TY - JOUR
T1 - Identification and characterization of a new pair of immunoglobulin-like receptors LMIR1 and 2 derived from murine bone marrow-derived mast cells
AU - Kumagai, Hidetoshi
AU - Oki, Toshihiko
AU - Tamitsu, Kaori
AU - Feng, Si Zhou
AU - Ono, Masao
AU - Nakajima, Hideaki
AU - Bao, Ying Chun
AU - Kawakami, Yuko
AU - Nagayoshi, Kazunari
AU - Copeland, Neal G.
AU - Gilbert, Debra J.
AU - Jenkins, Nancy A.
AU - Kawakami, Toshiaki
AU - Kitamura, Toshio
N1 - Funding Information:
This work was supported by grants from the Ministry of Education, Science, Sports and Culture, and the Ministry of Health and Welfare, Japan. This work was also supported in part by the National Cancer Institute, DHHS, USA. The division of Hematopoietic Factors is supported by Chugai Pharmaceutical. We also thank Anna Trivet for excellent technical assistance in chromosomal mapping and Mariko Ohara for language assistance.
PY - 2003/8/1
Y1 - 2003/8/1
N2 - We have identified and characterized two mouse cDNAs in a mouse antigen-stimulated bone marrow-derived mast cell cDNA library, both of which encode type I transmembrane proteins. The genes were closely mapped in the distal region of mouse chromosome 11 and expressed not only in mast cells but also widely in leukocytes. The extracellular domains of their encoded proteins contain a single variable immunoglobulin (Ig) motif sharing about 90% identity with amino acids, showing that they comprise a pair of molecules and belong to the Ig superfamily. We named these molecules leukocyte mono-Ig-like receptor1 and 2 (LMIR1 and 2). The intracellular domain of LMIR1 contains several immunoreceptor tyrosine-based inhibition motifs (ITIMs). When cross-linked, the intracellular domain was tyrosine phosphorylated and capable of recruiting tyrosine phosphatases, SHP-1 and SHP-2 and inositol polyphosphate 5-phosphatase, SHIP. LMIR2, on the other hand, contains a short cytoplasmic tail and a characteristic transmembrane domain carrying two positively charged amino acids associated with three kinds of immunoreceptor tyrosine-based activation motif (ITAM)-bearing molecules, DAP10, DAP12, and FcRγ. These findings suggest that a new pair of ITIM/ITAM-bearing receptors, LMIR1 and 2, regulate mast cell-mediated inflammatory responses through yet to be defined ligand(s).
AB - We have identified and characterized two mouse cDNAs in a mouse antigen-stimulated bone marrow-derived mast cell cDNA library, both of which encode type I transmembrane proteins. The genes were closely mapped in the distal region of mouse chromosome 11 and expressed not only in mast cells but also widely in leukocytes. The extracellular domains of their encoded proteins contain a single variable immunoglobulin (Ig) motif sharing about 90% identity with amino acids, showing that they comprise a pair of molecules and belong to the Ig superfamily. We named these molecules leukocyte mono-Ig-like receptor1 and 2 (LMIR1 and 2). The intracellular domain of LMIR1 contains several immunoreceptor tyrosine-based inhibition motifs (ITIMs). When cross-linked, the intracellular domain was tyrosine phosphorylated and capable of recruiting tyrosine phosphatases, SHP-1 and SHP-2 and inositol polyphosphate 5-phosphatase, SHIP. LMIR2, on the other hand, contains a short cytoplasmic tail and a characteristic transmembrane domain carrying two positively charged amino acids associated with three kinds of immunoreceptor tyrosine-based activation motif (ITAM)-bearing molecules, DAP10, DAP12, and FcRγ. These findings suggest that a new pair of ITIM/ITAM-bearing receptors, LMIR1 and 2, regulate mast cell-mediated inflammatory responses through yet to be defined ligand(s).
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U2 - 10.1016/S0006-291X(03)01245-2
DO - 10.1016/S0006-291X(03)01245-2
M3 - Article
C2 - 12893283
AN - SCOPUS:0043172587
SN - 0006-291X
VL - 307
SP - 719
EP - 729
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -