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Book: Folding for the synapse

Wyttenbach, Andreas / O'Connor, Vincent

2011

Author's details	Andreas Wyttenbach ; Vincent O'Connor, ed
Language	English
Size	VIII, 318 S. : Ill., graph. Darst.
Publisher	Springer
Publishing place	New York u.a.
Publishing country	United States
Document type	Book
HBZ-ID	HT016590969
ISBN	978-1-4419-7060-2 ; 9781441970619 ; 1-4419-7060-6 ; 1441970614
Database	Catalogue ZB MED Medicine, Health

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Article: Role of heat shock proteins during polyglutamine neurodegeneration: mechanisms and hypothesis.

Wyttenbach, Andreas

Journal of molecular neuroscience : MN

2004 Volume 23, Issue 1-2, Page(s) 69–96

Abstract: A common feature of many neurodegenerative diseases, including Alzheimer's and Parkinsons's disease, the prion disorders, and the CAG repeat polyglutamine (polyQ) diseases, is the occurrence of protein aggregates within or outside of nerve cells. ... ...

Abstract	A common feature of many neurodegenerative diseases, including Alzheimer's and Parkinsons's disease, the prion disorders, and the CAG repeat polyglutamine (polyQ) diseases, is the occurrence of protein aggregates within or outside of nerve cells. Molecular chaperones such as heat shock proteins (HSPs) have been proposed to play a critical role in preventing the accumulation of misfolded proteins that lead to the deposition of aggregates during pathology. This article focuses on the role of HSPs during polyQ pathologies, which include Huntington's disease, spinal and bulbar muscular atrophy, dentatorubral and pallidoluysian atrophy, and several forms of spinocerebellar ataxia. Recently, unifying mechanisms that are involved during polyQ disease have emerged, such as abnormal transcription, impaired degradation systems, and interference of a polyQ expansion with neuronal survival and death-signaling pathways like the activation of caspases and kinases. This article reviews recent studies that point to the involvement of these mechanisms during polyQ pathology and discusses how HSPs can interfere with such processes by paying special attention to HSPs as modulators of survival and death-signaling pathways.
MeSH term(s)	Animals ; Cell Death/genetics ; Heat-Shock Proteins/genetics ; Heat-Shock Proteins/metabolism ; Humans ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism ; Neurodegenerative Diseases/genetics ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/physiopathology ; Peptides/metabolism ; Protein Folding ; Signal Transduction/genetics ; Trinucleotide Repeat Expansion/genetics
Chemical Substances	Heat-Shock Proteins ; Molecular Chaperones ; Peptides ; polyglutamine (26700-71-0)
Language	English
Publishing date	2004
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1043392-2
ISSN	0895-8696
ISSN	0895-8696
DOI	10.1385/JMN:23:1-2:069
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Book: Folding for the synapse

Wyttenbach, Andreas / O'Connor, Vincent

2011

Author's details	Andreas Wyttenbach, Vincent O'Connor, editors
MeSH term(s)	Protein Folding ; Synapses ; Molecular Chaperones
Language	English
Size	viii, 318 p. :, ill.
Publisher	Springer
Publishing place	New York
Document type	Book
ISBN	9781441970602 ; 1441970606 ; 9781441970619 ; 1441970614
Database	Catalogue of the US National Library of Medicine (NLM)

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Book ; Online: Folding for the Synapse

Wyttenbach, Andreas / O'Connor, Vincent

2011

Abstract: Folding for the Synapse" addresses the current view on how protein folding and misfolding, controlled by molecular chaperones, contribute to synapse function and dysfunction. Molecular chaperones have been studied in relation to de novo protein folding, ...

