Title: Leukocyte gelatinase B cleavage releases encephalitogens from human myelin basic protein
Authors: Proost, Paul ×
Van Damme, Jozef
Opdenakker, Ghislain #
Issue Date: May-1993
Series Title: Biochemical and Biophysical Research Communications vol:192 issue:3 pages:1175-81
Abstract: Gelatinase B, a marker enzyme for chronic inflammatory diseases such as rheumatoid arthritis and multiple sclerosis (MS), was found to cleave human myelin basic protein (MBP). Human MBP was digested with gelatinase B from leukocytes. The MBP peptide fragments were separated by RP-HPLC and the gelatinase B cleavage sites established by aminoterminal sequence analysis. Several novel P1-P1' cleavage sites for gelatinase B were found. The positions of the cleavage sites in human MBP were such that at least one peptide coincided with a documented major MBP-autoantigen. This study annotates human MBP as a substrate for human gelatinase B, determines novel P1-P'1 cleavage sites and defines one of the metalloproteinases as a possible link in the pathogenesis of demyelinating diseases such as MS.
ISSN: 0006-291X
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Laboratory of Molecular Immunology (Rega Institute)
Academic Center for General Practice
Laboratory of Immunobiology (Rega Institute)
× corresponding author
# (joint) last author

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