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Notes: A, B. Western blotting was used to observe the overexpression efficiency. C The MTT assay was used for cell viability detection. Red dots were recorded, and the ratio of TUNEL-positive cells was evaluated to reflect cell apoptosis. G—I Western blotting was performed to analyze the expression of proapoptotic proteins, such as cleaved caspase-3 and PARP. Abbreviation: Ad-Mst1, adenovirus-loaded Mst1. Mst1 enhancement activates mitochondrial apoptosis Subsequently, we explored the mechanism by which Mst1 overexpression induced apoptosis in breast cancer cells.

Previous studies have suggested that Mst1 is the upstream mediator of mitochondrial homeostasis. The early feature of mitochondrial apoptosis is a reduction in the mitochondrial membrane potential that reflects mitochondrial functions, such as ATP production and oxidative stress. In light of the central role of the mitochondrial potential in ATP production, 35 we measured total ATP production in the Mst1-overexpressed cells.

We also found that mitochondrial ROS production was significantly increased in response to Mst1 overexpression as assessed via flow cytometry Figure 2D and E , indicating that Mst1 overexpression induced mitochondrial oxidative injury. Figure 2 Mitochondrial apoptosis is activated by Mst1 overexpression. C ATP production was measured.

The relative ROS content was recorded as a ratio to that of the control group. F—J Western blotting was performed to analyze the expression of mitochondrial apoptotic proteins.

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The late feature of mitochondrial apoptosis is the activation of mitochondrial apoptotic proteins. Conversely, the antiapoptotic proteins related to mitochondrial apoptosis, such as Bcl-2 and survivin, were obviously downregulated in response to Mst1 overexpression Figure 2F — J. Altogether, our data illustrated that Mst1 overexpression was accompanied by activation of mitochondrial apoptosis in tongue cancer.

Mst1 triggers Drp1-related mitochondrial fragmentation Next, experiments were conducted to analyze the mechanism by which Mst1 overexpression activated mitochondrial apoptosis.

Previous studies have found a causal role of mitochondrial fragmentation in initiating the caspase-9—related mitochondrial apoptosis pathways in several cancer types.

To answer this question, the mitochondrial morphology was observed in response to Mst1 overexpression in MDA-MB cells. As shown in Figure 3A and B , compared to that of the control group, Mst1 overexpression generated significant massive fragmentation of the mitochondria. Subsequently, the mitochondrial length was measured to quantify mitochondrial fragmentation according to the method described in previous reports.

Figure 3 Mst1 overexpression activates mitochondrial fragmentation in a manner dependent on Drp1. Notes: A, B Immunofluorescence for mitochondria using a mitochondrial-specific antibody Tom The average length of the mitochondria was measured, and this parameter was used to quantify mitochondrial fragmentation.

C—F Western blotting was applied to evaluate the expression of pro-fission proteins, including Drp1, Mff and Fis1. Relative Drp1 expression was recorded in response to Mst1 overexpression.

G—I qPCR assay was used to evaluate the transcription of pro-fission factors. Based on previous findings, Drp1 is an indispensable factor that regulates mitochondrial division. As a consequence of Drp1 upregulation, the expression of pro-fission proteins, such as Drp1 and Mff, was mostly increased in the Mst1-overexpressed cells compared to those in the control group Figure 3C — F.

This information highlighted the promotive effects of Mst1 overexpression on mitochondrial fragmentation. Inhibition of Drp1-related mitochondrial fragmentation reduces mitochondrial stress and promotes cell survival in breast cancer cells The above data validated the regulatory effects of Mst1 on Drp1-related mitochondrial fragmentation.

However, whether Drp1-related mitochondrial fragmentation is required for the mitochondrial damage and cell apoptosis induced by Mst1 overexpression is unknown. To answer this question, Drp1 was deleted using siRNA. The knockdown efficiency was confirmed via Western blotting Figure 4A and B. Then, mitochondrial stress was determined by analyzing ROS production and cyt-c liberation.

Using the Western blotting assay, we found that cytoplasmic cyt-c cyto cyt-c expression was increased in response to Mst1 overexpression in MDA-MB cells Figure 4C and D , confirming that Mst1 overexpression contributed to cyt-c migration to the cytoplasm. This result was further supported by immunofluorescence assay Figure 4E and F. However, Mst1 overexpression-mediated cyt-c liberation was negated by Drp1 silencing.

Subsequently, mitochondrial ROS was analyzed by flow cytometry. This information verified the necessary role played by Drp1-related mitochondrial fragmentation in aggravating Mst1-mediated mitochondrial stress.

Figure 4 Loss of Drp1-related mitochondrial fragmentation attenuates mitochondrial damage and cell apoptosis. Western blotting was used to analyze the knockdown efficiency.

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Please disable your ad-blocker to continue using FileHippo. Nitro PDF Reader 3. User Rating. Download 32 bit 1.Notes: A, B Immunofluorescence for mitochondria using a mitochondrial-specific antibody Tom The plasmids were transfected into HaEpi cells with DNAfectin transfection reagent Tiangen, Beijing, China , according to the manufacturer's instructions and as described previously The 32 bit version will work on your system however.

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These results define the JNK pathway as a tumor suppressor that acts by triggering mitochondrial fragmentation with potential implications for new approaches to breast cancer therapy.

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