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Papers In Press, published online ahead of print May 16, 2002
Laboratory of Cancer Biology and Molecular Immunolgy, Graduate School of Pharmaceutical Sciences, The University of Tokyo, Tokyo, Tokyo 113-0033
Corresponding Author: irimura{at}mol.f.u-tokyo.ac.jp
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 ETn. The mMGL2 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 RT-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.
J. Biol. Chem, 10.1074/jbc.M203774200
Submitted on April 18, 2002
Revised on May 16, 2002
Accepted on May 16, 2002
Molecular cloning and characterization of a novel mouse macrophage C-type lectin, mMGL2, which has a distinct carbohydrate specificity from mMGL1
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