Marburg's Variant of Multiple Sclerosis Correlates with a Less Compact Structure of Myelin Basic Protein |
| |
| Institution: | 1. Nuffield Department of Orthopaedics, Rheumatology and Musculoskeletal Sciences, University of Oxford, Oxford, United Kingdom;2. Department of Plastic Surgery, Stoke Mandeville Hospital, Buckinghamshire Healthcare NHS Trust, Aylesbury, United Kingdom;3. The Spires Cleft Centre, John Radcliffe Hospital, Oxford University Hospitals, Oxford, United Kingdom;4. Department of Pediatrics, McMaster University, Hamilton, Ontario, Canada;5. Division of Plastic and Reconstructive Surgery, Department of Surgery, Hospital for Sick Children, University of Toronto, Toronto, Ontario, Canada;6. MD Anderson Center for INSPiRED Cancer Care, the University of Texas, Houston, Texas, United States |
| |
| Abstract: | Multiple sclerosis (MS) is an autoimmune disease in which the myelin sheath of the central nervous system is degraded, and the 18.5 kDa isoform of myelin basic protein (MBP) is reduced in cationicity. In a unique case of acute, fulminating MS (Marburg's variant), MBP is considerably less cationic than MBP from both normal, and chronic MS-afflicted individuals. This electron microscopical study has identified that,in vitro,the less cationic Marburg MBP isomer forms a more extended protein-lipid complex than MBP from healthy or chronic MS-afflicted individuals. This correlation implies that chemical modifications to MBPin vivocontribute directly to the structural instability of myelin, and subsequent autoantigenic presentation of this protein, observedin vivoin MS. |
| |
| Keywords: | |
| 本文献已被 ScienceDirect 等数据库收录！ |
|
