The Structural Interactions of Molecular and Fibrillar Collagen Type I with Fibronectin and Its Role in the Regulation of Mesenchymal Stem Cell Morphology and Functional Activity

Abstract

The observed differences in the structure of native tissue and tissue formed in vitro cause the loss of functional activity of cells cultured in vitro. The lack of fundamental knowledge about the protein mechanism interactions limits the ability to effectively create in vitro native tissue. Collagen is able to spontaneously assemble into fibrils in vitro, but in vivo, other proteins, for example fibronectin, have a noticeable effect on this process. The molecular or fibrillar structure of collagen plays an equally important role. Therefore, we studied the interaction of the molecular and fibrillar structure of collagen with fibronectin. Atomic force and transmission electron microscopy showed that the presence of fibronectin does not affect the native structure and diameter of collagen fibrils. Confocal microscopy demonstrated that the collagen structure affects the cell morphology. Cells are better spread on molecular collagen compared with cells cultured on fibrillar collagen. Fibronectin promotes the formation of a large number of focal contacts, while in combination with collagen of both forms, its effect is leveled. Thus, understanding the mechanisms of the relationship between the protein structure and composition will effectively manage the creation in vitro of a new tissue with native properties.

BMP-Binding Polysulfonate Brushes to Control Growth Factor Presentation and Regulate Matrix Remodelling

“…In addition to such direct mechanisms, BMP2 is known to bind ECM proteins such as fibronectin [92]. Fibronectin fibre networks are in turn considered to be preliminary to the assembly of more complex ECM fibrous networks and were reported to precede the assembly of collagen I fibres [93,94]. Examination of ECM fibres deposited at the surface of polymer brushes confirmed the abundance of rich and dense fibronectin fibre networks (Figure 7C and Supplementary Figure S12).…”

Plasma Fibronectin as a Novel Predictor of Coronary Heart Disease: A Retrospective Study

“…FN is now considered an indicator of ECM deposition in atherosclerotic processes and may participate in the pathogenesis of CHD, as characterized by the formation of coronary atherosclerotic plaque [29]. It reportedly serves as a bridge between cells and the interstitial collagen meshwork, greatly influencing the migration and proliferation of VSMC during atherosclerosis progression [30,31]. In addition, FN might contribute to the transformation of VSMC from the contractile phenotype to a synthetic phenotype.…”

Focusing on the Native Matrix Proteins in Calcific Aortic Valve Stenosis

“… 41 Fibronectin is necessary for the ordinary collagen fibril packing and is closely associated with calcification. 42 It harbors binding sites for proteoglycans and integrins bridging ECM components with cells. 43 Periostin is essential for the normal embryonic development of the aortic valve.…”

“… 12 In other tissues, mechanical stress-induced myofibroblast activation implicates fibronectin, in a reversible process directly linked to the imposed mechanical forces, 67 which also directly affects matrix metalloproteinase–mediated proteolysis 68 and directly shapes the collagen–fibronectin interactions. 42 In contrast, myofibroblast activation of VICs, results in greater ECM stiffness, as they contract and add mechanical forces upon the remodeling tissue. 69 …”