Author's details	edited by Andreas Wyttenbach, Vincent O'Connor
Abstract	"Folding for the Synapse" addresses the current view on how protein folding and misfolding, controlled by molecular chaperones, contribute to synapse function and dysfunction. Molecular chaperones have been studied in relation to de novo protein folding, but there is increasing awareness that chaperone function is required for the regulation of protein dynamics when functioning physiologically as an isolated moiety or part of a protein complex. This book will introduce both important concepts of folding machineries and give examples of the biological relevance of further chaperone fu Folding for the Synapse addresses the current view on how protein folding and misfolding, controlled by molecular chaperones, contribute to synapse function and dysfunction. Molecular chaperones have been studied in relation to de novo protein folding, but there is increasing awareness that chaperone function is required for the regulation of protein dynamics when functioning physiologically as an isolated moiety or part of a protein complex. This book will introduce both important concepts of folding machineries and give examples of the biological relevance of further chaperone functions.
MeSH term(s)	Molecular Chaperones ; Protein Folding ; Synapses
Keywords	Biochemistry ; Cytology ; Medicine ; Neurobiology ; Neurosciences ; Medizin / Gesundheit # Biochemie / Labormedizin ; Technik / Wissen # Biologie ; Technik / Wissen # Sonstiges
Language	English
Size	Online-Ressource, v.: digital
Publisher	Springer Science+Business Media, LLC
Publishing place	Boston, MA
Document type	Book ; Online
Note	Includes bibliographical references and index
ISBN	9781441970602 ; 9781441970619 ; 1441970606 ; 1441970614
DOI	10.1007/978-1-4419-7061-9
Database	Former special subject collection: coastal and deep sea fishing

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Article ; Online: Neurotoxic protein oligomerisation associated with polyglutamine diseases.

Hands, Sarah L / Wyttenbach, Andreas

Acta neuropathologica

2010 Volume 120, Issue 4, Page(s) 419–437

Abstract: Polyglutamine (polyQ) diseases are associated with a CAG/polyQ expansion mutation in unrelated proteins. Upon elongation of the glutamine tract, disease proteins aggregate within cells, mainly in the central nervous system (CNS) and this aggregation ... ...

Abstract	Polyglutamine (polyQ) diseases are associated with a CAG/polyQ expansion mutation in unrelated proteins. Upon elongation of the glutamine tract, disease proteins aggregate within cells, mainly in the central nervous system (CNS) and this aggregation process is associated with neurotoxicity. However, it remains unclear to what extent and how this aggregation causes neuronal dysfunction in the CNS. Aiming at preventing neuronal dysfunction, it will be crucial to determine the links between aggregation and cellular dysfunction, understand the folding pathway of polyQ proteins and discover the relative neurotoxicity of polyQ protein species formed along the aggregation pathway. Here, we review what is known about conformations of polyQ peptides and proteins in their monomeric state from experimental and modelling data, how conformational changes of polyQ proteins relate to their oligomerisation and morphology of aggregates and which cellular function are impaired by oligomers, in vitro and in vivo. We also summarise the key modulatory cellular mechanisms and co-factors, which could affect the folding pathway and kinetics of polyQ aggregation. Although many studies have investigated the relationship between polyQ aggregation and toxicity, these have mainly focussed on investigating changes in the formation of the classical hallmark of polyQ diseases, i.e. microscopically visible inclusion bodies. However, recent studies in which oligomeric species have been considered start to shed light on the identity of neurotoxic oligomeric species. Initial evidence suggests that conformational changes induced by polyQ expansions and their surrounding sequence lead to the formation of particular oligomeric intermediates that may differentially affect neurotoxicity.
MeSH term(s)	Animals ; Central Nervous System Diseases/genetics ; Central Nervous System Diseases/metabolism ; Central Nervous System Diseases/physiopathology ; Humans ; Models, Biological ; Mutation ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Peptides/genetics ; Peptides/metabolism ; Protein Binding/physiology ; Protein Conformation ; Protein Folding
Chemical Substances	Nerve Tissue Proteins ; Peptides ; polyglutamine (26700-71-0)
Language	English
Publishing date	2010-06-01
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1079-0
ISSN	1432-0533 ; 0001-6322
ISSN (online)	1432-0533
ISSN	0001-6322
DOI	10.1007/s00401-010-0703-0
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Article: Differential phosphoprotein labelling (DIPPL) using 32P and 33P.

Tolkovsky, Aviva M / Wyttenbach, Andreas

Methods in molecular biology (Clifton, N.J.)

2009 Volume 527, Page(s) 21–9, xi

Abstract: Differential labelling techniques like differential in-gel electrophoresis (DIGE) enable mixing a control with an experimental sample prior to protein separation, thereby reducing complexity and greatly improving the resolution and analysis of changes in ...

