| Glycosaminoglycans promote fibril formation by amyloidogenic immunoglobulin light chains through a transient interaction. | |
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MedLine Citation:
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PMID: 21640469 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Amyloid formation occurs when a precursor protein misfolds and aggregates, forming a fibril nucleus that serves as a template for fibril growth. Glycosaminoglycans are highly charged polymers known to associate with tissue amyloid deposits that have been shown to accelerate amyloidogenesis in vitro. We studied two immunoglobulin light chain variable domains from light chain amyloidosis patients with 90% sequence identity, analyzing their fibril formation kinetics and binding properties with different glycosaminoglycan molecules. We find that the less amyloidogenic of the proteins shows a weak dependence on glycosaminoglycan size and charge, while the more amyloidogenic protein responds only minimally to changes in the glycosaminoglycan. These glycosaminoglycan effects on fibril formation do not depend on a stable interaction between the two species but still show characteristic traits of an interaction-dependent mechanism. We propose that transient, predominantly electrostatic interactions between glycosaminoglycans and the precursor proteins mediate the acceleration of fibril formation in vitro. |
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Authors:
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Douglas J Martin; Marina Ramirez-Alvarado |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Date: 2011-05-18 |
Journal Detail:
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Title: Biophysical chemistry Volume: 158 ISSN: 1873-4200 ISO Abbreviation: Biophys. Chem. Publication Date: 2011 Sep |
Date Detail:
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Created Date: 2011-07-11 Completed Date: 2011-11-01 Revised Date: 2012-09-27 |
Medline Journal Info:
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Nlm Unique ID: 0403171 Medline TA: Biophys Chem Country: Netherlands |
Other Details:
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Languages: eng Pagination: 81-9 Citation Subset: IM |
Copyright Information:
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Copyright © 2011 Elsevier B.V. All rights reserved. |
Affiliation:
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Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN 55905, USA. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amyloid
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chemistry* Glycosaminoglycans / chemistry* Hydrogen-Ion Concentration Immunoglobulin Light Chains / chemistry* Kinetics Protein Binding Protein Structure, Tertiary Static Electricity |
| Grant Support | |
ID/Acronym/Agency:
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F30DK082169/DK/NIDDK NIH HHS; GM071514/GM/NIGMS NIH HHS; R01 GM071514-04/GM/NIGMS NIH HHS; R01 GM071514-07/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Amyloid; 0/Glycosaminoglycans; 0/Immunoglobulin Light Chains |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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