Applying chaperones to protein-misfolding disorders: Molecular chaperones against α-synuclein in Parkinson's disease

•Refolding protein is the key for neurodegenerative disorder.•Protein chaperones can be a target for therapeutic intervention in Parkinson's disease.•The various molecular chaperones have a complementary effect in PD. Parkinson's disease (PD) is a neurodegenerative disorder characterized b...

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Published inInternational journal of biological macromolecules Vol. 60; pp. 196 - 205
Main Authors Chaari, Ali, Hoarau-Véchot, Jessica, Ladjimi, Moncef
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.09.2013
Subjects
Aggregation
alpha-Synuclein - chemistry
alpha-Synuclein - metabolism
amyloid
animal disease models
Animals
Biomarkers
dopamine
heat shock proteins
Heat-Shock Proteins - chemistry
Heat-Shock Proteins - metabolism
Humans
idiopathic diseases
Lewy bodies
Lewy Bodies - metabolism
Molecular chaperones
Molecular Chaperones - chemistry
Molecular Chaperones - metabolism
Parkinson disease
Parkinson Disease - metabolism
Parkinson Disease - pathology
Parkinson's disease
protein aggregates
Protein Folding
Proteostasis Deficiencies - metabolism
Refolding
α-synuclein
Aggregation
Parkinson's disease
PD
Hsp
Molecular chaperones
α-syn
LB
Refolding
sHsp
α-synuclein
heat shock protein
small heat shock protein
Lewy body
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Abstract •Refolding protein is the key for neurodegenerative disorder.•Protein chaperones can be a target for therapeutic intervention in Parkinson's disease.•The various molecular chaperones have a complementary effect in PD. Parkinson's disease (PD) is a neurodegenerative disorder characterized by the accumulation of a protein called α-synuclein (α-syn) into inclusions known as lewy bodies (LB) within neurons. This accumulation is also due to insufficient formation and activity of dopamine produced in certain neurons within the substantia nigra. Lewy bodies are the pathological hallmark of the idiopathic disorder and the cascade that allows α-synuclein to misfold, aggregate and form these inclusions has been the subject of intensive research. Targeting these early steps of oligomerization is one of the main therapeutic approaches in order to develop neurodegenerative-modifying agents. Because the folding and refolding of alpha synuclein is the key point of this cascade, we are interested in this review to summarize the role of some molecular chaperones proteins such as Hsp70, Hsp90 and small heat shock proteins (sHsp) and Hsp 104. Hsp70 and its co-chaperone, Hsp70 and small heat shock proteins can prevent neurodegeneration by preventing α-syn misfolding, oligomerization and aggregation in vitro and in Parkinson disease animal models. Hsp104 is able to resolve disordered protein aggregates and cross beta amyloid conformers. Together, these chaperones have a complementary effect and can be a target for therapeutic intervention in PD.
AbstractList Parkinson's disease (PD) is a neurodegenerative disorder characterized by the accumulation of a protein called α-synuclein (α-syn) into inclusions known as lewy bodies (LB) within neurons. This accumulation is also due to insufficient formation and activity of dopamine produced in certain neurons within the substantia nigra. Lewy bodies are the pathological hallmark of the idiopathic disorder and the cascade that allows α-synuclein to misfold, aggregate and form these inclusions has been the subject of intensive research. Targeting these early steps of oligomerization is one of the main therapeutic approaches in order to develop neurodegenerative-modifying agents. Because the folding and refolding of alpha synuclein is the key point of this cascade, we are interested in this review to summarize the role of some molecular chaperones proteins such as Hsp70, Hsp90 and small heat shock proteins (sHsp) and Hsp 104. Hsp70 and its co-chaperone, Hsp70 and small heat shock proteins can prevent neurodegeneration by preventing α-syn misfolding, oligomerization and aggregation in vitro and in Parkinson disease animal models. Hsp104 is able to resolve disordered protein aggregates and cross beta amyloid conformers. Together, these chaperones have a complementary effect and can be a target for therapeutic intervention in PD.Parkinson's disease (PD) is a neurodegenerative disorder characterized by the accumulation of a protein called α-synuclein (α-syn) into inclusions known as lewy bodies (LB) within neurons. This accumulation is also due to insufficient formation and activity of dopamine produced in certain neurons within the substantia nigra. Lewy bodies are the pathological hallmark of the idiopathic disorder and the cascade that allows α-synuclein to misfold, aggregate and form these inclusions has been the subject of intensive research. Targeting these early steps of oligomerization is one of the main therapeutic approaches in order to develop neurodegenerative-modifying agents. Because the folding and refolding of alpha synuclein is the key point of this cascade, we are interested in this review to summarize the role of some molecular chaperones proteins such as Hsp70, Hsp90 and small heat shock proteins (sHsp) and Hsp 104. Hsp70 and its co-chaperone, Hsp70 and small heat shock proteins can prevent neurodegeneration by preventing α-syn misfolding, oligomerization and aggregation in vitro and in Parkinson disease animal models. Hsp104 is able to resolve disordered protein aggregates and cross beta amyloid conformers. Together, these chaperones have a complementary effect and can be a target for therapeutic intervention in PD.
