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Loss of epidermal MMP-14 expression interferes with angiogenesis but not with re-epithelialization

Zigrino, Paola, Ayachi, Ouissam, Schild, Alexander, Kaltenberg, Jennifer, Zamek, Jan, Nischt, Roswitha, Koch, Manuel, Mauch, Cornelia·2012·European Journal of Cell Biology
DOI 10.1016/j.ejcb.2012.05.003
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Abstract

Synthesis and activation of matrix metalloproteinases during wound healing are important for remodeling the extracellular matrix and modulating various cellular functions. The membrane-type 1 matrix metalloproteinase (MMP-14) has been shown to play a key role during these processes. To analyze the function of epidermal-derived MMP-14 during skin repair we generated mice lacking MMP-14 expression in the epidermis (MMP-14(ep-/-)). These mice displayed overall normal skin morphology and epidermal differentiation patterns. Wound repair in MMP-14(ep-/-) followed the same kinetics as in wild type mice (MMP-14(ep+/+)), and infiltration of neutrophils, leukocytes, and macrophages into the wound site was comparable. Microscopic analysis showed no altered re-epithelialization in the absence of epidermal MMP-14. Furthermore, epidermal differentiation at the end of the repair process and scar formation was normal. However, at day 14 post wounding, sustained angiogenesis was observed in MMP-14(ep-/-) mice in contrast to control mice. Interestingly, decreased levels of endostatin were detected in wound lysates of MMP-14(ep-/-) mice as well as in cultured keratinocytes. Taken together, these data indicate that MMP-14 expression in keratinocytes is dispensable for skin homeostasis and repair, but plays a crucial role in the epidermal-dermal crosstalk leading to modulation of vessel density.

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Metadata

Authors
Zigrino, P., Ayachi, O., Schild, A., Kaltenberg, J., Zamek, J., Nischt, R., Koch, M., & Mauch, C.
Venue
European Journal of Cell Biology
Publisher
Elsevier BV
Published
2012-10
Volume
91
Issue
10
Pages
748-756
ISSN
0171-9335
DOI
10.1016/j.ejcb.2012.05.003
Cited by
38
References
1
Language
en
Licence
Funders
  • Universität zu Köln (SFB 832)
  • Deutsche Forschungsgemeinschaft

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