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A retinal proteomics‐based study identifies αA‐crystallin as a sex steroid‐regulated protein
Author(s) -
D'Anna Claudia,
Cascio Caterina,
Cigna Diego,
Galizzi Giacoma,
Deidda Irene,
Bianchi Laura,
Russo Domenica,
Passantino Rosa,
Bini Luca,
Guarneri Patrizia
Publication year - 2011
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201000561
Subject(s) - proteomics , crystallin , biology , heat shock protein , fatty acid binding protein , proteome , neurodegeneration , steroid , microbiology and biotechnology , biochemistry , gene , medicine , hormone , disease
Abstract Sex steroids influence the structural and functional organization of ocular tissues, promote survival in several pathological conditions including retinal neurodegeneration and have a prominent role in age‐related eye diseases as well as neurodegenerative diseases. However, their underlying mechanisms are still elusive. We explored proteomic profiling of rat retinas following intravitreal injection of the bioactive 17β‐estradiol or androgen dihydrotestosterone. Using narrow range 2‐DE gels and MALDI‐TOF‐MS analysis, we identified three sex steroid‐regulated proteins: the galectin‐related‐inter‐fiber (GRIFIN) which is a galectin family member protein of unknown function, the fatty acid‐binding protein epidermal‐5 (FABP5) protein responsible for the fatty acid uptake and transport and the small heat shock αA‐crystallin (CRYAA) protein involved in preventing aggregation of denatured or unfolded proteins. Changes in the expression of these proteins revealed a predominant estrogenic effect and the multiple CRYAA protein species reflected posttranslational modifications. Sex steroid‐mediated modifications of CRYAA were confirmed by Western blotting analysis. This study provides new target proteins for sex steroids with a potential link to age‐related diseases associated with proteotoxic stress.