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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Husted, Cynthia Doudevski, Ivo Israelachvili, Jacob Hu, Yufang Zasadzinski, Joseph A. Wood, Denise Moscarello, Mario Genain, Claude |
| Description | Author Affiliation: Hu Y ( Departments of Chemical Engineering and Biology and Biomolecular Science and Engineering Program, University of California, Santa Barbara, CA 93106, USA.); |
| Abstract | This report describes force measurements and atomic force microscope imaging of lipid-protein interactions that determine the structure of a model membrane system that closely mimics the myelin sheath. Our results suggest that noncovalent, mainly electrostatic and hydrophobic, interactions are responsible for the multilamellar structure and stability of myelin. We find that myelin basic protein acts as a lipid coupler between two apposed bilayers and as a lipid 'hole-filler,' effectively preventing defect holes from developing. From our protein-mediated-adhesion and force-distance measurements, we develop a simple quantitative model that gives a reasonably accurate picture of the molecular mechanism and adhesion of bilayer-bridging proteins by means of noncovalent interactions. The results and model indicate that optimum myelin adhesion and stability depend on the difference between, rather than the product of, the opposite charges on the lipid bilayers and myelin basic protein, as well as on the repulsive forces associated with membrane fluidity, and that small changes in any of these parameters away from the synergistically optimum values can lead to large changes in the adhesion or even its total elimination. Our results also show that the often-asked question of which membrane species, the lipids or the proteins, are the 'important ones' may be misplaced. Both components work synergistically to provide the adhesion and overall structure. A better appreciation of the mechanism of this synergy may allow for a better understanding of stacked and especially myelin membrane structures and may lead to better treatments for demyelinating diseases such as multiple sclerosis. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 37 |
| Volume Number | 101 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2004-09-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Lipid Metabolism Lipids Chemistry Myelin Basic Protein Metabolism Hydrophobic And Hydrophilic Interactions Lipid Bilayers Membrane Fluidity Microscopy, Atomic Force Protein Binding Static Electricity Thermodynamics Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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