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Updated: Aug 14, 2026

Assessment of Acute Wound Healing using the Dorsal Subcutaneous Polyvinyl Alcohol Sponge Implantation and Excisional Tail Skin Wound Models.
Published on: March 25, 2020
Epidermal development and wound healing in matrix metalloproteinase 13-deficient mice
Bettina Hartenstein1, Bernd Thilo Dittrich, Dominique Stickens
1Division of Signal Transduction and Growth Control (A100), Deutsches Krebsforschungszentrum Heidelberg (DKFZ), Heidelberg, Germany.
Abstract:
Degradation of the extracellular matrix, which is an indispensable step in tissue remodelling processes such as embryonic development and wound healing of the skin, has been attributed to collagenolytic activity of members of the matrix metalloproteinase family (MMPs). Here, we employed mmp13 knockout mice to elucidate the function of MMP13 in embryonic skin development, skin homeostasis, and cutaneous wound healing. Overall epidermal architecture and dermal composition of non-injured skin were indistinguishable from wild-type mice. Despite robust expression of MMP13 in the early phase of wound healing, wild-type and mmp13 knockout animals did not differ in their efficiency of re-epithelialization, inflammatory response, granulation tissue formation, angiogenesis, and restoration of basement membrane. Yet, among other MMPs also expressed during wound healing, MMP8 was found to be enhanced in wounds of MMP13-deficient mice. In summary, skin homeostasis and also tissue remodelling processes like embryonic skin development and cutaneous wound healing are independent of MMP13 either owing to MMP13 dispensability or owing to functional substitution by other collagenolytic proteinases such as MMP8.
Insights
Matrix metalloproteinase-13 (MMP13) is not essential for embryonic skin development or wound healing. Other collagenolytic enzymes, like MMP8, can functionally substitute for MMP13, ensuring tissue remodeling processes occur normally.
Area of Science:
- Biochemistry
- Dermatology
- Molecular Biology
Background:
- Extracellular matrix degradation is crucial for tissue remodeling during embryonic development and wound healing.
- Matrix metalloproteinases (MMPs) are key enzymes responsible for collagen degradation.
- MMP13 has been implicated in these collagenolytic activities.
Purpose of the Study:
- To investigate the specific role of MMP13 in embryonic skin development, skin homeostasis, and cutaneous wound healing.
- To determine if MMP13 is essential for normal skin structure and repair processes.
- To identify potential compensatory mechanisms in the absence of MMP13.
Main Methods:
- Utilized mmp13 knockout mice and wild-type littermates for comparative analysis.
- Assessed skin architecture and dermal composition in non-injured skin.
- Evaluated wound healing parameters including re-epithelialization, inflammation, granulation tissue formation, angiogenesis, and basement membrane restoration.
- Analyzed the expression of other MMPs during the wound healing process.
Main Results:
- No significant differences were observed in epidermal architecture or dermal composition between mmp13 knockout and wild-type mice in non-injured skin.
- MMP13 deficiency did not impair wound healing efficiency, including re-epithelialization, inflammation, granulation tissue formation, angiogenesis, or basement membrane restoration.
- MMP8 expression was found to be upregulated in the wounds of MMP13-deficient mice, suggesting a compensatory role.
Conclusions:
- Skin homeostasis, embryonic skin development, and cutaneous wound healing are independent of MMP13.
- MMP13 dispensability or functional substitution by other collagenolytic proteinases, such as MMP8, ensures the integrity of these processes.
- These findings highlight the redundancy and adaptability of the extracellular matrix remodeling system.
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