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• W1507222022 abstract "NK cell mediated cytotoxicity is suppressed upon specific recognition of target MHC class I molecules (Ljunggren and Kärre 1990). It is currently thought that the control of NK cell activity depends on a subtle balance between inhibitory and activating signals; accordingly, every mature NK cell should bear at least one type of dominant inhibitory receptor for a self MHC class I product, thus preventing autoreactivity against normal cells. Recognition of H-2 products is mediated by members of the Ly-49 C-type lectin family (Yoxoyama 1995). In humans several inhibitory NK cell receptors (NKR) encoded by an immunoglobulin (Ig)-related multigene family specifically interact with different HLA class I allotypes (Colonna and Samaridis 1995; Wagtmann et al. 1995; Lanier and Phillips 1995; Moretra et al. 1996), and the term killer inhibitory receptors (KIRs) has been proposed. A common structural feature of the inhibitory NKR is the presence of cytoplasmic “immunoreceptor tyrosine-based inhibitory motifs” (ITIMs, V/IxYxxL sequences) which upon their tyrosine phosphorylation recruit protein tyrosine phosphatases (SHP-1 and SHP-2) involved in the downregulation of NK cell activity (Burshtyn et al. 1996; Campbell et al. 1996; Fry et al. 1996; Olcese et al. 1996). Remarkably, other members of the Ig superfamily (Ig-SF) NKR trigger NK cell mediated lysis upon their ligation by specific monoclonal antibodies (mAbs). These activating receptors (p50) are closely homologous to inhibitory molecules (p58) but contain shorter intracytoplasmic domains lacking ITIMs and display a different transmembrane region (Moretta et al. 1996)." @default.
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• W1507222022 date "1998-01-01" @default.
• W1507222022 modified "2023-10-16" @default.
• W1507222022 title "The CD94/NKG2 C-Type Lectin Receptor Complex" @default.
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• W1507222022 doi "https://doi.org/10.1007/978-3-642-46859-9_4" @default.
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