The quantity and conformation of lysozyme and the quantity of lipid deposited on hydrogel contact lenses is significantly influenced by the composition of the lens material. SH contact lens materials deposit low levels of lysozyme and high levels of lipid deposition compared with ionic contact lens materials. Although SH materials deposit only small amounts of lysozyme, the degree of lysozyme denaturation that occurs is higher relative to that seen on ionic lens materials.

Linker of Nucleoskeleton and Cytoskeleton (LINC) complexes span the nuclear envelope and transduce force from dynamic cytoskeletal networks to the nuclear lamina. Here we show that LINC complexes also signal from the nuclear envelope to critical regulators of the actin cytoskeleton. Specifically, we find that LINC complexes that contain the inner nuclear membrane protein Sun2 promote focal adhesion assembly by activating the small GTPase RhoA. A key effector in this process is the transcription factor/coactivator complex composed of SRF/Mkl1. A constitutively active form of SRF/Mkl1 was not sufficient to induce focal adhesion assembly in cells lacking Sun2, however, suggesting that LINC complexes support RhoA activity through a transcription-independent mechanism. Strikingly, we also find that the inner nuclear membrane protein Sun1 antagonizes Sun2 LINC complexes and inhibits RhoA activation and focal adhesion assembly. Thus different LINC complexes have opposing roles in the transcription-independent control of the actin cytoskeleton through the small GTPase RhoA.

The quantity and conformation of lysozyme deposited on hydrogel contact lens materials is significantly influenced by both lens material and care regimen.