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NCCs express multiple integrin subtypes with differential binding affinity to distinct ECM ligands.
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Meanwhile, a design using homology models of other integrin subtypes has also been successfully applied.
Special emphasis is placed on the activity and selectivity of the ligands to integrin subtypes.
A "spatial screening" procedure was used to identify highly active and selective ligands for the integrin subtypes αvβ3 and αIIbβ3.
Cyclic RGDfK and RGDyK compounds have a high affinity in the nanomolar range to αvβ3 and αvβ5 and have selectivity over other integrin subtypes [22, 23].
This morphology change is associated with a switch in integrin subtypes.
The α2 and β1 integrin subtypes were dramatically elevated, integrins α1 and α6 were lowered, whereas α5 was nearly lost in PC3res.
Fibrinogen is recognized by multiple integrin and non-integrin receptors found on tumor cells, stromal cells, and inflammatory cells.
There are at least eighteen α and eight β integrin isoforms, and the combination of α/β integrin subtypes determines the specific ECM protein to which each integrin binds.
Multiple integrin subunits have been found in the normal optic nerve head (Table 2).
Although the involvement of particular integrin combinations, essential for angiogenesis, remains controversial, it is likely that multiple integrin attack prevents compensatory mechanisms.
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