Abstract	Differential labelling techniques like differential in-gel electrophoresis (DIGE) enable mixing a control with an experimental sample prior to protein separation, thereby reducing complexity and greatly improving the resolution and analysis of changes in protein expression. Although the shift caused by phosphorylation to a more acidic pI can, in principle, reveal phosphorylation events using DIGE, analysis and verification of the phosphorylation are fraught with problems. Here we describe a differential phospho-labelling technique that obtains the same advantages as DIGE, which we named DIPPL, for differential phosphoprotein labelling. The technique involves labelling two samples, one with 32Pi (orthophosphate) and the other with 33Pi (orthophosphate). The two samples are mixed and proteins are separated on a single gel. Dried gels are exposed twice: once so that total radiation from 32P and 33P is collected on a film or screen; then acetate sheets are interposed between the gel and the screen such that 33P radiation is filtered out leaving 32P radiation to filter through. We demonstrate the utility of this approach by studying the MEK/ERK-dependent changes in stathmin phosphorylation induced by NGF in primary sympathetic neurons.
MeSH term(s)	Animals ; Electrophoresis, Gel, Two-Dimensional/methods ; Humans ; Isotope Labeling/methods ; Phosphoproteins/analysis ; Phosphoproteins/metabolism ; Phosphorus Radioisotopes/chemistry ; Phosphorus Radioisotopes/pharmacology
Chemical Substances	Phosphoproteins ; Phosphorus Radioisotopes
Language	English
Publishing date	2009
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	1064-3745
ISSN	1064-3745
DOI	10.1007/978-1-60327-834-8_2
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Article: The BH3-only protein Puma is both necessary and sufficient for neuronal apoptosis induced by DNA damage in sympathetic neurons.

Wyttenbach, Andreas / Tolkovsky, Aviva M

Journal of neurochemistry

2006 Volume 96, Issue 5, Page(s) 1213–1226

Abstract: DNA damage activates apoptosis in several neuronal populations and is an important component of neuropathological conditions. While it is well established that neuronal apoptosis, induced by DNA damage, is dependent on the key cell death regulators p53 ... ...

Abstract	DNA damage activates apoptosis in several neuronal populations and is an important component of neuropathological conditions. While it is well established that neuronal apoptosis, induced by DNA damage, is dependent on the key cell death regulators p53 and Bax, it is unknown which proteins link the p53 signal to Bax. Using rat sympathetic neurons as an in vitro model of neuronal apoptosis, we show that cytosine arabinoside is a DNA damaging drug that induces the expression of the BH3-only pro-apoptotic genes Noxa, Puma and Bim. Increased expression occurred after p53 activation, measured by its phosphorylation at serine 15, but prior to the conformational change of Bax at the mitochondria, cytochrome c (cyt c) release and apoptosis. Hence Noxa, Puma and Bim could potentially link p53 to Bax. We directly tested this hypothesis by the use of nullizygous mice. We show that Puma, but not Bim or Noxa, is a crucial mediator of DNA damage-induced neuronal apoptosis. Despite the powerful pro-apoptotic effects of overexpressed Puma in Bax-expressing neurons, Bax nullizygous neurons were resistant to Puma-induced death. Therefore, Puma provides the critical link between p53 and Bax, and is both necessary and sufficient to mediate DNA damage-induced apoptosis of sympathetic neurons.
MeSH term(s)	Animals ; Animals, Newborn ; Apoptosis/drug effects ; Apoptosis/physiology ; Apoptosis Regulatory Proteins/metabolism ; Blotting, Western/methods ; Cell Count/methods ; Cells, Cultured ; Cytarabine/pharmacology ; DNA Damage/physiology ; Drug Interactions ; Enzyme Inhibitors/pharmacology ; Gene Expression/drug effects ; Green Fluorescent Proteins/metabolism ; Immunohistochemistry/methods ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Mitogen-Activated Protein Kinase 3/metabolism ; Nerve Growth Factor/pharmacology ; Neurons/physiology ; Phosphorylation/drug effects ; Protein Transport/drug effects ; Proto-Oncogene Proteins c-mdm2/metabolism ; RNA, Messenger/metabolism ; Rats ; Rats, Wistar ; Reverse Transcriptase Polymerase Chain Reaction/methods ; Serine/metabolism ; Superior Cervical Ganglion/cytology ; Time Factors ; Transfection/methods ; Tumor Suppressor Protein p53/metabolism ; bcl-2-Associated X Protein/deficiency ; bcl-2-Associated X Protein/metabolism ; bcl-Associated Death Protein/metabolism ; bcl-X Protein/metabolism
Chemical Substances	Apoptosis Regulatory Proteins ; Bbc3 protein, rat ; Enzyme Inhibitors ; RNA, Messenger ; Tumor Suppressor Protein p53 ; bcl-2-Associated X Protein ; bcl-Associated Death Protein ; bcl-X Protein ; Cytarabine (04079A1RDZ) ; Green Fluorescent Proteins (147336-22-9) ; Serine (452VLY9402) ; Nerve Growth Factor (9061-61-4) ; Mdm2 protein, rat (EC 2.3.2.27) ; Proto-Oncogene Proteins c-mdm2 (EC 2.3.2.27) ; Mitogen-Activated Protein Kinase 3 (EC 2.7.11.24)
Language	English
Publishing date	2006-01-19
Publishing country	England
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80158-6
ISSN	1471-4159 ; 0022-3042 ; 1474-1644
ISSN (online)	1471-4159
ISSN	0022-3042 ; 1474-1644
DOI	10.1111/j.1471-4159.2005.03676.x
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Article: Differential phosphoprotein labeling (DIPPL), a method for comparing live cell phosphoproteomes using simultaneous analysis of (33)P- and (32)P-labeled proteins.

