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J. Biol. Chem., Vol. 277, Issue 32, 28892-28901, August 9, 2002
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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 The nucleotide sequence(s) reported in this paper has been submitted to the DDBJ/GenBankTM/EBI Data Bank with accession number(s) AY103461, AY103462.
Molecular Cloning and Characterization of a Novel Mouse
Macrophage C-type Lectin, mMGL2, Which Has a Distinct Carbohydrate
Specificity from mMGL1*
,
- and 
-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.
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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