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Galectin-1 is implicated in the protein kinase C epsilon/vimentin-controlled trafficking of integrin-beta1 in glioblastoma cells.

Fortin S, Le Mercier M, Camby I, Spiegl-Kreinecker S, Berger W, Lefranc F, Kiss R - Brain Pathol. (2009)

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Toxicology, Institute of Pharmacy, Univesité Libre de Bruxelles, Brussels.

ABSTRACT
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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Related in: MedlinePlus

Transient transfection of galectin-1 using targeted small interfering RNA (siRNA) decreases intracellular galectin-1 protein. WB analysis of galectin-1 expression levels at days 5, 7 and 9 post-transfection in control (ctrl), scramble-transfected (scr), and galectin-1-transfected (siGal1) U87 (A) and Hs683 (C) cells. Immunofluorescence (IF) analysis of galectin-1 expression levels in U87 day 7 post-transfection (B) and Hs683 day 5 post-transfection (D) using scrambled or anti-galectin-1 siRNA. Top rows are the corresponding bright fields to the IF images.
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fig01: Transient transfection of galectin-1 using targeted small interfering RNA (siRNA) decreases intracellular galectin-1 protein. WB analysis of galectin-1 expression levels at days 5, 7 and 9 post-transfection in control (ctrl), scramble-transfected (scr), and galectin-1-transfected (siGal1) U87 (A) and Hs683 (C) cells. Immunofluorescence (IF) analysis of galectin-1 expression levels in U87 day 7 post-transfection (B) and Hs683 day 5 post-transfection (D) using scrambled or anti-galectin-1 siRNA. Top rows are the corresponding bright fields to the IF images.

Mentions: Galectin-1-targeted siRNA was transiently transfected into both U87 and Hs683 glioblastoma cells. Levels of intracellular galectin-1 protein were measured by both WB and IF; galectin-1 was effectively diminished from day 5 to day 9 post-transfection in U87 cells (Figure 1A,B) and in Hs683 cells (Figure 1C,D) in comparison with control and scramble-transfected cells.


Galectin-1 is implicated in the protein kinase C epsilon/vimentin-controlled trafficking of integrin-beta1 in glioblastoma cells.

Fortin S, Le Mercier M, Camby I, Spiegl-Kreinecker S, Berger W, Lefranc F, Kiss R - Brain Pathol. (2009)

Transient transfection of galectin-1 using targeted small interfering RNA (siRNA) decreases intracellular galectin-1 protein. WB analysis of galectin-1 expression levels at days 5, 7 and 9 post-transfection in control (ctrl), scramble-transfected (scr), and galectin-1-transfected (siGal1) U87 (A) and Hs683 (C) cells. Immunofluorescence (IF) analysis of galectin-1 expression levels in U87 day 7 post-transfection (B) and Hs683 day 5 post-transfection (D) using scrambled or anti-galectin-1 siRNA. Top rows are the corresponding bright fields to the IF images.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2805865&req=5

fig01: Transient transfection of galectin-1 using targeted small interfering RNA (siRNA) decreases intracellular galectin-1 protein. WB analysis of galectin-1 expression levels at days 5, 7 and 9 post-transfection in control (ctrl), scramble-transfected (scr), and galectin-1-transfected (siGal1) U87 (A) and Hs683 (C) cells. Immunofluorescence (IF) analysis of galectin-1 expression levels in U87 day 7 post-transfection (B) and Hs683 day 5 post-transfection (D) using scrambled or anti-galectin-1 siRNA. Top rows are the corresponding bright fields to the IF images.
Mentions: Galectin-1-targeted siRNA was transiently transfected into both U87 and Hs683 glioblastoma cells. Levels of intracellular galectin-1 protein were measured by both WB and IF; galectin-1 was effectively diminished from day 5 to day 9 post-transfection in U87 cells (Figure 1A,B) and in Hs683 cells (Figure 1C,D) in comparison with control and scramble-transfected cells.

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Toxicology, Institute of Pharmacy, Univesité Libre de Bruxelles, Brussels.

ABSTRACT
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.

Show MeSH
Related in: MedlinePlus