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Fractalkine (CX3CL1) is synthesized as a type I transmembrane protein. Its unique CX(3)C chemokine domain is attached to a 241-amino acid mucin stalk, a 19-amino acid transmembrane domain, and a 37-amino acid intracellular domain of unknown function. A soluble form of fractalkine can be generated by proteolytic cleavage at the base of the mucin stalk. Novel monoclonal and polyclonal antibodies that specifically recognize only the amino- or carboxyl-terminal ends of the human fractalkine molecule have revealed that epithelial cells are the predominant cell type expressing transmembrane forms of fractalkine in human skin, the tonsil, and the large intestine. Using these specific anti-fractalkine reagents we do not detect high-level expression of fractalkine on endothelial cells in normal or inflamed colon samples obtained from patients with Crohn's disease or ulcerative colitis. In contrast to previous reports we do not detect fractalkine expression by Langerhans cells or immature dendritic cells in mucosal-associated lymphoid tissues in vivo. We show that the reagent used in previous studies, an anti-fractalkine N-terminal peptide antisera, cross-reacts with human CD84. Finally we discuss potential roles for fractalkine in constitutive leukocyte trafficking based on its observed pattern of expression in epithelia.

Type

Journal article

Journal

The American journal of pathology

Publication Date

03/2001

Volume

158

Pages

855 - 866

Addresses

Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.

Keywords

Colon, Epidermis, Cell Line, CHO Cells, Tumor Cells, Cultured, Epithelial Cells, Animals, Humans, Adenocarcinoma, Colorectal Neoplasms, Inflammatory Bowel Diseases, Peptides, Membrane Glycoproteins, Membrane Proteins, Protein Isoforms, Chemokines, CXC, Chemokines, CX3C, Antigens, CD, Antibodies, Antibody Specificity, Cross Reactions, Cricetinae, Keratins, Chemokine CX3CL1, Palatine Tonsil