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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
28
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pubmed:dateCreated |
1991-11-8
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pubmed:abstractText |
Mac-2, a galactose-binding lectin secretion by activated macrophages, is the major non-integrin laminin-binding protein in these cells. Mac-2 is also expressed by epithelial cells in the intestine and kidney. We wished to identify intestinal glycoproteins other than laminin that have a high affinity for Mac-2 and that could be considered as candidate ligands or partners for this lectin in intestinal epithelium. Certain lines of human colon adenocarcinoma cells produce two Mac-2-binding glycoproteins (M2BP-1 and M2BP-2) that were identified by their avid association with Mac-2 following detergent lysis and immunoprecipitation. These glycoproteins do not share a common epitope with Mac-2, and the interaction between Mac-2 and these proteins is mediated through the carbohydrate-binding domain of Mac-2 and sugar moieties on M2BP-1 and M2BP-2. M2BP-1 (98 kDa) and M2BP-2 (70 kDa) were purified by immunoaffinity chromatography and were specifically eluted with either galactose or lactose. Peptide maps revealed that M2BP-1 and M2BP-2 are structurally related. M2BP-1 is secreted and could conceivably associate with Mac-2 extracellularly. N-terminal sequence analysis of M2BP-2 suggests that these glycoproteins represent a unique subset of candidate ligands for this mammalian beta-galactoside lectin.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation,
http://linkedlifedata.com/resource/pubmed/chemical/Galactosides,
http://linkedlifedata.com/resource/pubmed/chemical/Galectin 3,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/beta-galactoside
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
|
pubmed:volume |
266
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18731-6
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:1917996-Adenocarcinoma,
pubmed-meshheading:1917996-Amino Acid Sequence,
pubmed-meshheading:1917996-Antigens, Differentiation,
pubmed-meshheading:1917996-Blotting, Western,
pubmed-meshheading:1917996-Colon,
pubmed-meshheading:1917996-Epithelial Cells,
pubmed-meshheading:1917996-Epithelium,
pubmed-meshheading:1917996-Galactosides,
pubmed-meshheading:1917996-Galectin 3,
pubmed-meshheading:1917996-Glycoproteins,
pubmed-meshheading:1917996-Humans,
pubmed-meshheading:1917996-Lectins,
pubmed-meshheading:1917996-Ligands,
pubmed-meshheading:1917996-Macrophages,
pubmed-meshheading:1917996-Molecular Sequence Data,
pubmed-meshheading:1917996-Precipitin Tests,
pubmed-meshheading:1917996-Tumor Cells, Cultured
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pubmed:year |
1991
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pubmed:articleTitle |
Mac-2-binding glycoproteins. Putative ligands for a cytosolic beta-galactoside lectin.
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pubmed:affiliation |
Molecular Immunology Laboratory, Massachusetts General Hospital, Boston.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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