Microstructural and mechanical differences between digested collagen-fibrin co-gels and pure collagen and fibrin gels.

TL;DR: This work reviews existing models of endothelial assembly in fibrin gel and posits that differerences between models are partially caused by microstructural differences in fibin gel.

TL;DR: This consistent biomechanical characterization provides a detailed and robust starting point for different 3D in vitro bioapplications, such as collagen and/or fibrin gels, which may have major implications for 3D cellular behavior by inducing divergent microenvironmental cues.

TL;DR: To create a pre-stressed model system, co-gels were fabricated from a combination of hyaluronic acid (HA) and reconstituted Type-I collagen (Col) to swell as the HA imbibes water, which in turn stretches (and stresses) the collagen network.

TL;DR: In this article, anisotropic mechanical resistance hypothesis of contact guidance was tested for human dermal fibroblasts in an aligned fibril network and the cross-linking was shown to increase the mechanical resistance anisotropy, without detectable change in network microstructure and without change in cell adhesion to the crosslinked fibrin gel.

TL;DR: The collagen superfamily of proteins now contains at least 19 proteins formally defined as collagens and an additional ten proteins that have collagen-like domains, and a number of experiments suggest it may be possible to inhibit collagen synthesis with oligo-nucleotides or antisense genes.

TL;DR: In addition to its primary role of providing scaffolding for the intravascular thrombus and also accounting for important clot viscoelastic properties, fibrin(ogen) participates in other biologic functions involving unique binding sites, some of which become exposed as a consequence of fibrIn formation.

TL;DR: Preliminary evidence from invertebrates is included which suggests that the principles for bipolar fibril assembly were established at least 500 million years ago, and how mature fibrils are assembled from early fibrILS is reviewed.

TL;DR: It was observed that the strain within collagen fibrils is always considerably smaller than in the whole tendon, which points toward the existence of additional gliding processes occurring at the interfibrillar level.