Document Detail


Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation.
MedLine Citation:
PMID:  22970795     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The toxicity of amyloid-forming peptides has been hypothesized to reside in the ability of protein oligomers to interact with and disrupt the cell membrane. Much of the evidence for this hypothesis comes from in vitro experiments using model membranes. However, the accuracy of this approach depends on the ability of the model membrane to accurately mimic the cell membrane. The effect of membrane composition has been overlooked in many studies of amyloid toxicity in model systems. By combining measurements of membrane binding, membrane permeabilization, and fiber formation, we show that lipids with the phosphatidylethanolamine (PE) headgroup strongly modulate the membrane disruption induced by IAPP (islet amyloid polypeptide protein), an amyloidogenic protein involved in type II diabetes. Our results suggest that PE lipids hamper the interaction of prefibrillar IAPP with membranes but enhance the membrane disruption correlated with the growth of fibers on the membrane surface via a detergent-like mechanism. These findings provide insights into the mechanism of membrane disruption induced by IAPP, suggesting a possible role of PE and other amyloids involved in other pathologies.
Authors:
Michele F M Sciacca; Jeffrey R Brender; Dong-Kuk Lee; Ayyalusamy Ramamoorthy
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2012-09-21
Journal Detail:
Title:  Biochemistry     Volume:  51     ISSN:  1520-4995     ISO Abbreviation:  Biochemistry     Publication Date:  2012 Oct 
Date Detail:
Created Date:  2012-10-02     Completed Date:  2012-12-10     Revised Date:  2013-10-17    
Medline Journal Info:
Nlm Unique ID:  0370623     Medline TA:  Biochemistry     Country:  United States    
Other Details:
Languages:  eng     Pagination:  7676-84     Citation Subset:  IM    
Affiliation:
Departments of Biophysics and Chemistry, University of Michigan, Ann Arbor, Michigan 48109-1055, United States.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Cell Membrane / chemistry,  metabolism*,  pathology
Circular Dichroism
Humans
Islet Amyloid Polypeptide / chemistry,  metabolism*
Liposomes / chemistry,  metabolism*
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular
Permeability
Phosphatidylcholines / chemistry,  metabolism
Phosphatidylethanolamines / chemistry,  metabolism*
Grant Support
ID/Acronym/Agency:
GM095640/GM/NIGMS NIH HHS; R01 GM095640/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Islet Amyloid Polypeptide; 0/Liposomes; 0/Phosphatidylcholines; 0/Phosphatidylethanolamines; 39382-08-6/phosphatidylethanolamine
Comments/Corrections

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