The Role of the Fibronectin Synergy Site for SkinWound Healing
Cells, ISSN: 2073-4409, Vol: 11, Issue: 13
2022
- 21Citations
- 34Captures
- 1Mentions
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
Citation Benchmarking is provided by Scopus and SciVal and is different from the metrics context provided by PlumX Metrics.
Metrics Details
- Citations21
- Citation Indexes21
- 21
- CrossRef13
- Captures34
- Readers34
- 34
- Mentions1
- Blog Mentions1
- Blog1
Article Description
Skin is constantly exposed to injuries that are repaired with different outcomes, either regeneration or scarring. Scars result from fibrotic processes modulated by cellular physical forces transmitted by integrins. Fibronectin (FN) is a major component in the provisional matrix assembled to repair skin wounds. FN enables cell adhesion binding of α5β 1/αIIβ 3 and αv-class integrins to an RGD-motif. An additional linkage for α5/αIIβ is the synergy site located in close proximity to the RGD motif. The mutation to impair the FN synergy region (Fn1) demonstrated that its absence permits complete development. However, only with the additional engagement to the FN synergy site do cells efficiently resist physical forces. To test how the synergy site-mediated adhesion affects the course of wound healing fibrosis, we used a mouse model of skin injury and in-vitro migration studies with keratinocytes and fibroblasts on FN. The loss of FN synergy site led to normal re-epithelialization caused by two opposing migratory defects of activated keratinocytes and, in the dermis, induced reduced fibrotic responses, with lower contents of myofibroblasts and FN deposition and diminished TGF- β1-mediated cell signalling. We demonstrate that weakened α5β 1-mediated traction forces on FNcause reduced TGF- β1 release from its latent complex.
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