Wyttenbach, Andreas / Tolkovsky, Aviva M

Molecular & cellular proteomics : MCP

2005 Volume 5, Issue 3, Page(s) 553–559

Abstract: We developed a differential method to reveal kinase-specific phosphorylation events in live cells. In this method, cells in which the specified kinase is inactive are labeled with (32)Pi, whereas cells in which the kinase is active are labeled with (33) ... ...

Abstract	We developed a differential method to reveal kinase-specific phosphorylation events in live cells. In this method, cells in which the specified kinase is inactive are labeled with (32)Pi, whereas cells in which the kinase is active are labeled with (33)Pi. The two cell extracts are then mixed, and proteins are separated on a single two-dimensional gel. The dried gel is exposed twice. The first exposure reveals both (32)P- and (33)P-labeled proteins; the kinase-specific spots are revealed because of (33)P labeling. The second exposure is conducted with two acetate sheets intervening between the gel and the detection plate. This maneuver screens out the less energetic (33)P-labeled proteins while allowing the more energetic (32)P-labeled proteins to be detected, thus leaving only those spots that were phosphorylated independently of the specified kinase. We demonstrate the utility of this method for detecting kinase substrates in rare tissue by focusing on extracellular signal-regulated kinase-specific phosphorylation of stathmin/OP18 in primary rat sympathetic neurons.
MeSH term(s)	Acetates/metabolism ; Animals ; Cell Survival ; Electrophoresis, Gel, Two-Dimensional ; Isotope Labeling ; Phosphoproteins/analysis ; Phosphoproteins/chemistry ; Phosphoproteins/metabolism ; Phosphorus Radioisotopes ; Phosphorylation ; Proteome/analysis ; Proteome/chemistry ; Proteome/metabolism ; Rats ; Rats, Wistar ; Stathmin/metabolism
Chemical Substances	Acetates ; Phosphoproteins ; Phosphorus Radioisotopes ; Proteome ; Stathmin
Language	English
Publishing date	2005-11-21
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2075924-1
ISSN	1535-9484 ; 1535-9476
ISSN (online)	1535-9484
ISSN	1535-9476
DOI	10.1074/mcp.T500028-MCP200
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Article ; Online: mTOR's role in ageing: protein synthesis or autophagy?

Hands, Sarah L / Proud, Christopher G / Wyttenbach, Andreas

Aging

2009 Volume 1, Issue 7, Page(s) 586–597

Abstract: The molecular and cellular mechanisms that regulate ageing are currently under scrutiny because ageing is linked to many human diseases. The nutrient sensing TOR pathway is emerging as a key regulator of ageing. TOR signaling is complex affecting several ...

