Hsp60, amateur chaperone in amyloid-beta fibrillogenesis.

Alberto Giuseppe Fucarino, Francesco Cappello, Dario Spigolon, Fabio Bucchieri, Claudia Marino, Silvia Vilasi, Fabio Librizzi, Alberto Fucarino, Dario Spigolon, Claudia Marino, Pier Luigi San Biagio, Silvia Vilasi, Rosa Passantino, Fabio Bucchieri, Maria Rosalia Mangione, Donatella Bulone, Francesco Cappello, Claudio Canale, Carmelinda Canale, Maria Rosalia MangionePier Luigi San Biagio

Risultato della ricerca: Article

15 Citazioni (Scopus)

Abstract

BACKGROUND:Molecular chaperones are a very special class of proteins that play essential roles in many cellular processes like folding, targeting and transport of proteins. Moreover, recent evidence indicates that chaperones can act as potentially strong suppressor agents in Alzheimer's disease (AD). Indeed, in vitro experiments demonstrate that several chaperones are able to significantly slow down or suppress aggregation of Aβ peptide and in vivo studies reveal that treatment with specific chaperones or their overexpression can ameliorate some distinct pathological signs characterizing AD.METHODS:Here we investigate using a biophysical approach (fluorescence, circular dichroism (CD), transmission electron (TEM) and atomic force (AFM) microscopy, size exclusion chromatography (SEC)) the effect of the human chaperonin Hsp60 on Aβ fibrillogenesis.RESULTS:We found that Hsp60 powerfully inhibits Aβ amyloid aggregation, by closing molecular pathways leading to peptide fibrillogenesis.CONCLUSIONS:We observe that Hsp60 inhibits Aβ aggregation through a more complex mechanism than a simple folding chaperone action. The action is specifically directed toward the early oligomeric species behaving as aggregation seeds for on-pathway amyloid fibrillogenesis.GENERAL SIGNIFICANCE:Understanding the specificity of the molecular interactions of Hsp60 with amyloid Aβ peptide allowed us to emphasize the important aspects to be taken into consideration when considering the recent promising therapeutic strategies for neurodegeneration.Copyright © 2016 Elsevier B.V. All rights reserved.
Lingua originaleEnglish
Numero di pagine10
RivistaBIOCHIMICA ET BIOPHYSICA ACTA
Volume1860
Stato di pubblicazionePublished - 2016

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Amyloid
Agglomeration
Peptides
Alzheimer Disease
Chaperonins
Molecular Chaperones
Atomic Force Microscopy
Circular Dichroism
Gel Chromatography
Molecular interactions
Size exclusion chromatography
Seeds
Carrier Proteins
Fluorescence
Electrons
Seed
Atomic force microscopy
Transmission electron microscopy
Proteins
Experiments

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology

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Hsp60, amateur chaperone in amyloid-beta fibrillogenesis. / Fucarino, Alberto Giuseppe; Cappello, Francesco; Spigolon, Dario; Bucchieri, Fabio; Marino, Claudia; Vilasi, Silvia; Librizzi, Fabio; Fucarino, Alberto; Spigolon, Dario; Marino, Claudia; San Biagio, Pier Luigi; Vilasi, Silvia; Passantino, Rosa; Bucchieri, Fabio; Mangione, Maria Rosalia; Bulone, Donatella; Cappello, Francesco; Canale, Claudio; Canale, Carmelinda; Mangione, Maria Rosalia; San Biagio, Pier Luigi.

In: BIOCHIMICA ET BIOPHYSICA ACTA, Vol. 1860, 2016.

Risultato della ricerca: Article

Fucarino, AG, Cappello, F, Spigolon, D, Bucchieri, F, Marino, C, Vilasi, S, Librizzi, F, Fucarino, A, Spigolon, D, Marino, C, San Biagio, PL, Vilasi, S, Passantino, R, Bucchieri, F, Mangione, MR, Bulone, D, Cappello, F, Canale, C, Canale, C, Mangione, MR & San Biagio, PL 2016, 'Hsp60, amateur chaperone in amyloid-beta fibrillogenesis.', BIOCHIMICA ET BIOPHYSICA ACTA, vol. 1860.
Fucarino, Alberto Giuseppe ; Cappello, Francesco ; Spigolon, Dario ; Bucchieri, Fabio ; Marino, Claudia ; Vilasi, Silvia ; Librizzi, Fabio ; Fucarino, Alberto ; Spigolon, Dario ; Marino, Claudia ; San Biagio, Pier Luigi ; Vilasi, Silvia ; Passantino, Rosa ; Bucchieri, Fabio ; Mangione, Maria Rosalia ; Bulone, Donatella ; Cappello, Francesco ; Canale, Claudio ; Canale, Carmelinda ; Mangione, Maria Rosalia ; San Biagio, Pier Luigi. / Hsp60, amateur chaperone in amyloid-beta fibrillogenesis. In: BIOCHIMICA ET BIOPHYSICA ACTA. 2016 ; Vol. 1860.
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title = "Hsp60, amateur chaperone in amyloid-beta fibrillogenesis.",
abstract = "BACKGROUND:Molecular chaperones are a very special class of proteins that play essential roles in many cellular processes like folding, targeting and transport of proteins. Moreover, recent evidence indicates that chaperones can act as potentially strong suppressor agents in Alzheimer's disease (AD). Indeed, in vitro experiments demonstrate that several chaperones are able to significantly slow down or suppress aggregation of Aβ peptide and in vivo studies reveal that treatment with specific chaperones or their overexpression can ameliorate some distinct pathological signs characterizing AD.METHODS:Here we investigate using a biophysical approach (fluorescence, circular dichroism (CD), transmission electron (TEM) and atomic force (AFM) microscopy, size exclusion chromatography (SEC)) the effect of the human chaperonin Hsp60 on Aβ fibrillogenesis.RESULTS:We found that Hsp60 powerfully inhibits Aβ amyloid aggregation, by closing molecular pathways leading to peptide fibrillogenesis.CONCLUSIONS:We observe that Hsp60 inhibits Aβ aggregation through a more complex mechanism than a simple folding chaperone action. The action is specifically directed toward the early oligomeric species behaving as aggregation seeds for on-pathway amyloid fibrillogenesis.GENERAL SIGNIFICANCE:Understanding the specificity of the molecular interactions of Hsp60 with amyloid Aβ peptide allowed us to emphasize the important aspects to be taken into consideration when considering the recent promising therapeutic strategies for neurodegeneration.Copyright {\circledC} 2016 Elsevier B.V. All rights reserved.",
author = "Fucarino, {Alberto Giuseppe} and Francesco Cappello and Dario Spigolon and Fabio Bucchieri and Claudia Marino and Silvia Vilasi and Fabio Librizzi and Alberto Fucarino and Dario Spigolon and Claudia Marino and {San Biagio}, {Pier Luigi} and Silvia Vilasi and Rosa Passantino and Fabio Bucchieri and Mangione, {Maria Rosalia} and Donatella Bulone and Francesco Cappello and Claudio Canale and Carmelinda Canale and Mangione, {Maria Rosalia} and {San Biagio}, {Pier Luigi}",
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T1 - Hsp60, amateur chaperone in amyloid-beta fibrillogenesis.

