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Leukocyte gelatinase B cleavage releases encephalitogens from human myelin basic protein

P Proost1, J Van Damme, G Opdenakker

  • 1Rega Institute for Medical Research, University of Leuven, Belgium.

Biochemical and Biophysical Research Communications
|May 14, 1993
PubMed

Insights

Gelatinase B, an enzyme linked to inflammatory diseases, cleaves human myelin basic protein (MBP). This cleavage generates fragments that may contribute to the development of demyelinating diseases like multiple sclerosis (MS).

Area of Science:

  • Biochemistry
  • Immunology
  • Neuroscience

Background:

  • Gelatinase B is a key enzyme in chronic inflammatory diseases, including rheumatoid arthritis and multiple sclerosis (MS).
  • Myelin basic protein (MBP) is a critical component of the myelin sheath and a known autoantigen in demyelinating diseases.

Purpose of the Study:

  • To investigate whether gelatinase B can cleave human myelin basic protein (MBP).
  • To identify the specific cleavage sites of gelatinase B on human MBP.
  • To explore the potential role of this interaction in the pathogenesis of demyelinating diseases.

Main Methods:

  • Digestion of human MBP using gelatinase B isolated from leukocytes.
  • Separation of MBP peptide fragments using reversed-phase high-performance liquid chromatography (RP-HPLC).
  • Determination of gelatinase B cleavage sites through aminoterminal sequence analysis.

Main Results:

  • Gelatinase B was confirmed to cleave human MBP.
  • Several novel P1-P1' cleavage sites for gelatinase B on human MBP were identified.
  • At least one resulting peptide fragment corresponded to a known major MBP-autoantigen.

Conclusions:

  • Human MBP is a substrate for human gelatinase B.
  • Novel cleavage sites for gelatinase B on MBP were defined.
  • Gelatinase B represents a potential link in the pathogenesis of demyelinating diseases, such as MS.

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