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Rapid Release and Unusual Stability of Immunodominant Peptide 45−89 from Citrullinated Myelin Basic Protein

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    Rapid Release and Unusual Stability of Immunodominant Peptide 45−89 from Citrullinated Myelin Basic Protein†
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    Department of Neurology and Center for Neuroimmunology, University of Alabama at Birmingham, Birmingham, Alabama 35233-7340, Neurology and Research Services, Birmingham Veterans Medical Center, Birmingham, Alabama 35233, and Department of Structural Biology and Biochemistry, The Hospital for Sick Children, Toronto, Ontario, Canada
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    Biochemistry

    Cite this: Biochemistry 1999, 38, 19, 6157–6163
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    https://doi.org/10.1021/bi982960s
    Published April 22, 1999
    Copyright © 1999 American Chemical Society
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    Abstract

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    Myelin basic protein (MBP) exists in a population of isoforms and isomers. The 18.5 kDa MBP-C1, the main human adult isoform, has 170 residues and is relatively unmodified, whereas the same isoform can be citrullinated on six arginine residues to create the MBP-C8 (MBP Cit6) isomer. MBP Cit6 dominates in MS brain, accounting for 45% rather than 25% of the population of MBP isomers. In the fulminant form of MS, known as Marburg's Disease, 18 of the 19 arginines in MBP are citrullinated (MBP Cit18). Citrullination of MBP could lead to instability of myelin or limited remyelination. In this investigation, the susceptibilities to degradation by cathepsin D of MBP Cit6 and MBP-C1, both from normal and MS brain tissue, and Marburg MBP Cit18 were compared. The pattern of digestion was similar, and no differences of corresponding isomers in normal and MS brain were noted. However, normal MBP Cit6 was degraded 10-fold more rapidly than MBP-C1, and MBP Cit18 was degraded even more rapidly. MBP peptide 45−89 was preserved regardless of isomer type or source. Its generation was directly related to the citrulline content of the MBP substrate being 4 times faster in normal MBP Cit6 and 35 times faster in Marburg MBP Cit18 than in normal MBP-C1. Peptide 45−89 from a citrullinated MBP exhibited more deamidation, and, regardless of source, showed an α-helix structure in a lipid mimetic environment. We postulate that the generation of MBP peptides, including those that are dominant and encephalitogenic, is directly related to deimination of arginine to citrulline in MBP.

    Copyright © 1999 American Chemical Society

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    †

     This work was supported by a Merit Review Grant and by the Multiple Sclerosis Society of Canada (G.H., M.A.M.).

    ‡

     Department of Neurology, University of Alabama at Birmingham.

    §

     Birmingham Veterans Medical Center.

    ‖

     The Hospital for Sick Children.

    *

     To whom correspondence should be addressed:  Department of Neurology, University of Alabama at Birmingham, Birmingham, AL 35233-7340. Telephone:  (205) 934-2402. Fax:  (205) 975-6030.

    ⊥

     Center for Neuroimmunology, University of Alabama at Birmingham.

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    This article is cited by 70 publications.

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    Biochemistry

    Cite this: Biochemistry 1999, 38, 19, 6157–6163
    Click to copy citationCitation copied!
    https://doi.org/10.1021/bi982960s
    Published April 22, 1999
    Copyright © 1999 American Chemical Society
    Request reuse permissions

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