rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2010-5-4
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pubmed:abstractText |
Cell motility and resistance to apoptosis characterize glioblastoma (GBM) growth and malignancy. In our current work we report that galectin-1, a homodimeric adhesion molecule and carbohydrate-binding protein with affinity for beta-galactosides, is linked with cell surface expression of integrin beta1 and the process of integrin trafficking. Using immunofluorescence, depletion of galectin-1 through both stable knockdown and transient-targeted small interfering RNA (siRNA) treatment induces an intracellular accumulation of integrin-beta1 coincident with a diminution of integrin-beta1 at points of cellular adhesion at the cell membrane. Galectin-1 depletion does not alter the gene expression level of integrin-beta1. Transient galectin-1 depletion effectuates as well the perinuclear accumulation of protein kinase C epsilon (PKCepsilon) and the intermediate filament vimentin, both of which have been shown to mediate integrin recycling in motile cells. Our results argue for the involvement of galectin-1 in the PKCepsilon/vimentin-controlled trafficking of integrin-beta1. The understanding of molecular mediators such as galectin-1 and the pathways through which they drive the cell invasion so descriptive of GBM is anticipated to reveal potential therapeutic targets that promote glioma malignancy.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-10050073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-10402232,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-10600702,
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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, CD29,
http://linkedlifedata.com/resource/pubmed/chemical/Antisense Elements (Genetics),
http://linkedlifedata.com/resource/pubmed/chemical/Galectin 1,
http://linkedlifedata.com/resource/pubmed/chemical/Integrin alpha Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C-epsilon,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/Vimentin,
http://linkedlifedata.com/resource/pubmed/chemical/integrin alpha9
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1750-3639
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
20
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
39-49
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pubmed:dateRevised |
2010-9-21
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pubmed:meshHeading |
pubmed-meshheading:18947333-Antigens, CD29,
pubmed-meshheading:18947333-Antisense Elements (Genetics),
pubmed-meshheading:18947333-Blotting, Western,
pubmed-meshheading:18947333-Brain Neoplasms,
pubmed-meshheading:18947333-Cell Line, Tumor,
pubmed-meshheading:18947333-Endoplasmic Reticulum,
pubmed-meshheading:18947333-Galectin 1,
pubmed-meshheading:18947333-Gene Silencing,
pubmed-meshheading:18947333-Genomics,
pubmed-meshheading:18947333-Glioblastoma,
pubmed-meshheading:18947333-Humans,
pubmed-meshheading:18947333-Integrin alpha Chains,
pubmed-meshheading:18947333-Neoplasm Proteins,
pubmed-meshheading:18947333-Protein Kinase C-epsilon,
pubmed-meshheading:18947333-RNA, Small Interfering,
pubmed-meshheading:18947333-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:18947333-Transfection,
pubmed-meshheading:18947333-Vimentin
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pubmed:year |
2010
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pubmed:articleTitle |
Galectin-1 is implicated in the protein kinase C epsilon/vimentin-controlled trafficking of integrin-beta1 in glioblastoma cells.
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pubmed:affiliation |
Laboratory of Toxicology, Institute of Pharmacy, Univesité Libre de Bruxelles, Brussels.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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