•Refolding protein is the key for neurodegenerative disorder.•Protein chaperones can be a target for therapeutic intervention in Parkinson's disease.•The various molecular chaperones have a complementary effect in PD. Parkinson's disease (PD) is a neurodegenerative disorder characterized by the accumulation of a protein called α-synuclein (α-syn) into inclusions known as lewy bodies (LB) within neurons. This accumulation is also due to insufficient formation and activity of dopamine produced in certain neurons within the substantia nigra. Lewy bodies are the pathological hallmark of the idiopathic disorder and the cascade that allows α-synuclein to misfold, aggregate and form these inclusions has been the subject of intensive research. Targeting these early steps of oligomerization is one of the main therapeutic approaches in order to develop neurodegenerative-modifying agents. Because the folding and refolding of alpha synuclein is the key point of this cascade, we are interested in this review to summarize the role of some molecular chaperones proteins such as Hsp70, Hsp90 and small heat shock proteins (sHsp) and Hsp 104. Hsp70 and its co-chaperone, Hsp70 and small heat shock proteins can prevent neurodegeneration by preventing α-syn misfolding, oligomerization and aggregation in vitro and in Parkinson disease animal models. Hsp104 is able to resolve disordered protein aggregates and cross beta amyloid conformers. Together, these chaperones have a complementary effect and can be a target for therapeutic intervention in PD.
Parkinson's disease (PD) is a neurodegenerative disorder characterized by the accumulation of a protein called α-synuclein (α-syn) into inclusions known as lewy bodies (LB) within neurons. This accumulation is also due to insufficient formation and activity of dopamine produced in certain neurons within the substantia nigra. Lewy bodies are the pathological hallmark of the idiopathic disorder and the cascade that allows α-synuclein to misfold, aggregate and form these inclusions has been the subject of intensive research. Targeting these early steps of oligomerization is one of the main therapeutic approaches in order to develop neurodegenerative-modifying agents. Because the folding and refolding of alpha synuclein is the key point of this cascade, we are interested in this review to summarize the role of some molecular chaperones proteins such as Hsp70, Hsp90 and small heat shock proteins (sHsp) and Hsp 104. Hsp70 and its co-chaperone, Hsp70 and small heat shock proteins can prevent neurodegeneration by preventing α-syn misfolding, oligomerization and aggregation in vitro and in Parkinson disease animal models. Hsp104 is able to resolve disordered protein aggregates and cross beta amyloid conformers. Together, these chaperones have a complementary effect and can be a target for therapeutic intervention in PD.
Parkinson's disease (PD) is a neurodegenerative disorder characterized by the accumulation of a protein called alpha -synuclein ( alpha -syn) into inclusions known as lewy bodies (LB) within neurons. This accumulation is also due to insufficient formation and activity of dopamine produced in certain neurons within the substantia nigra. Lewy bodies are the pathological hallmark of the idiopathic disorder and the cascade that allows alpha -synuclein to misfold, aggregate and form these inclusions has been the subject of intensive research. Targeting these early steps of oligomerization is one of the main therapeutic approaches in order to develop neurodegenerative-modifying agents. Because the folding and refolding of alpha synuclein is the key point of this cascade, we are interested in this review to summarize the role of some molecular chaperones proteins such as Hsp70, Hsp90 and small heat shock proteins (sHsp) and Hsp 104. Hsp70 and its co-chaperone, Hsp70 and small heat shock proteins can prevent neurodegeneration by preventing alpha -syn misfolding, oligomerization and aggregation in vitro and in Parkinson disease animal models. Hsp104 is able to resolve disordered protein aggregates and cross beta amyloid conformers. Together, these chaperones have a complementary effect and can be a target for therapeutic intervention in PD.
Author Chaari, Ali
Hoarau-Véchot, Jessica
Ladjimi, Moncef
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Keywords Aggregation
Parkinson's disease
PD
Hsp
Molecular chaperones
α-syn
LB
Refolding
sHsp
α-synuclein
heat shock protein
small heat shock protein
Lewy body
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Snippet •Refolding protein is the key for neurodegenerative disorder.•Protein chaperones can be a target for therapeutic intervention in Parkinson's disease.•The...
Parkinson's disease (PD) is a neurodegenerative disorder characterized by the accumulation of a protein called α-synuclein (α-syn) into inclusions known as...
Parkinson's disease (PD) is a neurodegenerative disorder characterized by the accumulation of a protein called alpha -synuclein ( alpha -syn) into inclusions...
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SubjectTerms Aggregation
alpha-Synuclein - chemistry
alpha-Synuclein - metabolism
amyloid
animal disease models
Animals
Biomarkers
dopamine
heat shock proteins
Heat-Shock Proteins - chemistry
Heat-Shock Proteins - metabolism
Humans
idiopathic diseases
Lewy bodies
Lewy Bodies - metabolism
Molecular chaperones
Molecular Chaperones - chemistry
Molecular Chaperones - metabolism
Parkinson disease
Parkinson Disease - metabolism
Parkinson Disease - pathology
Parkinson's disease
protein aggregates
Protein Folding
Proteostasis Deficiencies - metabolism
Refolding
α-synuclein
Title Applying chaperones to protein-misfolding disorders: Molecular chaperones against α-synuclein in Parkinson's disease
URI https://dx.doi.org/10.1016/j.ijbiomac.2013.05.032
https://www.ncbi.nlm.nih.gov/pubmed/23748003
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