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International Immunology Advance Access originally published online on August 28, 2006
International Immunology 2006 18(10):1499-1508; doi:10.1093/intimm/dxl083
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© The Japanese Society for Immunology. 2006. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

CMRF-35-like molecule-5 constitutes novel paired receptors, with CMRF-35-like molecule-1, to transduce activation signal upon association with FcR{gamma}

Masanori Fujimoto1,2, Hiroyuki Takatsu1,2 and Hiroshi Ohno1,2

1 Laboratory for Epithelial Immunobiology, Research Center for Allergy and Immunology, RIKEN, Yokohama 230-0045, Japan
2 Yokohama City University, 1-7-29 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan

Correspondence to: H. Ohno; E-mail: ohno{at}rcai.riken.jp

The murine CMRF-35-like molecule (CLM) family belongs to the Ig superfamily, and consists of nine mapped genes. Here we report that CLM-5 and CLM-1 constitute novel paired Ig-like receptors (PIRs). CLM-1 and CLM-5 genes are encoded in close vicinity on chromosome 11. CLM-1 has been reported to possess immunoreceptor tyrosine-based inhibitory motifs in its cytoplasmic region and to inhibit the differentiation of osteoclast. CLM-5 has an Ig domain that is highly homologous with that of CLM-1 in its extracellular domain, and possesses a negatively charged residue in its transmembrane domain. CLM-5, like CLM-1, is expressed in myeloid cells, such as dendritic cells, macrophages and granulocytes. We also show that CLM-5 interacts with FcR{gamma} to be expressed on the plasma membrane and that the cross-linking of CLM-5 leads to tyrosine phosphorylation of proteins, including FcR{gamma}, in the monocyte/macrophage cell line. Taken together, these characteristics suggest that CLM-1 and CLM-5 constitute novel PIRs and that CLM-5 may transduce activation signals as the activating receptor in myeloid cells.

Keywords: immunoglobulin superfamily, myeloid cells, RAW264.7, tyrosine phosphorylation

Transmitting editor: K. Okumura


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