Abstract
BackgroundThe cell-material interaction is a complex bi-directional and dynamic process that mimics to a certain extent the natural interactions of cells with the extracellular matrix. Cells tend to adhere and rearrange adsorbed extracellular matrix (ECM) proteins on the material surface in a fibril-like pattern. Afterwards, the ECM undergoes proteolytic degradation, which is a mechanism for the removal of the excess ECM usually approximated with remodeling. ECM remodeling is a dynamic process that consists of two opposite events: assembly and degradation.Methodology/Principal FindingsThis work investigates matrix protein dynamics on mixed self-assembled monolayers (SAMs) of –OH and –CH3 terminated alkanethiols. SAMs assembled on gold are highly ordered organic surfaces able to provide different chemical functionalities and well-controlled surface properties. Fibronectin (FN) was adsorbed on the different surfaces and quantified in terms of the adsorbed surface density, distribution and conformation. Initial cell adhesion and signaling on FN-coated SAMs were characterized via the formation of focal adhesions, integrin expression and phosphorylation of FAKs. Afterwards, the reorganization and secretion of FN was assessed. Finally, matrix degradation was followed via the expression of matrix metalloproteinases MMP2 and MMP9 and correlated with Runx2 levels. We show that matrix degradation at the cell material interface depends on surface chemistry in MMP-dependent way.Conclusions/SignificanceThis work provides a broad overview of matrix remodeling at the cell-material interface, establishing correlations between surface chemistry, FN adsorption, cell adhesion and signaling, matrix reorganization and degradation. The reported findings improve our understanding of the role of surface chemistry as a key parameter in the design of new biomaterials. It demonstrates the ability of surface chemistry to direct proteolytic routes at the cell-material interface, which gains a distinct bioengineering interest as a new tool to trigger matrix degradation in different biomedical applications.
Highlights
The interaction of cells with foreign materials takes place via the adsorbed layer of proteins such as fibronectin (FN), vitronectin, and fibrinogen, representing the soluble matrix proteins in the biological fluids [1]
water contact angle (WCA) decreases as the fraction of hydroxy groups increases from 115u on the methyl terminated self-assembled monolayers (SAMs) to 20u on the hydroxyl terminated one (Figure 1a)
There is a lack of understanding of the cell-material interaction from an integrated point of view that includes the amount and state of the adsorbed layer of proteins on the material surface, cell adhesion - including integrin expression and focal adhesion formation - cell signaling, matrix reorganization, secretion and degradation, i.e. matrix protein dynamics at the cell-material interface
Summary
The interaction of cells with foreign materials takes place via the adsorbed layer of proteins such as fibronectin (FN), vitronectin, and fibrinogen, representing the soluble matrix proteins in the biological fluids [1]. FAK is a key signaling protein contributing to integrin control of cell motility, invasion, survival, and proliferation [4]. It is not surprising that many cells cannot adapt and poorly survive in vitro and, when a foreign material is implanted in the body, the adjacent tissue cells do not interact properly because of lack of their ECM. The cell-material interaction is a complex bi-directional and dynamic process that mimics to a certain extent the natural interactions of cells with the extracellular matrix. Cells tend to adhere and rearrange adsorbed extracellular matrix (ECM) proteins on the material surface in a fibril-like pattern. ECM remodeling is a dynamic process that consists of two opposite events: assembly and degradation
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