Roger JW Truscott, Michael Friedrich,Michelle Hooi, Brian Lyons
To elucidate the molecular basis for humanage-related cataract.
Proteomic analysis of whole nuclei, dis-sected from lenses of cataract patients and age-matched normal controls, were utilised. Trypticdigestion was coupled with Liquid Chromatography/Mass Spectrometry/ Mass Spectrometry.
Over time, the crystallin proteins of the lens,which do not turn over, progressively degrade. Usingproteomic techniques we have been able to elucidatethe major modifications that take place with age.The main processes were found to be racemisation,deamidation and truncation.In many cases, the extent of modification at particularsites did not differ between the normal and the cataractlenses, however at certain sites there was a signifi-cantly greater degree of modification in the cataract lenses.
Proteomics may have established theroot cause of the major human blinding condition,age-related cataract. Cataract appears to result fromsite-specific decomposition of particular long-livedmacromolecules in the human lens.
GLISTENINGS IN INTRAOCULAR LENSES IN AUSTRALIA AND NEW ZEALAND- A COLLABORATIVE SURGICAL QUALITY AUDIT OVER THE 24 MONTH PERIOD UP TO FEBRUARY 2017. FINDINGS OF THIS AUDIT OF LENSES IMPLANTED BETWEEN 1995 AND 2016, HIGHLIGHT THE ONGOING PRESENCE AND SEVERITY OF VACUOLES EVEN IN THE MOST RECENTLY IMPLANTED LENSES.