http://www.cnr.it/ontology/cnr/individuo/prodotto/ID12581
A retinal proteomics-based study identifies aA-crystallin as a sex steroid-regulated protein (Articolo in rivista)
- Type
- Label
- A retinal proteomics-based study identifies aA-crystallin as a sex steroid-regulated protein (Articolo in rivista) (literal)
- Anno
- 2011-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1002/pmic.201000561 (literal)
- Alternative label
Claudia DAnna; Caterina Cascio; Diego Cigna; Giacoma Galizzi; Irene Deidda; Laura Bianchi; Domenica Russo; Rosa Passantino; Luca Bini, Patrizia Guarneri (2011)
A retinal proteomics-based study identifies aA-crystallin as a sex steroid-regulated protein
in Proteomics (Weinh., Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Claudia DAnna; Caterina Cascio; Diego Cigna; Giacoma Galizzi; Irene Deidda; Laura Bianchi; Domenica Russo; Rosa Passantino; Luca Bini, Patrizia Guarneri (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Institute of Biomedicine and Molecular Immunology, Palermo, Italy
Laboratory of Functional Proteomics, Molecular Biology Department, Universita` degli Studi di Siena, Italy (literal)
- Titolo
- A retinal proteomics-based study identifies aA-crystallin as a sex steroid-regulated protein (literal)
- 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 17b-estradiol or androgen dihydrotestosterone.
Using narrow range 2-DE gels and MALDI-TOF-MS analysis, we identified three sex steroidregulated
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
aA-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. (literal)
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