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Compared with NDU wounds, the Hippo-YAP pathway in DFU wounds was found to be significantly inhibited (Fig. 2A). Then we explored the detailed molecular mechanism of this phenomenon. The DNA scaffold of NETs can be hydrolyzed by
Figure 3. Compared with NDU wounds, the Hippo-YAP pathway in DFU wounds was found to be significantly inhibited (Fig. 2A). Then we explored the detailed molecular mechanism of this phenomenon. The DNA scaffold of NETs can be hydrolyzed by

Deskripsi

The molecular mechanism linking NET-derived DNA to Hippo-YAP pathway inhibition and endothelial-to-mesenchymal transition is elucidated, with DNase treatment as a potential therapeutic approach.

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In vitro endothelial-to-mesenchymal transition markers are quantified following NET exposure, demonstrating increased mesenchymal and decreased endothelial protein expression.

Figure 4

In vitro endothelial-to-mesenchymal transition markers are quantified following NET exposure, demonstrating increased mesenchymal and decreased endothelial protein expression.

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YAP phosphorylation and nuclear exclusion in NET-treated endothelial cells are characterized, linking NET exposure to Hippo pathway activation.

Figure 5

YAP phosphorylation and nuclear exclusion in NET-treated endothelial cells are characterized, linking NET exposure to Hippo pathway activation.

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Wound healing outcomes in Padi4-knockout diabetic mice compared to wild-type controls are documented, showing accelerated closure when NET formation is genetically ablated.

Figure 6

Wound healing outcomes in Padi4-knockout diabetic mice compared to wild-type controls are documented, showing accelerated closure when NET formation is genetically ablated.

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Histological analysis of wound tissue from NET-depleted and control diabetic mice reveals improved re-epithelialization and vascularization.

Figure 7

Histological analysis of wound tissue from NET-depleted and control diabetic mice reveals improved re-epithelialization and vascularization.

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DNase I treatment effects on diabetic wound healing in vivo are quantified, demonstrating that NET degradation promotes wound closure through preserved endothelial function.

Figure 8

DNase I treatment effects on diabetic wound healing in vivo are quantified, demonstrating that NET degradation promotes wound closure through preserved endothelial function.

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A proposed model integrating NET-mediated Hippo pathway suppression with endothelial-to-mesenchymal transition in delayed diabetic wound healing is diagrammed.

Figure 9

A proposed model integrating NET-mediated Hippo pathway suppression with endothelial-to-mesenchymal transition in delayed diabetic wound healing is diagrammed.

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Figure 3

Diagram
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Source Paper

Neutrophil Extracellular Traps Delay Diabetic Wound Healing by Inducing Endothelial-to-Mesenchymal Transition via the Hippo pathway.

International journal of biological sciences (2023)

PMID: 36594092

DOI: 10.7150/ijbs.78046

Cite This Figure

![Figure 3: The molecular mechanism linking NET-derived DNA to Hippo-YAP pathway inhibition and endothelial-to-mesenchymal transition is elucidated, with DNase treatment as a potential therapeutic approach.](https://pdfs.citedhealth.com/figures/36594092/184.png)

> Source: Shuofei Yang et al. "Neutrophil Extracellular Traps Delay Diabetic Wound Healing by Inducing Endothel." *International journal of biological sciences*, 2023. PMID: [36594092](https://pubmed.ncbi.nlm.nih.gov/36594092/)
<figure>
  <img src="https://pdfs.citedhealth.com/figures/36594092/184.png" alt="The molecular mechanism linking NET-derived DNA to Hippo-YAP pathway inhibition and endothelial-to-mesenchymal transition is elucidated, with DNase treatment as a potential therapeutic approach." />
  <figcaption>Figure 3. The molecular mechanism linking NET-derived DNA to Hippo-YAP pathway inhibition and endothelial-to-mesenchymal transition is elucidated, with DNase treatment as a potential therapeutic approach.<br>  Source: Shuofei Yang et al. "Neutrophil Extracellular Traps Delay Diabetic Wound Healing by Inducing Endothel." <em>International journal of biological sciences</em>, 2023. PMID: <a href="https://pubmed.ncbi.nlm.nih.gov/36594092/">36594092</a></figcaption>
</figure>

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