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MedChemExpress mmp3
Figure 5. Silencing GMPPB inhibits the proliferation and invasion of glioblastoma cells via the <t>Hippo/MMP3</t> pathway. (A) Representative heatmaps of transcriptome analysis indicate genes differ- entially regulated upon GMPPB knockdown in U87 cells, including MMP3 (boxed in red). (B) KEGG pathway analyses of GMPPB knockdown in U87 cells. Pathways potentially involved in invasion and migration, i.e., cell adhesion molecules, and pathways identified from the current study, i.e., Hippo signaling pathway, are highlighted in red boxes. (C) The indicated proteins in the Hippo pathway were analyzed by Western blotting in the GMPPB-knocked-down U251 cells and GMPPB-overexpressed A172 cells. (D) The protein MMP3 expression was displayed by Western blotting in the GMPPB- knocked-down U87, U251 cells, and GMPPB-overexpressed A172 cells. (E) MMP3 protein expression was displayed by Western blotting after si-NC and si-MMP3 RNA were transfected into A172 GMPPB- overexpressing cell lines. (F) Transwell assay analysis of the effect of si-NC or si-MMP3-transfected A172 GMPPB expression on GBM cell invasion *** p < 0.001. n = 3. Folds of invasion cell number = numbers of invaded cells in treatment groups/numbers of invaded cells in vector groups. (G) Verteporfin impacts the MMP3 protein expression displayed by Western blotting in GMPPB-overexpressing A172 cells. The concentration of verteporfin was 1 µg/mL and 2 µg/mL. β-actin was used as a loading control.
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Cayman Chemical onx-0914
Figure 5. Silencing GMPPB inhibits the proliferation and invasion of glioblastoma cells via the <t>Hippo/MMP3</t> pathway. (A) Representative heatmaps of transcriptome analysis indicate genes differ- entially regulated upon GMPPB knockdown in U87 cells, including MMP3 (boxed in red). (B) KEGG pathway analyses of GMPPB knockdown in U87 cells. Pathways potentially involved in invasion and migration, i.e., cell adhesion molecules, and pathways identified from the current study, i.e., Hippo signaling pathway, are highlighted in red boxes. (C) The indicated proteins in the Hippo pathway were analyzed by Western blotting in the GMPPB-knocked-down U251 cells and GMPPB-overexpressed A172 cells. (D) The protein MMP3 expression was displayed by Western blotting in the GMPPB- knocked-down U87, U251 cells, and GMPPB-overexpressed A172 cells. (E) MMP3 protein expression was displayed by Western blotting after si-NC and si-MMP3 RNA were transfected into A172 GMPPB- overexpressing cell lines. (F) Transwell assay analysis of the effect of si-NC or si-MMP3-transfected A172 GMPPB expression on GBM cell invasion *** p < 0.001. n = 3. Folds of invasion cell number = numbers of invaded cells in treatment groups/numbers of invaded cells in vector groups. (G) Verteporfin impacts the MMP3 protein expression displayed by Western blotting in GMPPB-overexpressing A172 cells. The concentration of verteporfin was 1 µg/mL and 2 µg/mL. β-actin was used as a loading control.
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MedChemExpress hy 114419 onx
Figure 5. Silencing GMPPB inhibits the proliferation and invasion of glioblastoma cells via the <t>Hippo/MMP3</t> pathway. (A) Representative heatmaps of transcriptome analysis indicate genes differ- entially regulated upon GMPPB knockdown in U87 cells, including MMP3 (boxed in red). (B) KEGG pathway analyses of GMPPB knockdown in U87 cells. Pathways potentially involved in invasion and migration, i.e., cell adhesion molecules, and pathways identified from the current study, i.e., Hippo signaling pathway, are highlighted in red boxes. (C) The indicated proteins in the Hippo pathway were analyzed by Western blotting in the GMPPB-knocked-down U251 cells and GMPPB-overexpressed A172 cells. (D) The protein MMP3 expression was displayed by Western blotting in the GMPPB- knocked-down U87, U251 cells, and GMPPB-overexpressed A172 cells. (E) MMP3 protein expression was displayed by Western blotting after si-NC and si-MMP3 RNA were transfected into A172 GMPPB- overexpressing cell lines. (F) Transwell assay analysis of the effect of si-NC or si-MMP3-transfected A172 GMPPB expression on GBM cell invasion *** p < 0.001. n = 3. Folds of invasion cell number = numbers of invaded cells in treatment groups/numbers of invaded cells in vector groups. (G) Verteporfin impacts the MMP3 protein expression displayed by Western blotting in GMPPB-overexpressing A172 cells. The concentration of verteporfin was 1 µg/mL and 2 µg/mL. β-actin was used as a loading control.
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Image Search Results


