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Adhesion force mostly represents the number and distribution of cell surface adhesion molecules[24].
The structures of many cell surface adhesion proteins comprise multiple tandem repeats of structurally similar domains.
Likewise, as differentiation continued, there were fewer cell surface adhesion proteins, and the adhesion force and R a decreased.
SOS5 has been shown to be a putative cell surface adhesion protein that is required for normal cell expansion.
Disruption of the endothelial-glycocalyx barrier exposes endothelial cell surface adhesion molecules that trigger the activation of mast cells, and the adhesion of platelets and white blood cells, thereby causing further inflammation [72] and nitric oxide production [73].
Integrins constitute the main cell surface adhesion receptors mediating cell-ECM adhesion.
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The integrins are a major family of cell surface-adhesion receptors involved in cell cell, cell matrix and cell pathogen interactions (23).
It was shown that hepatocyte aggregate morphology was mainly governed by a balance between cell contraction forces and cell-surface adhesion forces.
Many advances have also been made using parallel plate flow chambers to study the dynamics of cell-surface adhesion [29], [30].
Urokinase that also binds the RGG domain of nucleolin is implicated in mechanisms regulating pericellular proteolysis, cell-surface adhesion, and mitogenesis [21], [24].
These results plus those of the adhesion assay suggest that cell-surface adhesion in the normal ONH in vivo by AA astrocytes may differ than that of CA astrocytes.
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