AU - Fucarino, Alberto Giuseppe

AU - Cappello, Francesco

AU - Spigolon, Dario

AU - Bucchieri, Fabio

AU - Marino, Claudia

AU - Vilasi, Silvia

AU - Librizzi, Fabio

AU - Fucarino, Alberto

AU - Spigolon, Dario

AU - Marino, Claudia

AU - San Biagio, Pier Luigi

AU - Vilasi, Silvia

AU - Passantino, Rosa

AU - Bucchieri, Fabio

AU - Mangione, Maria Rosalia

AU - Bulone, Donatella

AU - Cappello, Francesco

AU - Canale, Claudio

AU - Canale, Carmelinda

AU - Mangione, Maria Rosalia

AU - San Biagio, Pier Luigi

PY - 2016

Y1 - 2016

N2 - BACKGROUND:Molecular chaperones are a very special class of proteins that play essential roles in many cellular processes like folding, targeting and transport of proteins. Moreover, recent evidence indicates that chaperones can act as potentially strong suppressor agents in Alzheimer's disease (AD). Indeed, in vitro experiments demonstrate that several chaperones are able to significantly slow down or suppress aggregation of Aβ peptide and in vivo studies reveal that treatment with specific chaperones or their overexpression can ameliorate some distinct pathological signs characterizing AD.METHODS:Here we investigate using a biophysical approach (fluorescence, circular dichroism (CD), transmission electron (TEM) and atomic force (AFM) microscopy, size exclusion chromatography (SEC)) the effect of the human chaperonin Hsp60 on Aβ fibrillogenesis.RESULTS:We found that Hsp60 powerfully inhibits Aβ amyloid aggregation, by closing molecular pathways leading to peptide fibrillogenesis.CONCLUSIONS:We observe that Hsp60 inhibits Aβ aggregation through a more complex mechanism than a simple folding chaperone action. The action is specifically directed toward the early oligomeric species behaving as aggregation seeds for on-pathway amyloid fibrillogenesis.GENERAL SIGNIFICANCE:Understanding the specificity of the molecular interactions of Hsp60 with amyloid Aβ peptide allowed us to emphasize the important aspects to be taken into consideration when considering the recent promising therapeutic strategies for neurodegeneration.Copyright © 2016 Elsevier B.V. All rights reserved.

AB - BACKGROUND:Molecular chaperones are a very special class of proteins that play essential roles in many cellular processes like folding, targeting and transport of proteins. Moreover, recent evidence indicates that chaperones can act as potentially strong suppressor agents in Alzheimer's disease (AD). Indeed, in vitro experiments demonstrate that several chaperones are able to significantly slow down or suppress aggregation of Aβ peptide and in vivo studies reveal that treatment with specific chaperones or their overexpression can ameliorate some distinct pathological signs characterizing AD.METHODS:Here we investigate using a biophysical approach (fluorescence, circular dichroism (CD), transmission electron (TEM) and atomic force (AFM) microscopy, size exclusion chromatography (SEC)) the effect of the human chaperonin Hsp60 on Aβ fibrillogenesis.RESULTS:We found that Hsp60 powerfully inhibits Aβ amyloid aggregation, by closing molecular pathways leading to peptide fibrillogenesis.CONCLUSIONS:We observe that Hsp60 inhibits Aβ aggregation through a more complex mechanism than a simple folding chaperone action. The action is specifically directed toward the early oligomeric species behaving as aggregation seeds for on-pathway amyloid fibrillogenesis.GENERAL SIGNIFICANCE:Understanding the specificity of the molecular interactions of Hsp60 with amyloid Aβ peptide allowed us to emphasize the important aspects to be taken into consideration when considering the recent promising therapeutic strategies for neurodegeneration.Copyright © 2016 Elsevier B.V. All rights reserved.

UR - http://hdl.handle.net/10447/198112

M3 - Article

VL - 1860

JO - BIOCHIMICA ET BIOPHYSICA ACTA

JF - BIOCHIMICA ET BIOPHYSICA ACTA

SN - 0006-3002

ER -