Post-translational modifications of lens crystallins are believed to play a major role in the development of human senile cataract.
To determine the effect of the modification of intraocular lens (IOL) surface properties on the adhesion of Staphylococcus epidermidis caused by fibronectin (FN) as the predominant proadhesive glycoprotein of the eye's initial foreign body reaction.
The excess oxidative stress was previously reported to induce extensive oxidative modifications on lens proteins especially α-crystalline protein, a major protein component of the mammalian eye lens resulting in the enhanced lens opacity [ 24, 25].
To identify the sites of DHA-and DHB-mediated modification, trypsin digests of lens fiber cell membrane fraction prepared from a 37-year-old and 58-year-old lens were analyzed by an 11-step multidimensional LC-MS/MS method as described previously (Wang et al., 2012).
To determine through safety studies the tissue effects and potential cataractogenesis of laser modification of the crystalline lens (photophaco modulation).
A Gaussian beam of fundamental mode is modulated by a pre-designed phase mask, which is a piecewise modification of an axicon lens, and followed by a Fourier transform to generate an ideal dark hollow beam at the focal plane.
Protein aggregation in the lens fibers as a result of oxidation, protein modifications, and/or proteolysis results in loss of lens transparency and cataract formation [7][50].
These studies will help reveal additional regulatory mechanisms of lens differentiation, such as post-translational modifications (Gong et al., 2014), and will aid the ongoing identification of novel lens disease-associated genes (Lachke et al., 2012).
Cataract is a protein conformational disease caused by posttranslational modifications of the structural lens proteins [3].
It is well established that the precise arrangement and packing of fibers in a crystalline array contributes to lens transparency [ 10, 20] and conversely, that any disruption or modification of this exact fiber arrangement adversely affects lens function[ 72, 73].
