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Originally published In Press as doi:10.1074/jbc.M203774200 on May 16, 2002

J. Biol. Chem., Vol. 277, Issue 32, 28892-28901, August 9, 2002
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Molecular Cloning and Characterization of a Novel Mouse Macrophage C-type Lectin, mMGL2, Which Has a Distinct Carbohydrate Specificity from mMGL1*

Makoto Tsuiji, Mayuko FujimoriDagger , Yoshimi Ohashi, Nobuaki Higashi, Thandi M. Onami§, Stephen M. Hedrick§, and Tatsuro Irimura

From the Laboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo 113-0033, Japan and the § Cancer Center and the Division of Biology, University of California, San Diego, La Jolla, California 92093-0687

A novel mouse macrophage galactose-type C-type lectin 2 (mMGL2) was identified by BLAST analysis of expressed sequence tags. The sequence of mMGL2 is highly homologous to the mMGL, which should now be called mMGL1. The open reading frame of mMGL2 contains a sequence corresponding to a type II transmembrane protein with 332 amino acids having a single extracellular C-type lectin domain. The 3'-untranslated region included long terminal repeats of mouse early transposon. The Mgl2 gene was cloned from a 129/SvJ mouse genomic library and sequenced. The gene spans 7,136 base pairs and consists of 10 exons, which is similar to the genomic organization of mMGL1. The reverse transcriptase-PCR analysis indicates that mMGL2 is expressed in cell lines and normal mouse tissues in a macrophage-restricted manner, also very similar to that of mMGL1. The mMGL2 mRNA was also detected in mMGL1-positive cells, which were sorted from thioglycollate-induced peritoneal cells with a mMGL1-specific monoclonal antibody, LOM-8.7. The soluble recombinant proteins of mMGL2 exhibited carbohydrate specificity for alpha - and beta -GalNAc-conjugated soluble polyacrylamides, whereas mMGL1 preferentially bound Lewis X-conjugated soluble polyacrylamides in solid phase assays. These two lectins may function cooperatively as recognition and endocytic molecules on macrophages and related cells.

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

The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBankTM/EBI Data Bank with accession number(s) AY103461, AY103462.

Dagger Present address: Dept. of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, 113-8657, Japan.

To whom correspondence should be addressed. Tel.: 813-5841-4870; Fax: 813-5841-4879; E-mail: irimura@mol.f.u-tokyo.ac.jp.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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