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J. Biol. Chem., Vol. 279, Issue 47, 49274-49280, November 19, 2004

This Article Full Text Full Text (PDF) All Versions of this Article: 279/47/49274    most recent M409300200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kumamoto, Y. Articles by Irimura, T. Search for Related Content PubMed PubMed Citation Articles by Kumamoto, Y. Articles by Irimura, T. Social Bookmarking                      What's this?

Identification of Sialoadhesin as a Dominant Lymph Node Counter-receptor for Mouse Macrophage Galactose-type C-type Lectin 1^*

Yosuke Kumamoto, Nobuaki Higashi, Kaori Denda-Nagai, Makoto Tsuiji, Koji Sato, Paul R. Crocker, and Tatsuro Irimura¶

From the Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo 113-0033, Japan and The Wellcome Trust Biocentre, School of Life Sciences, University of Dundee, Dundee DD1 5EH, United Kingdom

In the sensitization phase of contact hypersensitivity in mice, dermal macrophages (MØs) expressing MØ galactose-type C-type lectin1 (MGL1) are known to migrate from the dermis to lymph nodes (LNs) where they accumulate in the subcapsular sinus, interfollicular regions, and areas surrounding high endothelial venules. We hypothesize that the interactions between MGL1 and its ligands determine the localizations of MGL1-positive cells within the LNs. In the present study, our major aim was to isolate MGL1 counter-receptor(s) from lysates of LNs using affinity chromatography with immobilized recombinant MGL1. Fractions bound and eluted with EDTA were analyzed by SDS-PAGE and matrix-assisted laser desorption ionization time-of-flight mass spectrometry. One of the predominant components was sialoadhesin (Sn, Siglec-1). Sn from lysates of LNs was immobilized on microtiter plates precoated with anti-Sn monoclonal antibody, and binding of recombinant MGL1 and adhesion of cells expressing MGL1 were tested. The binding of recombinant MGL1 to Sn was shown to be dependent on Ca²⁺ and N-glycans on Sn. MGL1-transfected Chinese hamster ovary cells adhered to the Sn-coated plates, whereas mock transfectants did not. Immunohistochemical localization of anti-Sn monoclonal antibody in LN coincided with the subcapsular sinus area to which recombinant MGL1 was bound. Furthermore, the distribution of MGL1+ cells after sensitization with FITC was demonstrated to overlap with that of Sn within the subcapsular sinus of draining LNs. These results suggest that Sn acts as an endogenous counter-receptor for MGL1.

Received for publication, August 13, 2004 , and in revised form, September 10, 2004.

^* This work was supported by grants-in-aid from the Ministry of Education, Science, Sports and Culture of Japan (09254101, 11557180, 11672162, and 12307054), the Research Association for Biotechnology, Special Coordination Funds for Promoting Science and Technology of the Ministry of Education, Culture, Sports, Science and Technology, the Program for Promotion of Basic Research Activities for Innovative Biosciences, the Program for Promotion of Fundamental Studies in Health Sciences of the Organization for Pharmaceutical Safety and Research, and the Wellcome Trust. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed: Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo 113-0033, Japan. Tel.: 81-3-5841-4870; Fax: 81-3-5841-4879; E-mail: irimura{at}mol.f.u-tokyo.ac.jp.

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