Defining the proteome of human iris,ciliary body,retinal pigment epithelium,and choroid |
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| Authors: | Pingbo Zhang David Kirby Craig Dufresne Yan Chen Randi Turner Sara Ferri Deepak P Edward Jennifer E Van Eyk Richard D Semba |
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| Institution: | 1. Department of Ophthalmology, Johns Hopkins University School of Medicine, Baltimore, MD, USA;2. Thermo Fisher Scientific, West Palm Beach, FL, USA;3. King Khaled Eye Specialist Hospital, Riyadh, Kingdom of Saudi Arabia;4. Advanced Clinical Biosystems Research Institute, Cedars‐Sinai Medical Center, Los Angeles, CA, USA;5. Department of Medicine, The Heart Institute, Cedars‐Sinai Medical Center, Los Angeles, CA, USA |
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| Abstract: | The iris is a fine structure that controls the amount of light that enters the eye. The ciliary body controls the shape of the lens and produces aqueous humor. The retinal pigment epithelium and choroid (RPE/choroid) are essential in supporting the retina and absorbing light energy that enters the eye. Proteins were extracted from iris, ciliary body, and RPE/choroid tissues of eyes from five individuals and fractionated using SDS‐PAGE. After in‐gel digestion, peptides were analyzed using LC‐MS/MS on an Orbitrap Elite mass spectrometer. In iris, ciliary body, and RPE/choroid, we identified 2959, 2867, and 2755 nonredundant proteins with peptide and protein false‐positive rates of <0.1% and <1%, respectively. Forty‐three unambiguous protein isoforms were identified in iris, ciliary body, and RPE/choroid. Four “missing proteins” were identified in ciliary body based on ≥2 proteotypic peptides. The mass spectrometric proteome database of the human iris, ciliary body, and RPE/choroid may serve as a valuable resource for future investigations of the eye in health and disease. The MS proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE partner repository with the dataset identifiers PXD001424 and PXD002194. |
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| Keywords: | Biomedicine Choroid Ciliary body Eye Iris Retinal pigment epithelium |
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