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Ganglioside GD3 induces convergence and synergism of adhesion and hepatocyte growth factor/Met signals in melanomas.

Furukawa K, Kambe M, Miyata M, Ohkawa Y, Tajima O, Furukawa K - Cancer Sci. (2013)

Bottom Line: In this study, we analyzed the effects of GD3 expression on cell signals triggered by hepatocyte growth factor (HGF)/Met interaction and by adhesion to collagen type I (CL-I).When resistance to induced apoptosis by H2O2 was examined, only GD3+ cells treated with both HGF and adhesion to CL-I showed clearly low percentages of dead cells compared with GD3- cells or GD3+ cells treated with either one of the stimulants.Cell growth measured by 5-ethynyl-2' deoxyuridine uptake also showed synergistic effects in GD3+ cells.

View Article: PubMed Central - PubMed

Affiliation: Department of Biomedical Sciences, Chubu University College of Life and Health Sciences, Kasugai, Japan; Department of Biochemistry II, Nagoya University Graduate School of Medicine, Nagoya, Japan.

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Reduction of Akt and Erks phosphorylation levels by costimulation with hepatocyte growth factor (HGF) and adhesion to collagen type I (CL-I) using an anti-GD3 mAb. (A) Phosphorylation levels of Akt and Erks by costimulation with HGF and adhesion to CL-I (3.0 × 105 cells/3.5-cm dish) after treatment with an anti-GD3 mAb R24 were analyzed with Western immunoblotting. (B) Bands of GD3+ cells and GD3− cells in (A) were scanned and the band intensities of the phosphorylated Akt and Erks were measured and presented after correction with those of total proteins. Black bars, samples with mAb R24 treatment; gray bars, samples without mAb R24 treatment. β-actin bands indicate equal loading of samples.
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fig06: Reduction of Akt and Erks phosphorylation levels by costimulation with hepatocyte growth factor (HGF) and adhesion to collagen type I (CL-I) using an anti-GD3 mAb. (A) Phosphorylation levels of Akt and Erks by costimulation with HGF and adhesion to CL-I (3.0 × 105 cells/3.5-cm dish) after treatment with an anti-GD3 mAb R24 were analyzed with Western immunoblotting. (B) Bands of GD3+ cells and GD3− cells in (A) were scanned and the band intensities of the phosphorylated Akt and Erks were measured and presented after correction with those of total proteins. Black bars, samples with mAb R24 treatment; gray bars, samples without mAb R24 treatment. β-actin bands indicate equal loading of samples.

Mentions: To examine whether GD3 is involved in the enhanced phosphorylation of Akt and Erks when cells are costimulated with HGF and adhesion to CL-I, we examined the inhibitory effects of an anti-GD3 mAb R24 on GD3+ and GD3− N1 cells. Phosphorylation levels of Akt and Erks were diminished in GD3+ cells but not in GD3− cells after treatment with mAb R24 (Fig.6). These results, together with the results of GD3 synthase knockdown, indicate that GD3 is involved in the enhanced phosphorylation of the signaling molecules.


Ganglioside GD3 induces convergence and synergism of adhesion and hepatocyte growth factor/Met signals in melanomas.

Furukawa K, Kambe M, Miyata M, Ohkawa Y, Tajima O, Furukawa K - Cancer Sci. (2013)

Reduction of Akt and Erks phosphorylation levels by costimulation with hepatocyte growth factor (HGF) and adhesion to collagen type I (CL-I) using an anti-GD3 mAb. (A) Phosphorylation levels of Akt and Erks by costimulation with HGF and adhesion to CL-I (3.0 × 105 cells/3.5-cm dish) after treatment with an anti-GD3 mAb R24 were analyzed with Western immunoblotting. (B) Bands of GD3+ cells and GD3− cells in (A) were scanned and the band intensities of the phosphorylated Akt and Erks were measured and presented after correction with those of total proteins. Black bars, samples with mAb R24 treatment; gray bars, samples without mAb R24 treatment. β-actin bands indicate equal loading of samples.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4317880&req=5

fig06: Reduction of Akt and Erks phosphorylation levels by costimulation with hepatocyte growth factor (HGF) and adhesion to collagen type I (CL-I) using an anti-GD3 mAb. (A) Phosphorylation levels of Akt and Erks by costimulation with HGF and adhesion to CL-I (3.0 × 105 cells/3.5-cm dish) after treatment with an anti-GD3 mAb R24 were analyzed with Western immunoblotting. (B) Bands of GD3+ cells and GD3− cells in (A) were scanned and the band intensities of the phosphorylated Akt and Erks were measured and presented after correction with those of total proteins. Black bars, samples with mAb R24 treatment; gray bars, samples without mAb R24 treatment. β-actin bands indicate equal loading of samples.
Mentions: To examine whether GD3 is involved in the enhanced phosphorylation of Akt and Erks when cells are costimulated with HGF and adhesion to CL-I, we examined the inhibitory effects of an anti-GD3 mAb R24 on GD3+ and GD3− N1 cells. Phosphorylation levels of Akt and Erks were diminished in GD3+ cells but not in GD3− cells after treatment with mAb R24 (Fig.6). These results, together with the results of GD3 synthase knockdown, indicate that GD3 is involved in the enhanced phosphorylation of the signaling molecules.

Bottom Line: In this study, we analyzed the effects of GD3 expression on cell signals triggered by hepatocyte growth factor (HGF)/Met interaction and by adhesion to collagen type I (CL-I).When resistance to induced apoptosis by H2O2 was examined, only GD3+ cells treated with both HGF and adhesion to CL-I showed clearly low percentages of dead cells compared with GD3- cells or GD3+ cells treated with either one of the stimulants.Cell growth measured by 5-ethynyl-2' deoxyuridine uptake also showed synergistic effects in GD3+ cells.

View Article: PubMed Central - PubMed

Affiliation: Department of Biomedical Sciences, Chubu University College of Life and Health Sciences, Kasugai, Japan; Department of Biochemistry II, Nagoya University Graduate School of Medicine, Nagoya, Japan.

Show MeSH
Related in: MedlinePlus