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*
Gastrointestinal Unit, Department of Medicine, Center for the Study of Inflammatory Bowel Disease, Massachusetts General Hospital and Harvard Medical School, Boston, MA 02114;
Division of Gastroenterology, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA 02116; and
Division of Gastroenterology, Albany Medical College, Albany, NY 12208
Fractalkine is a unique chemokine that combines properties of both chemoattractants and adhesion molecules. Fractalkine mRNA expression has been observed in the intestine. However, the role of fractalkine in the healthy intestine and during inflammatory mucosal responses is not known. Studies were undertaken to determine the expression and function of fractalkine and the fractalkine receptor CX3CR1 in the human small intestinal mucosa. We identified intestinal epithelial cells as a novel source of fractalkine. The basal expression of fractalkine mRNA and protein in the intestinal epithelial cell line T-84 was under the control of the inflammatory mediator IL-1ß. Fractalkine was shed from intestinal epithelial cell surface upon stimulation with IL-1ß. Fractalkine localized with caveolin-1 in detergent-insoluble glycolipid-enriched membrane microdomains in T-84 cells. Cellular distribution of fractalkine was regulated during polarization of T-84 cells. A subpopulation of isolated human intestinal intraepithelial lymphocytes expressed the fractalkine receptor CX3CR1 and migrated specifically along fractalkine gradients after activation with IL-2. Immunohistochemistry demonstrated fractalkine expression in intestinal epithelial cells and endothelial cells in normal small intestine and in active Crohn’s disease mucosa. Furthermore, fractalkine mRNA expression was significantly up-regulated in the intestine during active Crohn’s disease. This study demonstrates that fractalkine-CX3CR1-mediated mechanism may direct lymphocyte chemoattraction and adhesion within the healthy and diseased human small intestinal mucosa.
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C. A. Haskell, M. D. Cleary, and I. F. Charo Unique Role of the Chemokine Domain of Fractalkine in Cell Capture. KINETICS OF RECEPTOR DISSOCIATION CORRELATE WITH CELL ADHESION J. Biol. Chem., October 27, 2000; 275(44): 34183 - 34189. [Abstract] [Full Text] [PDF]
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J. K. Harrison, A. M. Fong, P. A. W. Swain, S. Chen, Y.-R. A. Yu, M. N. Salafranca, W. B. Greenleaf, T. Imai, and D. D. Patel Mutational Analysis of the Fractalkine Chemokine Domain. BASIC AMINO ACID RESIDUES DIFFERENTIALLY CONTRIBUTE TO CX3CR1 BINDING, SIGNALING, AND CELL ADHESION J. Biol. Chem., June 8, 2001; 276(24): 21632 - 21641. [Abstract] [Full Text] [PDF]
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R. Nishiyama, T. Sakaguchi, T. Kinugasa, X. Gu, R. P. MacDermott, D. K. Podolsky, and H.-C. Reinecker Interleukin-2 Receptor beta Subunit-dependent and -independent Regulation of Intestinal Epithelial Tight Junctions J. Biol. Chem., September 14, 2001; 276(38): 35571 - 35580. [Abstract] [Full Text] [PDF]
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C.-L. Tsou, C. A. Haskell, and I. F. Charo Tumor Necrosis Factor-alpha -converting Enzyme Mediates the Inducible Cleavage of Fractalkine J. Biol. Chem., November 21, 2001; 276(48): 44622 - 44626. [Abstract] [Full Text] [PDF]
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