Objective: To determine the Protein Profile of cataract lenses in Parkinson’s disease (PD).

Background: Protein accumulation, mainly αB-crystallin, in the lens causes cataract. PD is associated with a higher risk for cataract; the pathophysiology and the protein profile in the PD lens however remain unclear.

Methods: During cataract surgery (phacoemulsification), we collected the rinsing fluid and lens particles from six eyes from PD patients and 9 control eyes. The supernatant, pellet and residual lens fragments in the supernatant (RLFs) were studied for protein profiles using Coomassie or Silver staining and Western blots.

Results: PD patients showed no definite uniform band pattern in the proteins retrieved from the supernatant or pellet; but differences were seen in the RLFS. In Coomassie stains, a band at 30-34 kDa, which was present in all controls, was absent or very lowly expressed in five PD samples. On the other hand, in silver stains, two of these PD samples displayed an additional band at 76 kDa which was absent in controls. αSYN appeared as a single or double band (mean 23.3 and 18.8 kDa); alphaB-crystallin as single band (mean 18.9 kDa). αSYN was prominent in the supernatant but was scarce in the pellet. In PD patients, αSYN in the RLFS tended to be more prominent compared to controls.

Conclusions: An interaction between α-synuclein and αB-crystallin may play a key role in the pathophysiology of cataract development, especially in but not only PD. To our knowledge this is the first human in-vivo study of cataract lens in PD.

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MDS Abstracts - https://www.mdsabstracts.org/abstract/alpha-synuclein-and-crystallin-expression-in-human-lens-in-parkinsons-disease/