Fibronectin (FN) is a component of the interstitial ECM. It also mediates cell attachment and function [16]. It is a fibril-forming glycoprotein which is structurally a dimer of two identical proteins of 250 kDa covalently attached via disulfide bonds at their C termini. It is ubiquitously expressed in tissues. Different functional motifs on its structure helps fibronectin to interact with GAGs, collagens, fibrin and integrins facilitating matrix organization and cell-matrix interactions [18]. For example, fibronectin serves as a template for proper collagen fibrillogenesis by forming a fibril…mehr
Fibronectin (FN) is a component of the interstitial ECM. It also mediates cell attachment and function [16]. It is a fibril-forming glycoprotein which is structurally a dimer of two identical proteins of 250 kDa covalently attached via disulfide bonds at their C termini. It is ubiquitously expressed in tissues. Different functional motifs on its structure helps fibronectin to interact with GAGs, collagens, fibrin and integrins facilitating matrix organization and cell-matrix interactions [18]. For example, fibronectin serves as a template for proper collagen fibrillogenesis by forming a fibril network engaged by cell surface integrins [16]. Cellular traction force causes FN to be stretched several times over its resting length [18]. As a result of such stretching, cryptic integrin-binding sites within the FN molecule is exposed resulting in pleiotropic changes in cellular behavior [18]. Hence FN acts as an extracellular mechano-regulator in addition to its role in cell migration during development. Studies have also shown the implication of FN in cardiovascular diseases and tumor metastasis
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