Molecular mechanisms of cell adehsion
The Gullberg laboratory has characterized the integrin α11β1, which is expressed on subsets of normal fibroblasts and on carcinoma-associated fibroblasts. Cells lacking α11β1 display disturbed cell-collagen interactions, altered metalloproteinase synthesis and reduced cell proliferation. Major projects within the group aim to further understand the role of this collagen receptor and other fibroblast integrins during health and in disease.
- (2022). Upregulated integrin α11 in the stroma of cutaneous squamous cell carcinoma promotes skin carcinogenesis. Frontiers in Oncology.
- (2022). Integrin α11β1 in tumor fibrosis: more than just another cancer-associated fibroblast biomarker? Journal of cell communication and signaling.
- (2022). Integrin α11β1 and syndecan-4 dual receptor ablation attenuates cardiac hypertrophy in the pressure overloaded heart. American Journal of Physiology. Heart and Circulatory Physiology. H1057-H1071.
- (2021). Selectivity of the collagen-binding integrin inhibitors, TC-I-15 and obtustatin. Toxicology and Applied Pharmacology.
- (2021). Role of evolutionary conserved residues in integrin α11 cytoplasmic tail.
- (2021). Collagen assembly at the cell surface: dogmas revisited. Cells. 1-22.
- (2020). Integrin α11β1 is a receptor for collagen XIII. Cell and Tissue Research.
- (2020). Generation of a novel mouse strain with fibroblast-specific expression of Cre recombinase. Matrix Biology Plus.
1990 Phd Medical Chemistry, Uppsala University
1990-1992 Post Doc, Molecular Biology Institute, University of California Los Angeles
1993-2003 Researcher, Uppsala University
2004- today Professor, Department of Biomedicine, UoB