Premium
Proteome analysis of lipofuscin in human retinal pigment epithelial cells
Author(s) -
Schutt F.,
Ueberle B.,
Schnölzer M.,
Holz F.G.,
Kopitz J.
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03312-4
Subject(s) - lipofuscin , retinal pigment epithelium , retinal , proteome , macular degeneration , chemistry , retinal disorder , proteomics , microbiology and biotechnology , biology , biochemistry , medicine , ophthalmology , gene
Excessive accumulation of lipofuscin in postmitotic retinal pigment epithelial cells is a common pathogenetic pathway in various blinding retinal diseases including age‐related macular degeneration, which is now the most common cause of registerable blindness in the industrialized nations. To better understand the role of lipofuscin accumulation and to manipulate the pathogenetic mechanisms on both experimental and therapeutic levels we analyzed the proteome of isolated human ocular lipofuscin granules from human RPE cells. After homogenization and fractionation by gradient ultracentrifugation of the RPE/choroid complex from 10 pairs of human donors, protein compounds were separated by 2D gel electrophoresis and analyzed using matrix‐assisted laser desorption/ionization mass spectrometry and HPLC‐coupled electrospray tandem mass spectrometry. Besides a better understanding of downstream pathways, this approach may provide new targets for therapeutic interventions in a currently untreatable disease.