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Fig. 8 | Acta Neuropathologica Communications

Fig. 8

From: Isoaspartic acid is present at specific sites in myelin basic protein from multiple sclerosis patients: could this represent a trigger for disease onset?

Fig. 8

A summary of the sites of modification detected in human MBP. a A histogram of the percentage modification at particular sites for controls () and multiple sclerosis (MS) patients (). The underlined residues in bold correspond to the site of modification in MBP. (+) total Asp racemization in peptide YLATASTMDHAR with and without Met oxidation; (#) total deamidation of Gln147 incorporating all isomers of Asp GVDAEGTLSK. [^] total Asp145 racemization incorporating the Gln and Glu versions of peptide GVDAEGTLSK. Values for Met sulfoxide 21 were not plotted since the levels increased significantly with age. All values are the mean of all ages ± SEM. Asterisks represent level of significance (* p ≤ 0.05, ** ≤ 0.01 and *** ≤ 0.001, Mann–Whitney-U). b A model of MBP23 highlighting the residues that differ significantly in multiple sclerosis. The amino acid residues in blue correspond to the unmodified conformation, those in magenta illustrate the changes in conformation in multiple sclerosis. With the exception of TAHYGSLPQK, all the modifications are clustered within two zones as illustrated; site A) contains six and site B) contains three modified residues. At each of these amino acid residues, the extent of modification was found to be significantly different in multiple sclerosis patients compared with controls. Sites of Asp racemization labeled as D-Asp in 6b, include all Asp isomers (i.e. D-Asp, L-isoAsp and D-isoAsp). In the case of TQDENPVVHFFK only the D-isoAsp version was significantly different

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