Alexa Klettner1, Andreas Tholey2, Alena Wiegandt2, Elisabeth Richert1, Bernhard Nölle1, Günther Deuschl3, Johann Roider1, Susanne A Schneider3,4. 1. Department of Ophthalmology, University Hospital Schleswig-Holstein, Campus Kiel, Kiel, Germany. 2. Systematic Proteomics & Bioanalytics, Inst. Experimental Medicine, Christian-Albrechts-Universität zu Kiel, Kiel, Germany. 3. Department of Neurology, University Hospital Schleswig-Holstein, Campus Kiel, Kiel, Germany. 4. Department of Neurology, Ludwig-Maximilians-University Munich, Klinikum Großhadern, Munich, Germany.
Abstract
BACKGROUND: We previously showed that the protein pattern of lenses removed in cataract surgery differs between patients with Parkinson's disease and age-matched controls. In this study, we identified the protein reduced in abundance in the 34- to 37-kDa gel band. METHODS: During cataract surgery (phacoemulsification), we collected the rinsing fluid and lens particles from the eyes of PD patients and controls. Residual lens fragments in the supernatant of 3 PD patients and aged-matched controls were studied for protein profiles using liquid chromatography-mass spectrometry and Western blots. RESULTS: We identified glyceraldehyde-3-phosphate dehydrogenase by mass spectrometry as the protein reduced in abundance and verified this finding in Western blots. CONCLUSIONS: Glyceraldehyde-3-phosphate dehydrogenase has been implicated in PD development. The reduction of glyceraldehyde-3-phosphate dehydrogenase in the lenses of PD patients may be a new biomarker for PD and might also indicate an important role for this protein in PD development.
BACKGROUND: We previously showed that the protein pattern of lenses removed in cataract surgery differs between patients with Parkinson's disease and age-matched controls. In this study, we identified the protein reduced in abundance in the 34- to 37-kDa gel band. METHODS: During cataract surgery (phacoemulsification), we collected the rinsing fluid and lens particles from the eyes of PDpatients and controls. Residual lens fragments in the supernatant of 3 PDpatients and aged-matched controls were studied for protein profiles using liquid chromatography-mass spectrometry and Western blots. RESULTS: We identified glyceraldehyde-3-phosphate dehydrogenase by mass spectrometry as the protein reduced in abundance and verified this finding in Western blots. CONCLUSIONS:Glyceraldehyde-3-phosphate dehydrogenase has been implicated in PD development. The reduction of glyceraldehyde-3-phosphate dehydrogenase in the lenses of PDpatients may be a new biomarker for PD and might also indicate an important role for this protein in PD development.
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