Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

It is well established that the expression profiles of multiple and possibly redundant matrix-remodeling proteases (e.g., collagenases) differ strongly in health, disease, and development. Although enzymatic redundancy might be inferred from their close similarity in structure, their in vivo activity can lead to extremely diverse tissue-remodeling outcomes. We observed that proteolysis of collagen-rich natural extracellular matrix (ECM), performed uniquely by individual homologous proteases, leads to distinct events that eventually affect overall ECM morphology, viscoelastic properties, and molecular composition. We revealed striking differences in the motility and signaling patterns, morphology, and gene-expression profiles of cells interacting with natural collagen-rich ECM degraded by different collagenases. Thus, in contrast to previous notions, matrix-remodeling systems are not redundant and give rise to precise ECM-cell crosstalk. Because ECM proteolysis is an abundant biochemical process that is critical for tissue homoeostasis, these results improve our fundamental understanding its complexity and its impact on cell behavior.

Original publication




Journal article


Proceedings of the National Academy of Sciences of the United States of America

Publication Date





10884 - 10889


Department of Biological Regulation, Weizmann Institute of Science, Rehovot 76100, Israel;


Cell-Matrix Junctions, Extracellular Matrix, Fibroblasts, Animals, Humans, Rats, Collagen, Imaging, Three-Dimensional, Rheology, Sequence Homology, Amino Acid, Viscosity, Principal Component Analysis, Elasticity, Matrix Metalloproteinase 1, Matrix Metalloproteinase 13, Proteolysis