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CD1D is the humangene that encodes the proteinCD1d,[1] a member of the CD1 (cluster of differentiation 1) family of glycoproteins expressed on the surface of various human antigen-presenting cells. They are non-classical MHC proteins, related to the class I MHC proteins, and are involved in the presentation of lipid antigens to T cells. CD1d is the only member of the group 2 CD1 molecules.
α-galactosylceramide (α-GalCer), a compound originally derived from the marine sponge Agelas mauritanius[2] with no physiological role but great research utility.
iGb3, a self antigen which has been implied in iNKT selection.[4]
HS44, a synthetic amino cyclitolic ceramide analogue which has less contact with the TCR, activating iNKTs in a more constrained way than α-GalCer (specially in relation to Th2 cytokines production) and thus being more interesting for therapeutic use.[5]
CD1d tetramers
CD1d tetramers are protein constructs composed of four CD1d molecules joined together and usually fluorescently labelled, used to identify NKT cells or other CD1d-reactive cells. In particular, type I NKT cells and some type II NKT cells are stained by them. A differentiation of these two types can be obtained in human by using an antibody against the TCR Vα24 chain, which is specific of type I NKT cells.[6]
Although they are the most widely used of CD1d oligomers, sometimes CD1d dimers (two units) or pentamers (five units) are used instead.[6]
Melián A, Beckman EM, Porcelli SA, Brenner MB (1996). "Antigen presentation by CD1 and MHC-encoded class I-like molecules". Curr. Opin. Immunol. 8 (1): 82–8. doi:10.1016/S0952-7915(96)80109-9. PMID8729450.
Joyce S (2001). "CD1d and natural T cells: how their properties jump-start the immune system". Cell. Mol. Life Sci. 58 (3): 442–69. doi:10.1007/PL00000869. PMID11315191.
Blumberg RS, Terhorst C, Bleicher P, et al. (1991). "Expression of a nonpolymorphic MHC class I-like molecule, CD1D, by human intestinal epithelial cells". J. Immunol. 147 (8): 2518–24. PMID1717564.
Balk SP, Burke S, Polischuk JE, et al. (1994). "Beta 2-microglobulin-independent MHC class Ib molecule expressed by human intestinal epithelium". Science. 265 (5169): 259–62. doi:10.1126/science.7517575. PMID7517575.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Kawano T, Cui J, Koezuka Y, et al. (1997). "CD1d-restricted and TCR-mediated activation of valpha14 NKT cells by glycosylceramides". Science. 278 (5343): 1626–9. doi:10.1126/science.278.5343.1626. PMID9374463.
Katabami S, Matsuura A, Chen HZ, et al. (1998). "Structural organization of rat CD1 typifies evolutionarily conserved CD1D class genes". Immunogenetics. 48 (1): 22–31. doi:10.1007/s002510050396. PMID9601940.
Somnay-Wadgaonkar K, Nusrat A, Kim HS, et al. (1999). "Immunolocalization of CD1d in human intestinal epithelial cells and identification of a beta2-microglobulin-associated form". Int. Immunol. 11 (3): 383–92. doi:10.1093/intimm/11.3.383. PMID10221650.
Campbell NA, Kim HS, Blumberg RS, Mayer L (1999). "The nonclassical class I molecule CD1d associates with the novel CD8 ligand gp180 on intestinal epithelial cells". J. Biol. Chem. 274 (37): 26259–65. doi:10.1074/jbc.274.37.26259. PMID10473580.