Syndecan-1 shedding by meprin β impairs keratinocyte adhesion and differentiation in hyperkeratosis

Research output: Contribution to journalResearch articleContributedpeer-review

Contributors

  • Florian Peters - , Kiel University, University of Zurich (Author)
  • Sascha Rahn - , Kiel University (Author)
  • Marion Mengel - , Kiel University (Author)
  • Franka Scharfenberg - , Kiel University (Author)
  • Anna Otte - , Kiel University (Author)
  • Tomas Koudelka - , Kiel University (Author)
  • Erwin F. Wagner - , Medical University of Vienna (Author)
  • F. Thomas Wunderlich - , Max Planck Institute for Metabolism Research (Author)
  • Michael Haase - , Department of Pediatric Surgery (Author)
  • Ronald Naumann - , Max Planck Institute of Molecular Cell Biology and Genetics (Author)
  • Andreas Tholey - , Kiel University (Author)
  • Christoph Becker-Pauly - , Kiel University (Author)

Abstract

Dysregulation of proteolytic enzymes has huge impact on epidermal homeostasis, which can result in severe pathological conditions such as fibrosis or Netherton syndrome. The metalloprotease meprin β was found to be upregulated in hyperproliferative skin diseases. AP-1 transcription factor complex has been reported to induce Mep1b expression. Since AP-1 and its subunit fos-related antigen 2 (fra-2) are associated with the onset and progression of psoriasis, we wanted to investigate if this could partially be attributed to increased meprin β activity. Here, we demonstrate that fra-2 transgenic mice show increased meprin β expression and proteolytic activity in the epidermis. To avoid influence by other fra-2 regulated genes, we additionally generated a mouse model that enabled tamoxifen-inducible expression of meprin β under the Krt5-promotor to mimic the pathological condition. Interestingly, induced meprin β expression in the epidermis resulted in hyperkeratosis, hair loss and mottled pigmentation of the skin. Employing N-terminomics revealed syndecan-1 as a substrate of meprin β in skin. Shedding of syndecan-1 at the cell surface caused delayed calcium-induced differentiation and impaired adhesion of keratinocytes, which was blocked by the meprin β inhibitor fetuin-B.

Details

Original languageEnglish
Pages (from-to)37-69
Number of pages33
JournalMatrix Biology
Volume102
Publication statusPublished - Aug 2021
Peer-reviewedYes

External IDs

PubMed 34508852

Keywords

ASJC Scopus subject areas

Keywords

  • Ectodomain shedding, Hyperkeratosis, Meprin, Skin, Syndecan-1