Source:http://linkedlifedata.com/resource/pubmed/id/17176047
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
51
|
| pubmed:dateCreated |
2007-3-6
|
| pubmed:abstractText |
Gelatinase B (MMP-9) and galectin-3 are widely known to participate in tumor cell invasion and metastasis. Glycans derived from MMP-9 expressed in MCF-7 breast cancer and THP-1 myeloid leukemia cells were compared with those from MMP-9 expressed in natural neutrophils. The many O-linked glycans of neutrophil gelatinase B presented a cluster of mainly galactosylated core II structures, 46% of which were ligands for galectin-3; 11% contained two to three N-acetyllactosamine repeating units that are high-affinity ligands for the lectin. The glycan epitopes thus provide MMP-9 with both high-affinity and (presumably) high-avidity interactions with galectin-3. In contrast, the O-glycans released from MMP-9 expressed in MCF-7 and THP-1 cells were predominantly sialylated core I structures. Only 10% of MCF-7 and THP-1 gelatinase B O-glycans were ligands for galectin-3 and contained only a maximum single N-acetyllactosamine repeat. Consistent with the glycan analysis, surface plasmon resonance binding assays indicated that the cancer-associated glycoforms of MMP-9 bound galectin-3 with an affinity and avidity significantly reduced compared with those of the natural neutrophil MMP-9. Galectin-3 exists as a multimer that also binds laminin, providing a means of localizing neutrophil MMP-9 in the extracellular matrix (ECM). The analytical data presented here suggest that MMP-9 glycoforms secreted by tumor cells are unlikely to be tethered at the site of secretion, thus promoting more extensive cleavage of the ECM and providing a rationale for the contribution that gelatinase B makes to cancer cell metastasis.
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| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
1520-4995
|
| pubmed:author | |
| pubmed:issnType |
Electronic
|
| pubmed:day |
26
|
| pubmed:volume |
45
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
15249-58
|
| pubmed:meshHeading |
pubmed-meshheading:17176047-Animals,
pubmed-meshheading:17176047-Breast Neoplasms,
pubmed-meshheading:17176047-Carbohydrate Conformation,
pubmed-meshheading:17176047-Cattle,
pubmed-meshheading:17176047-Cell Line, Tumor,
pubmed-meshheading:17176047-Down-Regulation,
pubmed-meshheading:17176047-Extracellular Matrix,
pubmed-meshheading:17176047-Galectin 3,
pubmed-meshheading:17176047-Glycosylation,
pubmed-meshheading:17176047-Humans,
pubmed-meshheading:17176047-Isoenzymes,
pubmed-meshheading:17176047-Leukemia, Myeloid,
pubmed-meshheading:17176047-Matrix Metalloproteinase 9,
pubmed-meshheading:17176047-Neoplasm Invasiveness,
pubmed-meshheading:17176047-Neoplasm Metastasis,
pubmed-meshheading:17176047-Neutrophils,
pubmed-meshheading:17176047-Polysaccharides,
pubmed-meshheading:17176047-Protein Binding,
pubmed-meshheading:17176047-Surface Plasmon Resonance
|
| pubmed:year |
2006
|
| pubmed:articleTitle |
Cancer-associated glycoforms of gelatinase B exhibit a decreased level of binding to galectin-3.
|
| pubmed:affiliation |
Glycobiology Institute, Department of Biochemistry, University of Oxford, UK.
|
| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
|