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Identification and characterization of a new pair of immunoglobulin-like receptors LMIR1 and 2 derived from murine bone marrow-derived mast cells

  1. Author:
    Kumagai, H.
    Oki, T.
    Tamitsu, K.
    Feng, S. Z.
    Ono, M.
    Nakajima, H.
    Bao, Y. C.
    Kawakami, Y.
    Nagayoshi, K.
    Copeland, N. G.
    Gilbert, D. J.
    Jenkins, N. A.
    Kawakami, T.
    Kitamura, T.

  2. Author Address

    Univ Tokyo, Inst Med Sci, Div Cell Therapy, Adv Clin Res Ctr,Minato Ku, 6-1 Shirokanedai 4 Chome, Tokyo 1088639, Japan Univ Tokyo, Inst Med Sci, Div Cell Therapy, Adv Clin Res Ctr,Minato Ku, Tokyo 1088639, Japan Univ Tokyo, Inst Med Sci, Div Hematopoiet Factors, Adv Clin Res Ctr,Minato Ku, Tokyo 1088639, Japan Chugai Pharmaceut Co Ltd, Toshima Ku, Tokyo 1718545, Japan Ehime Univ, Sch Med, Dept Pathol 2, Shigenobu, Ehime 7910295, Japan La Jolla Inst Allergy Immunol, Div Allergy, San Diego, CA 92121 USA NCI, Frederick Canc Res & Dev Ctr, Mouse Canc Genet Program, Frederick, MD 21702 USA Kitamura T Univ Tokyo, Inst Med Sci, Div Cell Therapy, Adv Clin Res Ctr,Minato Ku, 6-1 Shirokanedai 4 Chome, Tokyo 1088639, Japan
    1. Year: 2003
  2. Journal: Biochemical and Biophysical Research Communications
    1. 307
    2. 3
    3. Pages: 719-729
  4. Type of Article: Article
  1. Abstract:

    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 I I 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 FcRgamma. 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). (C) 2003 Elsevier Inc. All rights reserved.

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