Document Detail


Molecular cloning and characterization of a novel mouse macrophage C-type lectin, mMGL2, which has a distinct carbohydrate specificity from mMGL1.
MedLine Citation:
PMID:  12016228     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Makoto Tsuiji; Mayuko Fujimori; Yoshimi Ohashi; Nobuaki Higashi; Thandi M Onami; Stephen M Hedrick; Tatsuro Irimura
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2002-05-16
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  277     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2002 Aug 
Date Detail:
Created Date:  2002-08-05     Completed Date:  2002-09-09     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  28892-901     Citation Subset:  IM    
Affiliation:
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.
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MeSH Terms
Descriptor/Qualifier:
3' Untranslated Regions
Amino Acid Sequence
Animals
Antibodies, Monoclonal / metabolism
Asialoglycoproteins
Base Sequence
Carbohydrate Metabolism
Cell Line
Cloning, Molecular
Cytoplasm / metabolism
DNA, Complementary / metabolism
Dose-Response Relationship, Drug
Endocytosis
Exons
Female
Hydrogen-Ion Concentration
Immunohistochemistry
Lectins / biosynthesis*,  genetics*,  metabolism*
Lectins, C-Type*
Macrophages / metabolism*
Membrane Proteins*
Mice
Mice, Inbred C57BL
Molecular Sequence Data
Phylogeny
Protein Binding
Protein Structure, Tertiary
RNA, Messenger / metabolism
Recombinant Fusion Proteins / metabolism
Recombinant Proteins / metabolism
Reverse Transcriptase Polymerase Chain Reaction
Sequence Homology, Amino Acid
Tissue Distribution
Chemical
Reg. No./Substance:
0/3' Untranslated Regions; 0/Antibodies, Monoclonal; 0/Asialoglycoproteins; 0/DNA, Complementary; 0/Lectins; 0/Lectins, C-Type; 0/MGL2 protein, mouse; 0/Membrane Proteins; 0/Mgl1 protein, mouse; 0/RNA, Messenger; 0/Recombinant Fusion Proteins; 0/Recombinant Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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