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J. Biol. Chem., Vol. 276, Issue 38, 35571-35580, September 21, 2001
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From the Interleukin (IL)-15 is able to regulate tight
junction formation in intestinal epithelial cells. However, the
mechanisms that regulate the intestinal barrier function in response to
IL-15 and the involved subunits of the IL-15 ligand-receptor system are
unknown. We determined the IL-2R
Interleukin-2 Receptor
Subunit-dependent and
-independent Regulation of Intestinal Epithelial Tight Junctions*
§,§,,,¶,, and
Gastrointestinal Unit, Department of
Medicine, Center for the Study of Inflammatory Bowel Disease,
Massachusetts General Hospital & Harvard Medical School, Boston,
Massachusetts 02114 and the ¶ Division of Gastroenterology, Albany
Medical College, Albany, New York 12208
subunit and
IL-15-dependent regulation of tight junction-associated
proteins in the human intestinal epithelial cell line T-84. The
IL-2R subunit was expressed and induced signal transduction in
caveolin enriched rafts in intestinal epithelial cells. IL-15-mediated
tightening of intestinal epithelial monolayers correlated with the
enhanced recruitment of tight junction proteins into Triton
X-100-insoluble protein fractions. IL-15-mediated up-regulation of ZO-1
and ZO-2 expression was independent of the IL-2R subunit, whereas
the phosphorylation of occludin and enhanced membrane association of
claudin-1 and claudin-2 by IL-15 required the presence of the
IL-2R subunit. Recruitment of claudins and hyperphosphorylated
occludin into tight junctions resulted in a more marked induction of
tight junction formation in intestinal epithelial cells than the
up-regulation of ZO-1 and ZO-2 by itself. The regulation of the
intestinal epithelial barrier function by IL-15 involves
IL-2R-dependent and -independent signaling pathways
leading to the recruitment of claudins, hyperphosphorylated occludin,
ZO-1, and ZO-2 into the tight junctional protein complex.
*
This work was supported by National Institutes of Health
Grants DK 51003 and DK 54427 (to H.C.R.), DK 21474 (to R. P. M.), DK 41557 (to D. K. P.), DK 43351 (to H. C. R.,
D. K. P., and R. P. M.), and PO1 DK 33506 (to
H. C. R.).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: Gastrointestinal
Unit, Jackson Bldg. R711, Massachusetts General Hospital, 32 Fruit St.,
Boston, MA 02114. E-mail:
reinecker@helix.mgh.harvard.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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