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Literature DB >> 30450365

Filter Retardation Assay for Detecting and Quantifying Polyglutamine Aggregates Using Caenorhabditis elegans Lysates.

Olga Sin^1,2, Alejandro Mata-Cabana³, Renée I Seinstra⁴, Ellen A A Nollen⁴.

Abstract

Protein aggregation is a hallmark of several neurodegenerative diseases and is associated with impaired protein homeostasis. This imbalance is caused by the loss of the protein's native conformation, which ultimately results in its aggregation or abnormal localization within the cell. Using a C. elegans model of polyglutamine diseases, we describe in detail the filter retardation assay, a method that captures protein aggregates in a cellulose acetate membrane and allows its detection and quantification by immunoblotting.

Entities: Chemical

Keywords: Amyloid; C. elegans; Dot blot; Filter retardation assay; Filter trap assay; Polyglutamine; Protein aggregation

Year: 2018 PMID： 30450365 PMCID： PMC6235101 DOI： 10.21769/BioProtoc.3042

Source DB: PubMed Journal: Bio Protoc ISSN： 2331-8325

8 in total

1. Membrane filter assay for detection of amyloid-like polyglutamine-containing protein aggregates.

Authors: E E Wanker; E Scherzinger; V Heiser; A Sittler; H Eickhoff; H Lehrach
Journal: Methods Enzymol Date: 1999 Impact factor: 1.600

Review 2. Unfolding the role of protein misfolding in neurodegenerative diseases.

Authors: Claudio Soto
Journal: Nat Rev Neurosci Date: 2003-01 Impact factor: 34.870

3. Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo.

Authors: E Scherzinger; R Lurz; M Turmaine; L Mangiarini; B Hollenbach; R Hasenbank; G P Bates; S W Davies; H Lehrach; E E Wanker
Journal: Cell Date: 1997-08-08 Impact factor: 41.582

4. A kinetic assessment of the C. elegans amyloid disaggregation activity enables uncoupling of disassembly and proteolysis.

Authors: Jan Bieschke; Ehud Cohen; Amber Murray; Andrew Dillin; Jeffery W Kelly
Journal: Protein Sci Date: 2009-11 Impact factor: 6.725

Review 5. Cellular Regulation of Amyloid Formation in Aging and Disease.

Authors: Esther Stroo; Mandy Koopman; Ellen A A Nollen; Alejandro Mata-Cabana
Journal: Front Neurosci Date: 2017-02-14 Impact factor: 4.677

6. Identification of an RNA Polymerase III Regulator Linked to Disease-Associated Protein Aggregation.

Authors: Olga Sin; Tristan de Jong; Alejandro Mata-Cabana; Michelle Kudron; Mohamad Amr Zaini; Francesco A Aprile; Renée I Seinstra; Esther Stroo; Roméo Willinge Prins; Céline N Martineau; Hai Hui Wang; Wytse Hogewerf; Anne Steinhof; Erich E Wanker; Michele Vendruscolo; Cornelis F Calkhoven; Valerie Reinke; Victor Guryev; Ellen A A Nollen
Journal: Mol Cell Date: 2017-03-16 Impact factor: 17.970

Review 7. Chaperones in Polyglutamine Aggregation: Beyond the Q-Stretch.

Authors: E F E Kuiper; Eduardo P de Mattos; Laura B Jardim; Harm H Kampinga; Steven Bergink
Journal: Front Neurosci Date: 2017-03-23 Impact factor: 4.677

8. Lack of pathogenic potential of peripheral α-synuclein aggregates from Parkinson's disease patients.

Authors: Ariadna Recasens; Iria Carballo-Carbajal; Annabelle Parent; Jordi Bové; Ellen Gelpi; Eduardo Tolosa; Miquel Vila
Journal: Acta Neuropathol Commun Date: 2018-02-08 Impact factor: 7.801

8 in total

4 in total

Filter Retardation Assay for Detecting and Quantifying Polyglutamine Aggregates Using Caenorhabditis elegans Lysates.

1. Membrane filter assay for detection of amyloid-like polyglutamine-containing protein aggregates.

Review 2. Unfolding the role of protein misfolding in neurodegenerative diseases.

3. Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivo.

4. A kinetic assessment of the C. elegans amyloid disaggregation activity enables uncoupling of disassembly and proteolysis.

Review 5. Cellular Regulation of Amyloid Formation in Aging and Disease.

6. Identification of an RNA Polymerase III Regulator Linked to Disease-Associated Protein Aggregation.

Review 7. Chaperones in Polyglutamine Aggregation: Beyond the Q-Stretch.

8. Lack of pathogenic potential of peripheral α-synuclein aggregates from Parkinson's disease patients.

1. Huntingtin Polyglutamine Fragments Are a Substrate for Hsp104 in Saccharomyces cerevisiae.

2. The Proteasome Activators Blm10/PA200 Enhance the Proteasomal Degradation of N-Terminal Huntingtin.

3. Filter trapping protocol to detect aggregated proteins in human cell lines.

4. Exploiting flow cytometry for the unbiased quantification of protein inclusions in Caenorhabditis elegans.