Trehalose effects on a-crystallin aggregates

Bruno Giuseppe Pignataro, Claudia Cascio, Claudia Cascio, Francesco Attanasio, Anna Savarino, Salvatore Fisichella, Enrico Rizzarelli, Vincenzo Giuseppe Nicoletti, Caterina Cascio, Valentina Nicoletti

Risultato della ricerca: Articlepeer review

17 Citazioni (Scopus)

Abstract

α-Crystallin in its native state is a large, heterogeneous, low-molecular weight (LMW) aggregate that under certain conditions may progressively became part of insoluble high-molecular weight (HMW) systems. These systems are supposed to play a relevant role in eye lens opacification and vision impairment. In this paper, we report the effects of trehalose on α-crystallin aggregates. The role of trehalose in α-crystallin stress tolerance, chaperone activity and thermal stability is studied. The results show that trehalose stabilizes the α-crystallin native structure, inhibits α-crystallin aggregation, and disaggregates preformed LMW systems not affecting its chaperone activity
Lingua originaleEnglish
pagine (da-a)899-905
Numero di pagine7
RivistaBiochemical and Biophysical Research Communications
Volume354
Stato di pubblicazionePublished - 2007

All Science Journal Classification (ASJC) codes

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  • ???subjectarea.asjc.1300.1303???
  • ???subjectarea.asjc.1300.1312???
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