Institute of Fundamental Technological Research
Polish Academy of Sciences

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K.A. Jansen

FOM Institute AMOLF (NL)

Recent publications
1.  Piechocka I.K., Jansen K.A., Broedersz C.P., Kurniawan N.A., MacKintosh F.C., Koenderink G.H., Multi-scale strain-stiffening of semiflexible bundle networks, SOFT MATTER, ISSN: 1744-683X, DOI: 10.1039/c5sm01992c, Vol.12, No.7, pp.2145-2156, 2016

Abstract:
Bundles of polymer filaments are responsible for the rich and unique mechanical behaviors of many biomaterials, including cells and extracellular matrices. In fibrin biopolymers, whose nonlinear elastic properties are crucial for normal blood clotting, protofibrils self-assemble and bundle to form networks of semiflexible fibers. Here we show that the extraordinary strain-stiffening response of fibrin networks is a direct reflection of the hierarchical architecture of the fibrin fibers. We measure the rheology of networks of unbundled protofibrils and find excellent agreement with an affine model of extensible wormlike polymers. By direct comparison with these data, we show that physiological fibrin networks composed of thick fibers can be modeled as networks of tight protofibril bundles. We demonstrate that the tightness of coupling between protofibrils in the fibers can be tuned by the degree of enzymatic intermolecular crosslinking by the coagulation factor XIII. Furthermore, at high stress, the protofibrils contribute independently to the network elasticity, which may reflect a decoupling of the tight bundle structure. The hierarchical architecture of fibrin fibers can thus account for the nonlinearity and enormous elastic resilience characteristic of blood clots.

Affiliations:
Piechocka I.K. - other affiliation
Jansen K.A. - FOM Institute AMOLF (NL)
Broedersz C.P. - Princeton University (US)
Kurniawan N.A. - Eindhoven University of Technology (NL)
MacKintosh F.C. - Vrije Universiteit (NL)
Koenderink G.H. - FOM Institute AMOLF (NL)
2.  Jansen K.A., Bacabac R.G., Piechocka I.K., Koenderink G.H., Cells actively stiffen fibrin networks by generating contractile stress, BIOPHYSICAL JOURNAL, ISSN: 0006-3495, DOI: 10.1016/j.bpj.2013.10.008, Vol.105, No.10, pp.2240-2251, 2013

Abstract:
During wound healing and angiogenesis, fibrin serves as a provisional extracellular matrix. We use a model system of fibroblasts embedded in fibrin gels to study how cell-mediated contraction may influence the macroscopic mechanical properties of their extracellular matrix during such processes. We demonstrate by macroscopic shear rheology that the cells increase the elastic modulus of the fibrin gels. Microscopy observations show that this stiffening sets in when the cells spread and apply traction forces on the fibrin fibers. We further show that the stiffening response mimics the effect of an external stress applied by mechanical shear. We propose that stiffening is a consequence of active myosin-driven cell contraction, which provokes a nonlinear elastic response of the fibrin matrix. Cell-induced stiffening is limited to a factor 3 even though fibrin gels can in principle stiffen much more before breaking. We discuss this observation in light of recent models of fibrin gel elasticity, and conclude that the fibroblasts pull out floppy modes, such as thermal bending undulations, from the fibrin network, but do not axially stretch the fibers. Our findings are relevant for understanding the role of matrix contraction by cells during wound healing and cancer development, and may provide design parameters for materials to guide morphogenesis in tissue engineering.

Affiliations:
Jansen K.A. - FOM Institute AMOLF (NL)
Bacabac R.G. - FOM Institute AMOLF (NL)
Piechocka I.K. - other affiliation
Koenderink G.H. - FOM Institute AMOLF (NL)

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