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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1A
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pubmed:dateCreated |
1998-5-13
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pubmed:abstractText |
We investigated alterations in the expression of integrin on adriamycin-resistant MCF-7 (MCF-7/ADR) cells, which had been selected from MCF-7 human breast cancer cells, in order to examine the mechanisms behind the acquisition of malignancy in breast cancer progression. Expression of the alpha 6 integrin subunit of MCF-7/ADR cells was stronger than that of MCF-7 cells, whereas expression of alpha 2 integrin subunit of MCF-7/ADR cells was weaker than that of MCF-7 cells. MCF-7/ADR showed increased binding activity to laminin, but not to collagen or fibronectin, compared to those of parental MCF-7 cells. Adhesion of MCF-7 cells to collagen and laminin was inhibited by the addition of antibody to alpha 2 and alpha 6 integrin subunit, respectively. On the other hand, adhesion of MCF-7/ADR cells to collagen was not inhibited by the addition of antibody to alpha 2, alpha 3 or alpha 6 integrin subunit. Adhesion of MCF-7/ADR cells to laminin was inhibited by not only the antibody to alpha 6 subunit but also the antibody to the alpha 3 subunit. The transmigratory activity of MCF-7/ADR cells was higher than that of MCF-7 cells. A significant inhibitory effect on the transmigration of MCF-7/ADR cells was observed by the addition of antibody to alpha 6 and beta 1 integrin subunit. MCF-7/ADR cells appeared smaller and flatter than MCF-7 cells, and spread to a greater extent on the culture dish. MCF-7 cells cultured on Matrigel for 24 hours formed clusters. In contrast to this, MCF-7/ADR cells expanded with a tubular-like pattern on Matrigel. The spread of MCF-7/ADR cells was incompletely inhibited by addition of the antibody to alpha 3 integrin subunit, and completely inhibited by addition of the antibody to alpha 6 and beta 1 integrin subunit. These findings suggest that integrins on MCF-7/ADR cells are altered from those on parental MCF-7 cells in not only expression but also function, and that interaction between cancer cells and extracellular matrix protein is involved in augmentation of the invasiveness of MCF-7/ADR cells.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/Doxorubicin,
http://linkedlifedata.com/resource/pubmed/chemical/Drug Combinations,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/Laminin,
http://linkedlifedata.com/resource/pubmed/chemical/Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/matrigel
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pubmed:status |
MEDLINE
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pubmed:issn |
0250-7005
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
257-62
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:9568087-Breast Neoplasms,
pubmed-meshheading:9568087-Carcinoma,
pubmed-meshheading:9568087-Cell Adhesion,
pubmed-meshheading:9568087-Cell Adhesion Molecules,
pubmed-meshheading:9568087-Collagen,
pubmed-meshheading:9568087-Doxorubicin,
pubmed-meshheading:9568087-Drug Combinations,
pubmed-meshheading:9568087-Drug Resistance, Neoplasm,
pubmed-meshheading:9568087-Female,
pubmed-meshheading:9568087-Humans,
pubmed-meshheading:9568087-Integrins,
pubmed-meshheading:9568087-Laminin,
pubmed-meshheading:9568087-Neoplasm Invasiveness,
pubmed-meshheading:9568087-Proteoglycans,
pubmed-meshheading:9568087-Tumor Cells, Cultured
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pubmed:articleTitle |
Altered expression of integrins in adriamycin-resistant human breast cancer cells.
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pubmed:affiliation |
Laboratory of Experimental Pathology, Aichi Cancer Center Research Institute, Nagoya, Japan.
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pubmed:publicationType |
Journal Article
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