial epithelial cell. Exposure of the cells to
LXA4 produced a dose-dependent increase in
[Ca2+]i followed by a recovery to basal
values in primary culture and in 16HBE14o
Lipoxin A4 Stimulates a Cytosolic Ca2+
Increase in Human Bronchial Epithelium*
cells.
The LXA4-induced [Ca2+]i increase
was completely abolished after pre-treatment of the 16HBE14o cells with pertussis toxin (G-protein
inhibitor). The [Ca2+]i response was not
affected by the removal of external [Ca2+] but completely
inhibited by thapsigargin (Ca2+-ATPase inhibitor)
treatment. Pre-treatment of the bronchial epithelial cells with either
MDL hydrochloride (adenylate cyclase inhibitor) or
(Rp)-cAMP (cAMP-dependent
protein kinase inhibitor) inhibited the Ca2+ response to
LXA4. However, the response was not affected by
chelerytrine chloride (protein kinase C inhbitor) or montelukast
(cysteinyl leukotriene receptor antagonist). The LXA4
receptor mRNA was detected, by RT-PCR, in primary culture of human
bronchial epithelium and in immortalized 16HBE14o cells.
The functional consequences of the effect of LXA4 on
intracellular [Ca2+]i have been investigated
on Cl secretion, measured using the short-circuit
techniques on 16HBE14o monolayers grown on permeable
filters. LXA4 produced a sustained stimulation of
the Cl secretion by 16HBE14o monolayers,
which was inhibited by BAPTA-AM, a chelator of intracellular calcium.
Taken together our results provided evidence for the stimulation of a
[Ca2+]i increase by LXA4 through
a mechanism involving its specific receptor and protein kinase
A activation and resulting in a subsequent Ca2+-dependent Cl secretion by
human airway epithelial cells.
*
This work was funded by The Wellcome Trust
(055695/Z/98/Z/CH/TG/JF), Convention Industrielle de Formation par la
Recherche research Grant 99679, the Fondation Institut de
France, and the Regional Council of Languedoc, Roussillon, France.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: INSERM U454, CHU
Arnaud de Villeneuve, 34295 Montpellier Cedex 05, France. Tel.: 33-4-67-33-59-31; Fax: 33-4-67-63-28-55; E-mail:
urbach@montp.inserm.fr.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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