Journal Highlight: Defining the proteome of human iris, ciliary body, retinal pigment epithelium, and choroid

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  • Published: May 23, 2016
  • Author: spectroscopyNOW
  • Channels: Proteomics
thumbnail image: Journal Highlight: Defining the proteome of human iris, ciliary body, retinal pigment epithelium, and choroid
The mass spectrometric proteome of the human iris, ciliary body, and retinal pigment epithelium/choroid has been determined and the data deposited in the ProteomeXchange Consortium

Defining the proteome of human iris, ciliary body, retinal pigment epithelium, and choroid

Proteomics, 2016, 16, 1146-1153
Pingbo Zhang, David Kirby, Craig Dufresne, Yan Chen, Randi Turner, Sara Ferri, Deepak P. Edward, Jennifer E. Van Eyk and Richard D. Semba

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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