Fanger N A, Cosman D, Peterson L, Braddy S C, Maliszewski C R, Borges L
Immunex Corporation, Seattle, Washington 98101, USA.
Eur J Immunol. 1998 Nov;28(11):3423-34. doi: 10.1002/(SICI)1521-4141(199811)28:11<3423::AID-IMMU3423>3.0.CO;2-2.
The MHC class I binding proteins leukocyte immunoglobulin-like receptor (LIR)-1 and -2 recognize a similar broad spectrum of HLA-A, -B and -C alleles but are differentially expressed in lymphocytes, monocytes, and dendritic cells. In monocytes, phosphorylation of LIR-1 and LIR-2 results in the binding of the tyrosine phosphatase SHP-1. Coligation of either LIR with Fcgamma receptor I (CD64) inhibits tyrosine phosphorylation of the associated Fc receptor gamma chain and Syk molecules, as well as intracellular calcium mobilization. These findings suggest that LIR-1 and LIR-2 function as unique MHC class I receptors involved in the inhibition or down-modulation of monocyte activation signals, particularly those mediated through the receptors for IgG, IgE and IgA.
MHC I类结合蛋白白细胞免疫球蛋白样受体（LIR）-1和-2识别相似的广泛HLA-A、-B和-C等位基因谱，但在淋巴细胞、单核细胞和树突状细胞中差异表达。在单核细胞中，LIR-1和LIR-2的磷酸化导致酪氨酸磷酸酶SHP-1的结合。LIR与Fcγ受体I（CD64）的共结合抑制相关Fc受体γ链和Syk分子的酪氨酸磷酸化以及细胞内钙动员。这些发现表明，LIR-1和LIR-2作为独特的MHC I类受体，参与单核细胞激活信号的抑制或下调，特别是那些通过IgG、IgE和IgA受体介导的信号。
