Identification of a mitogen-activated protein kinase site in human myelin basic protein in situ

被引:15
作者
Yon, M
Ackerley, CA
Mastronardi, FG
Groome, N
Moscarello, MA
机构
[1] HOSP SICK CHILDREN,DEPT BIOCHEM,TORONTO,ON M5G 1X8,CANADA
[2] OXFORD BROOKES UNIV,SCH BIOL & MOLEC SCI,OXFORD OX3 0BP,ENGLAND
[3] HOSP SICK CHILDREN,DEPT PATHOL,TORONTO,ON M5G 1X8,CANADA
关键词
mitogen-activated protein kinase; phosphorylation; myelin basic protein; multiple sclerosis;
D O I
10.1016/0165-5728(95)00183-2
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Ultrastructural localization of a specific phosphorylated isomer of myelin basic protein (MBP) has been achieved with a monoclonal antibody specific for human MBP sequence, 89-105, in which Thr(98) was phosphorylated. Cryosections of human brain white matter revealed that gold particles were found localized almost exclusively to the major dense line demonstrating that threonine 98 in the sequence Thr-Pro-Arg-Thr-Pro-Pro-Pro, a mitogen-activated protein kinase-specific site, was phosphorylated in vivo. In two cases of multiple sclerosis, the density of gold particles in myelin was reduced by about 30%, in one case by 42%, and by 80% in a fourth case. However, gold labelling was seen in areas of demyelination suggesting that the phosphorylated threonyl peptide was protected from degradation.
引用
收藏
页码:55 / 59
页数:5
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