What we investigate

Our laboratory investigates the role of skin fibroblasts in chronic skin wounds. We employ mass spectrometry-based proteomic approaches to study molecular mechanisms which are dysregulated in perturbed wound healing. A special focus lies on the role and function of the extracellular matrix.

KEYWORDS
fibroblasts, extracellular matrix, proteomics, skin, wound healing

Immunofluorescence staining of lysosomes <em>(green)</em>, and counterstaining of nuclei <em>(blue)</em> in normal human fibroblasts (NHF) and chronic wound-associated fibroblasts (cWAF). cWAF exhibit an enlarged and delocalized lysosomal compartment.
Immunofluorescence staining of lysosomes (green), and counterstaining of nuclei (blue) in normal human fibroblasts (NHF) and chronic wound-associated fibroblasts (cWAF). cWAF exhibit an enlarged and delocalized lysosomal compartment.
Our research in more detail

Normal wound healing requires coordination in time and space between resident cell types of the dermis and epidermis and invading immune cells. Fibroblasts are key players in dermal wound healing. We propose that fibroblasts are terminally modified in chronic wounds and actively contribute to their pathogenesis, conceptually similar to cancer-associated fibroblasts. Our aim is to understand the molecular pathways dysregulated in chronic wound-associated fibroblasts (cWAFs) and their influence on disease.

We employ mass spectrometry-based proteomics to study disease relevant perturbations in protein abundances, putting emphasis on the role of the extracellular matrix (ECM). Amongst others, we are interested in how the ECM is altered in disease and how it influences intracellular protein homeostasis. A common feature that is observed in many diseases is an alteration of lysosomal protein degradation. This may lead on the one hand to accumulation of toxic protein aggregates and on the other hand to increased secretion of lysosomal proteases promoting tissue inflammation and damage. We are interested in the molecular mechanisms that alter protein degradation and secretion and actively contribute to perturbed wound healing and related human diseases.

 
Prof. Jörn Dengjel


Prof. Jörn Dengjel
University of Fribourg
Department of Biology
Chemin du Musée 10
1700 Fribourg

Email   Website

Selected publications

SKINTEGRITY.CH Principal Investigators are in bold:

  • Zhou J, Rasmussen NL, Olsvik HL, Akimov V, Hu Z, Evjen G, Kaeser-Pebernard S, Sankar DS, Roubaty C, Verlhac P, van de Beek N, Reggiori F, Abudu YP, Blagoev B, Lamark T, Johansen T & Dengjel J (2023). TBK1 phosphorylation activates LIR-dependent degradation of the inflammation repressor TNIP1. J Cell Biol, 222(2). e202108144.
  • Martínez-Martínez E, Tölle R, Donauer J, Gretzmeier C, Bruckner-Tuderman L & Dengjel J (2021). Increased abundance of Cbl E3 ligases alters PDGFR signaling in recessive dystrophic epidermolysis bullosa. Matrix Biol, 103. pp. 58-73.
  • Berberich B, Thriene K, Gretzmeier C, Kühl T, Bayer H, Athanasiou I, Rafei-Shamsabadi DA, Bruckner-Tuderman L, Nyström A, Kiritsi D & Dengjel J. (2020). Proteomic profiling of fibroblasts isolated from chronic wounds identifies disease-relevant signaling pathways. J Invest Dermatol, 140(11), pp. 2280-2290.
  • Dengjel J, Bruckner-Tuderman L & Nyström A. (2020). Skin proteomics - analysis of the extracellular matrix in health and disease. Expert Rev Proteomics, 17(5), pp. 377-391.