rdf:type |
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lifeskim:mentions |
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pubmed:issue |
19
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pubmed:dateCreated |
1996-11-21
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pubmed:abstractText |
Galectin-3 is a beta-galactoside-specific lectin implicated in diverse processes involved in cellular interactions. Recently, the Mac-2-binding protein, a heavily N-glycosylated secreted protein with a subunit Mr of 97,000, was identified as its ligand. The present study characterizes the interaction between galectin-3 and Mac-2-binding protein in whole cells and measures their relative expression levels. Incubation of A375 cells with affinity-purified Mac-2-binding protein resulted in its binding to galectin-3 on the cell surface in a specific carbohydrate-dependent manner. Mac-2-binding protein also induced homotypic cell aggregation, which was inhibited by lactose or Fab' fragments of an anti-galectin-3 antibody. Northern blotting analysis revealed differences in the transcriptional regulation of galectin-3 and Mac-2-binding protein. These results provide the first direct evidence for a Mac-2-binding protein function and suggest that it may play a role in tumor cell embolization during metastasis through interaction with galectin-3.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Neoplasm,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Galectin 3,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/LGALS3BP protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Markers, Biological
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0008-5472
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
56
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4530-4
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:8813152-Antigens, Differentiation,
pubmed-meshheading:8813152-Antigens, Neoplasm,
pubmed-meshheading:8813152-Blotting, Northern,
pubmed-meshheading:8813152-Breast Neoplasms,
pubmed-meshheading:8813152-Carrier Proteins,
pubmed-meshheading:8813152-Cell Adhesion,
pubmed-meshheading:8813152-Cell Aggregation,
pubmed-meshheading:8813152-DNA, Complementary,
pubmed-meshheading:8813152-Female,
pubmed-meshheading:8813152-Galectin 3,
pubmed-meshheading:8813152-Gene Expression Regulation, Neoplastic,
pubmed-meshheading:8813152-Glycoproteins,
pubmed-meshheading:8813152-Humans,
pubmed-meshheading:8813152-Melanoma,
pubmed-meshheading:8813152-Neoplastic Cells, Circulating,
pubmed-meshheading:8813152-Protein Binding,
pubmed-meshheading:8813152-Tumor Markers, Biological
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pubmed:year |
1996
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pubmed:articleTitle |
Interactions between galectin-3 and Mac-2-binding protein mediate cell-cell adhesion.
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pubmed:affiliation |
Tumor Progression and Metastasis Program, Karmanos Cancer Institute, Wayne State University, Detroit, Michigan 48201, USA.
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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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