Document Detail


Docosahexaenoic and eicosapentaenoic acids segregate differently between raft and nonraft domains.
MedLine Citation:
PMID:  22853900     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Omega-3 polyunsaturated fatty acids (n-3 PUFA), enriched in fish oils, are increasingly recognized to have potential benefits for treating many human afflictions. Despite the importance of PUFA, their molecular mechanism of action remains unclear. One emerging hypothesis is that phospholipids containing n-3 PUFA acyl chains modify the structure and composition of membrane rafts, thus affecting cell signaling. In this study the two major n-3 PUFA found in fish oils, eicosapentaenoic (EPA) and docosahexaenoic (DHA) acids, are compared. Using solid-state (2)H NMR spectroscopy we explored the molecular organization of 1-[(2)H(31)]palmitoyl-2-eicosapentaenoylphosphatidylcholine (PEPC-d(31)) and 1-[(2)H(31)]palmitoyl-2-docosahexaenoylphosphatidylcholine (PDPC-d(31)) in mixtures with sphingomyelin (SM) and cholesterol (chol). Our results indicate that whereas both PEPC-d(31) and PDPC-d(31) can accumulate into SM-rich/chol-rich raftlike domains, the tendency for DHA to incorporate into rafts is more than twice as great as for EPA. We propose that DHA may be the more bioactive component of fish oil that serves to disrupt lipid raft domain organization. This mechanism represents an evolution in the view of how PUFA remodel membrane architecture.
Authors:
Justin A Williams; Shawn E Batten; Mitchel Harris; Benjamin Drew Rockett; Saame Raza Shaikh; William Stillwell; Stephen R Wassall
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2012-07-17
Journal Detail:
Title:  Biophysical journal     Volume:  103     ISSN:  1542-0086     ISO Abbreviation:  Biophys. J.     Publication Date:  2012 Jul 
Date Detail:
Created Date:  2012-08-02     Completed Date:  2012-12-10     Revised Date:  2013-07-21    
Medline Journal Info:
Nlm Unique ID:  0370626     Medline TA:  Biophys J     Country:  United States    
Other Details:
Languages:  eng     Pagination:  228-37     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Biophysical Society. Published by Elsevier Inc. All rights reserved.
Affiliation:
Department of Physics, Indiana University-Purdue University Indianapolis, Indianapolis, Indiana, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Cholesterol / chemistry
Detergents
Docosahexaenoic Acids / chemistry*
Eicosapentaenoic Acid / chemistry*
Magnetic Resonance Spectroscopy
Membrane Microdomains / chemistry*
Membranes, Artificial
Oleic Acids / chemistry
Phosphatidylcholines / chemistry
Sphingomyelins / chemistry
Temperature
Grant Support
ID/Acronym/Agency:
R15AT006122/AT/NCCAM NIH HHS
Chemical
Reg. No./Substance:
0/1-palmitoyl-2-elaidoylphosphatidylcholine; 0/Detergents; 0/Membranes, Artificial; 0/Oleic Acids; 0/Phosphatidylcholines; 0/Sphingomyelins; 1553-41-9/Eicosapentaenoic Acid; 25167-62-8/Docosahexaenoic Acids; 57-88-5/Cholesterol; 59403-54-2/1-palmitoyl-2-docosahexaenoyl-sn-glycero-3-phosphocholine; TE895536Y5/1-palmitoyl-2-oleoylphosphatidylcholine
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Drying transition in the hydrophobic gate of the GLIC channel blocks ion conduction.
Next Document:  Mechanism for calcium ion sensing by the C2A domain of synaptotagmin I.