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

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

Fisica e Chimica - Emilio Segrè

Risultato della ricerca: Article › peer 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 originale	English
pagine (da-a)	899-905
Numero di pagine	7
Rivista	Biochemical and Biophysical Research Communications
Volume	354
Stato di pubblicazione	Published - 2007

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Trehalose effects on a-crystallin aggregates. / Pignataro, Bruno Giuseppe; Cascio, Claudia; Cascio, Claudia; Attanasio, Francesco; Savarino, Anna; Fisichella, Salvatore; Rizzarelli, Enrico; Nicoletti, Vincenzo Giuseppe; Cascio, Caterina; Nicoletti, Valentina.

In: Biochemical and Biophysical Research Communications, Vol. 354, 2007, pag. 899-905.

Risultato della ricerca: Article › peer review

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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",

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AU - Pignataro, Bruno Giuseppe

AU - Cascio, Claudia

AU - Attanasio, Francesco

AU - Savarino, Anna

AU - Fisichella, Salvatore

AU - Rizzarelli, Enrico

AU - Nicoletti, Vincenzo Giuseppe

AU - Cascio, Caterina

AU - Nicoletti, Valentina

PY - 2007

Y1 - 2007

N2 - 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

AB - 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

UR - http://hdl.handle.net/10447/31710

M3 - Article

VL - 354

SP - 899

EP - 905

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

ER -

Trehalose effects on a-crystallin aggregates

Abstract

All Science Journal Classification (ASJC) codes

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