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Am J Physiol Gastrointest Liver Physiol 285: G223-G234, 2003. First published March 13, 2003; doi:10.1152/ajpgi.00445.2002
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MUCOSAL BIOLOGY

Intestinal epithelial CD23 mediates enhanced antigen transport in allergy: evidence for novel splice forms

Linda C. H. Yu,1 Guillaume Montagnac,2,3 Ping-Chang Yang,1 Daniel H. Conrad,4 Alexandre Benmerah,2,3 and Mary H. Perdue1

1Intestinal Disease Research Programme, McMaster University, Hamilton, Ontario, Canada L8N 3Z5; 2INSERM E9925, Faculté Necker, 75730 Paris; 3Department of Infectious Diseases, Cochin Institute, INSERM U567/CNRS UMP 8104, 75014 Paris, France; 4Department of Microbiology and Immunology, Virginia Commonwealth University, Richmond, Virginia 23298

Submitted 18 October 2002 ; accepted in final form 9 March 2003

We previously demonstrated enhanced transepithelial antigen transport in the intestine of allergic rodents associated with elevated expression of the low-affinity IgE receptor CD23 on enterocytes. Here, we examined the role of CD23 in the transport phenomenon using CD23/ mice and characterized the isoform of intestinal epithelial CD23. Jejunal segments of sensitized mice were challenged with antigen. Enhanced transepithelial antigen transport and transmucosal antigen flux were found in the intestine of sensitized CD23+/+ but not CD23/ mice. RT-PCR showed that enterocytes expressed only the isoform b of CD23. Sequencing revealed classic and alternative CD23b transcripts lacking exon 5 (b{Delta}5) or 6, all of which were translated into functional IgE receptors. The protein encoded by b{Delta}5 but not the classic b transcript was able to mediate the uptake of anti-CD23 or IgE, whereas both CD23 proteins were internalized after binding to IgE/antigen complexes. Our results suggest that the classic and alternative forms of CD23b display distinct endocytic properties, suggesting that they are likely to play different roles in transepithelial transport of IgE and allergens.

mouse; transgenic/knockout; mucosa; Fc receptors; antigen binding



Address for reprint requests and other correspondence: M. H. Perdue, IDRP, HSC 3N5C, McMaster Univ., 1200 Main St. W., Hamilton, ON, Canada L8N 3Z5 (E-mail: perdue{at}mcmaster.ca).




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