Literature DB >> 26834087

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

Pingbo Zhang1, David Kirby1, Craig Dufresne2, Yan Chen1, Randi Turner1, Sara Ferri1, Deepak P Edward1,3, Jennifer E Van Eyk4,5, Richard D Semba1.   

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.
© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

Entities:  

Keywords:  Biomedicine; Choroid; Ciliary body; Eye; Iris; Retinal pigment epithelium

Mesh:

Substances:

Year:  2016        PMID: 26834087      PMCID: PMC4833206          DOI: 10.1002/pmic.201500188

Source DB:  PubMed          Journal:  Proteomics        ISSN: 1615-9853            Impact factor:   3.984


  10 in total

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  10 in total

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