Live Cells Process Exogenous Peptide as Fibronectin Fibrillogenesis In Vivo

Force-induced fibronectin fibrillogenesis in vitro†

Adsorption-induced fibronectin aggregation and fibrillogenesis.

Fibronectin (Fn), a high molecular weight glycoprotein, is a central element of extracellular matrix architecture that is involved in several fundamental cell processes. In the context of bone biology, little is known about the influence of the mineral surface on fibronectin supramolecular assembly. We investigate fibronectin morphological properties induced by its adsorption onto a model miner...

Interdomain association in fibronectin: insight into cryptic sites and fibrillogenesis.

The process by which fibronectin (FN), a soluble multidomain protein found in tissue fluids, forms insoluble fibrillar networks in the extracellular matrix is poorly understood. Cryptic sites found in FN type III domains have been hypothesized to function as nucleation points, thereby initiating fibrillogenesis. Exposure of these sites could occur upon tension-mediated mechanical rearrangement ...

Localization of cell surface sites involved in fibronectin fibrillogenesis

Fibronectin binding sites on cultured human fibroblasts were localized by high voltage electron microscopy using either 5- or 18-nm colloidal gold beads (Au5 or Au18) bound to intact fibronectin, the 70-kD amino-terminal fragment of fibronectin that blocks incorporation of exogenous fibronectin into extracellular matrix, or 160-180-kD fragments of fibronectin with cell adhesion and heparin-bind...

Role of Material-Driven Fibronectin Fibrillogenesis in Protein Remodeling

Protein remodeling at the cell-material interface is an important phenomenon that should be incorporated into the design of advanced biomaterials for tissue engineering. In this work, we address the relationship between fibronectin (FN) activity at the material interface and remodeling, including proteolytic cascades. To do so, we studied FN adsorption on two chemically similar substrates, poly...