Proteomics

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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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Publications

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]

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