Dataset Information

The proteome of human iris

ABSTRACT: The iris is a fine structure that controls the amount of light that enters the eye. Iris diseases that result in visual disability and blindness include iritis, primary angle closure glaucoma, and pigment dispersion syndrome. A detailed investigation of the proteome of the normal human iris may provide a foundation for new investigations into the iris biology and pathophysiology. We conducted an in-depth proteomic analysis of five normal irides. Proteins were fractionated using SDS-PAGE. After in-gel digestion, peptides were analyzed using LC-MS/MS on an Orbitrap Elite mass spectrometer. We identified 3,000 non-redundant proteins in the human iris, including 26 unambiguous protein isoforms. The proteins identified in the iris included numerous proteins involved in smooth muscle motility, melanosome development, extracellular matrix, and selenoproteins involved in redox signaling. The MS proteome database of the human iris may serve as a valuable resource for future investigations of the eye in health and disease.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Richard D. Semba

PROVIDER: MSV000081765 | MassIVE | Wed Nov 29 12:31:00 GMT 2017

SECONDARY ACCESSION(S): PXD001424

REPOSITORIES: MassIVE

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

Zhang Pingbo P Kirby David D Dufresne Craig C Chen Yan Y Turner Randi R Ferri Sara S Edward Deepak P DP Van Eyk Jennifer E JE Semba Richard D RD

Proteomics 20160311 7

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/M ...[more]

PMID: 26834087

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Project description:The choroid is the vascular layer situated between the outer sclera and the inner retina. Together with the ciliary body and the iris it forms the uvea. Because of its rich blood supply it is also called the nutritive layer and it supplies oxygen and nutrition to the retinal pigment epithelium and the outer retina. Due to its vascular nature it acts as a heat sink and helps in thermoregulation within the eye. It also contains a pigment “melanin”, which absorbs excess light within the eye and prevents scattering. . The human choroid is thickest posteriorly where it measures 0.2 mm, whereas anteriorly it measures 0.1 mm.. The aim of this study was to characterize the choroid proteome to generate a resource for future studies on the choroid . The method used in this study combined bRPLC and LC-MS/MS analysis of the proteins isolated from the three cadaver samples of healthy donors. Subsequently, we classified the proteins based on gene ontology and pathway analysis. A total of 5,249 non redundant proteins were identified in the human choroid. Gene ontology classification pinpointed proteins involved in protein metabolism, regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolism, transport, cell growth and/or maintenance and immune response. Several proteins identified in normal choroid have previously been identified in human choroid where these proteins are related to glaucoma, ocular inflammation, toxoplasmic retinochoroiditis, diabetic retinopathy, open-angle glaucoma and Grave’s disease. The top canonical pathway in which the choroid proteins participated are EIF2 signaling, integrin signalling, mitochondrial dysfunction, regulation of eIF4 and p70S6K signaling and clathrin-mediated endocytosis signalling. Around 800 choroid proteins were related to infectious diseases. The results of this study illustrate the largest number of proteins identified in human choroid and may serve as a valuable resource for future investigations of choroid biology and disease. Proteomic analysis of choroid proteins could provide versatile information to understand choroidal functions and the underlying pathogenesis of choroidal pathologies.