Mode of Adsorption and Orientation of an Extracellular Matrix Protein Affect Its Cell-Adhesion-Promoting Activity

Ligand-binding specificities of laminin-binding integrins: A comprehensive survey of laminin–integrin interactions using recombinant α3β1, α6β1, α7β1 and α6β4 integrins

“…Laminin-411 seems to be the least favored ligand for the laminin-binding integrins, since it was only recognized by integrins a6h1 and a7X1h1 with modest affinities. Since laminin-411 has been shown to be prone to inactivation upon drying on plastic surfaces (Kortesmaa et al, 2000) and direct adsorption of extracellular matrix proteins onto plastic surfaces often leads to a reduction in their celladhesive activities (Fitchmun et al, 1998), we cannot exclude the possibility that the modest integrin binding displayed by laminin-411 was partly due to denaturation of laminin-411 on the plastic surface. In contrast, laminin-511/521 was the most favored ligand, binding to all the laminin-binding integrins, except for a7X2h1, with relatively high affinities.…”

Biomaterial–stem cell interactions and their impact on stem cell response

“…While the effect of protein denaturation on stem cell properties has not yet been properly investigated, orientation effects are known and specic interactions between charges on the protein and the substrate surface will inuence the orientation of proteins adsorbing from the serum. 59 The orientation dictates whether the cell surface receptors are able to recognize the individual adhesive proteins and can bind to the corresponding recognition sites. 60 Whereas bronectin was found to adsorb most strongly to hydrophobic surfaces, vitronectin can easily change its arrangement and adheres also to hydrophilic surfaces.…”

Cell micropatterning on an albumin‐based substrate using an inkjet printing technique

“…Cell attachment on a substrate is significantly affected by the adsorbed protein on the substrate. The existence of cell adhesion proteins such as fibronectin, vitronectin, and laminin promotes cell adhesion 20–23. We investigated fibronectin adsorption on cross‐linked albumin substrates printed with PEI in the pattern “FN” by using peroxidase‐labeled fibronectin.…”

“…The existence of cell adhesion proteins such as fibronectin, vitronectin, and laminin promotes cell adhesion. [20][21][22][23] We investigated fibronectin adsorption on cross-linked albumin substrates printed with PEI in the pattern ''FN'' by using peroxidase-labeled fibronectin. As shown in Figure 3, fibronectin adsorption took place on the PEI-printed region but not on the surrounding PEI-nonprinted cross-linked albumin surface.…”