Figure 5. Silencing GMPPB inhibits the proliferation and invasion of glioblastoma cells via the Hippo/MMP3 pathway. (A) Representative heatmaps of transcriptome analysis indicate genes differ- entially regulated upon GMPPB knockdown in U87 cells, including MMP3 (boxed in red). (B) KEGG pathway analyses of GMPPB knockdown in U87 cells. Pathways potentially involved in invasion and migration, i.e., cell adhesion molecules, and pathways identified from the current study, i.e., Hippo signaling pathway, are highlighted in red boxes. (C) The indicated proteins in the Hippo pathway were analyzed by Western blotting in the GMPPB-knocked-down U251 cells and GMPPB-overexpressed A172 cells. (D) The protein MMP3 expression was displayed by Western blotting in the GMPPB- knocked-down U87, U251 cells, and GMPPB-overexpressed A172 cells. (E) MMP3 protein expression was displayed by Western blotting after si-NC and si-MMP3 RNA were transfected into A172 GMPPB- overexpressing cell lines. (F) Transwell assay analysis of the effect of si-NC or si-MMP3-transfected A172 GMPPB expression on GBM cell invasion *** p < 0.001. n = 3. Folds of invasion cell number = numbers of invaded cells in treatment groups/numbers of invaded cells in vector groups. (G) Verteporfin impacts the MMP3 protein expression displayed by Western blotting in GMPPB-overexpressing A172 cells. The concentration of verteporfin was 1 µg/mL and 2 µg/mL. β-actin was used as a loading control.

Journal: International journal of molecular sciences

Article Title: Silencing GMPPB Inhibits the Proliferation and Invasion of GBM via Hippo/MMP3 Pathways.

doi: 10.3390/ijms241914707

Figure Lengend Snippet: Figure 5. Silencing GMPPB inhibits the proliferation and invasion of glioblastoma cells via the Hippo/MMP3 pathway. (A) Representative heatmaps of transcriptome analysis indicate genes differ- entially regulated upon GMPPB knockdown in U87 cells, including MMP3 (boxed in red). (B) KEGG pathway analyses of GMPPB knockdown in U87 cells. Pathways potentially involved in invasion and migration, i.e., cell adhesion molecules, and pathways identified from the current study, i.e., Hippo signaling pathway, are highlighted in red boxes. (C) The indicated proteins in the Hippo pathway were analyzed by Western blotting in the GMPPB-knocked-down U251 cells and GMPPB-overexpressed A172 cells. (D) The protein MMP3 expression was displayed by Western blotting in the GMPPB- knocked-down U87, U251 cells, and GMPPB-overexpressed A172 cells. (E) MMP3 protein expression was displayed by Western blotting after si-NC and si-MMP3 RNA were transfected into A172 GMPPB- overexpressing cell lines. (F) Transwell assay analysis of the effect of si-NC or si-MMP3-transfected A172 GMPPB expression on GBM cell invasion *** p < 0.001. n = 3. Folds of invasion cell number = numbers of invaded cells in treatment groups/numbers of invaded cells in vector groups. (G) Verteporfin impacts the MMP3 protein expression displayed by Western blotting in GMPPB-overexpressing A172 cells. The concentration of verteporfin was 1 µg/mL and 2 µg/mL. β-actin was used as a loading control.

Article Snippet: In order to further explore if MMP3 is one of the downstream target genes in the Hippo pathway, we applied the YAP inhibitor drug verteporfin (MCE, Concord, CA, USA, catalog number CL318952), which has been shown to disrupt YAP-TEAD interactions and to affect expression of its downstream target genes, such as Ki67, EGFR, CDH2, and ITGB1 [29,42].

Techniques: Knockdown, Migration, Western Blot, Expressing, Transfection, Transwell Assay, Plasmid Preparation, Concentration Assay, Control