Abstract	The molecular and cellular mechanisms that regulate ageing are currently under scrutiny because ageing is linked to many human diseases. The nutrient sensing TOR pathway is emerging as a key regulator of ageing. TOR signaling is complex affecting several crucial cellular functions and two such functions, which show clear effects on ageing, are protein synthesis and autophagy. In this article we discuss the relative importance of both these processes in ageing, identify how TOR regulates translation and autophagy and speculate on links between the TOR signaling network and ageing pathways.
MeSH term(s)	Aging/physiology ; Animals ; Autophagy/physiology ; Humans ; Intracellular Signaling Peptides and Proteins/physiology ; Protein Biosynthesis/physiology ; Protein Serine-Threonine Kinases/physiology ; TOR Serine-Threonine Kinases
Chemical Substances	Intracellular Signaling Peptides and Proteins ; MTOR protein, human (EC 2.7.1.1) ; Protein Serine-Threonine Kinases (EC 2.7.11.1) ; TOR Serine-Threonine Kinases (EC 2.7.11.1)
Language	English
Publishing date	2009-07-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	1945-4589
ISSN (online)	1945-4589
DOI	10.18632/aging.100070
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Article ; Online: In vitro and in vivo aggregation of a fragment of huntingtin protein directly causes free radical production.

Hands, Sarah / Sajjad, Mohammad U / Newton, Michael J / Wyttenbach, Andreas

The Journal of biological chemistry

2011 Volume 286, Issue 52, Page(s) 44512–44520

Abstract: Neurodegenerative diseases are characterized by intra- and/or extracellular protein aggregation and oxidative stress. Intense attention has been paid to whether protein aggregation itself contributes to abnormal production of free radicals and ensuing ... ...

Abstract	Neurodegenerative diseases are characterized by intra- and/or extracellular protein aggregation and oxidative stress. Intense attention has been paid to whether protein aggregation itself contributes to abnormal production of free radicals and ensuing cellular oxidative damage. Although this question has been investigated in the context of extracellular protein aggregation, it remains unclear whether protein aggregation inside cells alters the redox homeostasis. To address this, we have used in vitro and in vivo (cellular) models of Huntington disease, one of nine polyglutamine (poly(Q)) disorders, and examined the causal relationship among intracellular protein aggregation, reactive oxygen species (ROS) production, and toxicity. Live imaging of cells expressing a fragment of huntingtin (httExon1) with a poly(Q) expansion shows increased ROS production preceding cell death. ROS production is poly(Q) length-dependent and not due to the httExon 1 flanking sequence. Aggregation inhibition by the MW7 intrabody and Pgl-135 treatment abolishes ROS production, showing that increased ROS is caused by poly(Q) aggregation itself. To examine this hypothesis further, we determined whether aggregation of poly(Q) peptides in vitro generated free radicals. Monitoring poly(Q) protein aggregation using atomic force microscopy and hydrogen peroxide (H(2)O(2)) production over time in parallel we show that oligomerization of httEx1Q53 results in early generation of H(2)O(2). Inhibition of poly(Q) oligomerization by the single chain antibody MW7 abrogates H(2)O(2) formation. These results demonstrate that intracellular protein aggregation directly causes free radical production, and targeting potentially toxic poly(Q) oligomers may constitute a therapeutic target to counteract oxidative stress in poly(Q) diseases.
MeSH term(s)	Cell Death ; Cell Line ; Humans ; Huntingtin Protein ; Huntington Disease/genetics ; Huntington Disease/metabolism ; Hydrogen Peroxide/metabolism ; Microscopy, Atomic Force ; Models, Biological ; Nerve Tissue Proteins/chemistry ; Nerve Tissue Proteins/genetics ; Nerve Tissue Proteins/metabolism ; Nuclear Proteins/chemistry ; Nuclear Proteins/genetics ; Nuclear Proteins/metabolism ; Peptides/chemistry ; Peptides/genetics ; Peptides/metabolism ; Protein Multimerization ; Protein Structure, Quaternary ; Single-Chain Antibodies/chemistry
Chemical Substances	HTT protein, human ; Huntingtin Protein ; Nerve Tissue Proteins ; Nuclear Proteins ; Peptides ; Single-Chain Antibodies ; polyglutamine (26700-71-0) ; Hydrogen Peroxide (BBX060AN9V)
Language	English
Publishing date	2011-10-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M111.307587
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