Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-5-4
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.
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, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-10647931, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-11145198, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-11241742, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-11745417, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-11746774, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-11934885, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-12110574, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-12125737, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-12297042, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-14550305, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-15473836, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-15623601, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-15800333, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-16051185, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-16105842, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-16270034, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-16445683, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-16759163, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-16904305, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-16959902, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-17255961, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-17693103, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-17786537, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-17954373, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-18313712, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-18431251, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-8175907, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-8662811, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-8973477, http://linkedlifedata.com/resource/pubmed/commentcorrection/18947333-9730976
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1750-3639
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
20
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
39-49
pubmed:dateRevised
2010-9-21
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
pubmed:year
2010
pubmed:articleTitle
Galectin-1 is implicated in the protein kinase C epsilon/vimentin-controlled trafficking of integrin-beta1 in glioblastoma cells.
pubmed:affiliation
Laboratory of Toxicology, Institute of Pharmacy, Univesité Libre de Bruxelles, Brussels.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't