Extracellular matrix-cell interactions Sample Clauses

Extracellular matrix-cell interactions. 2.4.1 Extracellular matrix in embryonic development In addition to the intrinsic properties of ESCs that direct cell fate, embryonic development is also governed by ECM-growth factor interactions. At the earliest stages of embryogenesis, cellsbegin to produce endogenous ECM components such as collagen, laminin, fibronectin, and glycosaminoglycans (GAGs) that serve an important role in the regulation of cellular proliferation and differentiation during [55–58]. For instance, laminin appears as early as the 2-cell stage [59] and fibronectin and type IV collagen appear in the inner cell mass of day 3/4 blastocysts [60]. The ECM functions to control the spatiotemporal release of growth factors, facilitate growth factor-receptor interactions, and mediate morphogen gradients by providing a reservoir of proteins [61]. During cell specification, the ECM also serves to define boundaries between different cell types and provide scaffolding for developing organs. Furthermore, ECM facilitates cellular migration by providing an adhesive substrate for cell attachment during embryogenesis. GAGs function to form morphogen gradients during early embryonic development by sequestration of secreted growth factors, thus directing the pattern of tissue morphogenesis. GAGs are ubiquitous in the pericellular space and are found bound to core proteins present on the cell surface and within the extracellular matrix. GAGs are composed of linear polysaccharide chains consisting of repeating disaccharide units of an amino sugar (N-acetylglucosamine or N-acetylgalactosamine) and an uronic sugar (glucuronic acid or iduronic acid) or galactose and are classified into four types known as heparin/heparin sulfate (HS), chondroitin sulfate (CS)/dermatan sulfate (DS), keratan sulfate (KS), and hyaluronic acid (HA). In particular, HS has been extensively studied for its role in embryonic development, specifically in the regulation of FGF signaling where HS facilitates the formation of the FGF-FGFR complex [62–64]. Heparan sulfate (HS) is a negatively charged GAG that binds via electrostatic interactions to growth factors including VEGF, FGF2, and PDGF [65,66]. The sugar structure of HS chains consist of repeating units of glucuronic acid (GlcUA) and N- acetylglucosamine (GlcNAc), which are polymerized by the enzymatic complex Exostosin1/2 (EXT1/EXT2) during chain eleongation [67]. The backbone of HS is subjected to further modification such as de-N-acetylation, N-sulfation, 6-O-sulfation, 3- O...
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