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 D’Anna; 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 D’Anna; Caterina Cascio; Diego Cigna; Giacoma Galizzi; Irene Deidda; Laura Bianchi; Domenica Russo; Rosa Passantino; Luca Bini, Patrizia Guarneri (literal)
Pagina inizio
  • 986 (literal)
Pagina fine
  • 990 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 11 (literal)
Rivista
Note
  • 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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