Citation:Liu H,Anders F,Funke S,Mercieca K,Grus F,Prokosch V.Proteome alterations in aqueous humour of primary open angle glaucoma patients.Int J Ophthalmol 2020;13(1):176-179,doi:10.18240/ijo.2020.01.24
Proteome alterations in aqueous humour of primary open angle glaucoma patients
Received:July 23, 2019  Revised:November 20, 2019
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DOI:10.18240/ijo.2020.01.24
Key Words:primary open angle glaucoma  aqueous humor  proteomics  Wnt signaling pathway
Fund Project:Suppored by German Research Foundation (DFG 1569 1-1).
                 
AuthorInstitution
Hanhan Liu Department of Ophthalmology, University Medical Center of the Johannes Gutenberg University Mainz, Mainz 55131, Germany; Experimental and Translational Ophthalmology, Department of Ophthalmology, University Medical Center of the Johannes Gutenberg University Mainz, Mainz 55131, Germany
Fabian Anders Experimental and Translational Ophthalmology, Department of Ophthalmology, University Medical Center of the Johannes Gutenberg University Mainz, Mainz 55131, Germany
Sebastian Funke Experimental and Translational Ophthalmology, Department of Ophthalmology, University Medical Center of the Johannes Gutenberg University Mainz, Mainz 55131, Germany
Karl Mercieca Royal Eye Hospital, School of Medicine, University of Manchester, Manchester M202UL, United Kingdom
Franz Grus Experimental and Translational Ophthalmology, Department of Ophthalmology, University Medical Center of the Johannes Gutenberg University Mainz, Mainz 55131, Germany
Verena Prokosch Department of Ophthalmology, University Medical Center of the Johannes Gutenberg University Mainz, Mainz 55131, Germany
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Abstract:
      AIM: To unravel the primary open angle glaucoma (POAG) related proteomic changes in aqueous humour (AH).

    METHODS: Totally 35 patients listed for cataract surgery (controls: n=12, age: 67.4±13.6y) or trabeculectomy for POAG (n=23, age: 72.5±8.3y) were included. AH samples of those patients were obtained during cataract surgery or trabeculectomy. AH samples were subsequently pooled into the experimental groups under equal contribution in terms of protein amount of each individual patient. Protein samples were analyzed by a linear trap quadrupol Orbitrap Mass Spectrometry device with an upstream liquid chromatography system. The obtained raw data were analyzed using the Maxquant proteome software and compared. Proteins with a fold-change ratio higher than a cut-off of 2 were considered as noticeably altered.

    RESULTS: A total number of 175 proteins could be identified out of the AH from POAG and cataract by means of quantitative mass spectrometric analysis. Apolipoprotein D (fold change, 3.16 times), complement C3 (2.96), pigment epithelium-derived factor (2.86), dickkopf-related protein 3 (2.18) and wingless-related integration (Wnt) inhibitory factor 1 (2.35) were significantly upregulated within the AH of glaucoma compared to cataract serving as controls.

    CONCLUSION: AH provides a tool to analyze changes in glaucoma and shows striking changes in Wnt signaling inhibitory molecules and other proteins.

PMC FullText Html:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6942938/
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