CD23 (the low-affinity IgE receptor) as a C-type lectin: a multidomain and multifunctional molecule |
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Authors: | Kijimoto-Ochiai S |
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Institution: | (1) Institute of Immunology and Institute for Genetic Medicine, Hokkaido University, Sapporo 060-0815 (Japan), JP |
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Abstract: | This review, regards the low-affinity receptor CD23 as a C-type lectin and compares it with other C-type lectins and C-type
lectin-like receptors. C-type lectins such as the asialoglycoprotein receptor, as well as the dendritic cell immunoreceptor
and the dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin on dendritic cell lectin, possess amino
acid sequences which interact with Ca++ and sugar, and many of them possess an endocytosis signal sequence that includes tyrosine or serine in the cytoplasmic region.
In contrast, natural killer receptors lack the Ca++ and sugar-binding amino acids but conserve homologous cysteines in the form of C-type lectin, and possess an immunoreceptor
tyrosine-based inhibitory motif in the cytoplasmic region which inhibits killer activity when they recognize the self major
histocompatibility (MHC) class I molecule. Since human CD23a form has a similar amino acid sequence, the possibility that
this sequence is an endocytosis signal or an ITIM is discussed. The function of the reverse RGD and RGD-binding inhibitory
peptide in human CD23 from the point of view of the relation between a C-type lectin and MHC class II molecules is also considered.
Received 21 May 2001; received after revision 28 November 2001; accepted 29 November 2001 |
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Keywords: | , Low-affinity receptor for IgE, CD23, NK receptor, C-type lectin(-like) domain, inverse RGD sequence, RGD-binding,,,,,inhibitory peptide, ITIM, endocytosis signal, |
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