Degradation of myelin proteins by cathepsin B and inhibition by E-64 analogue.

Abstract

Purified human brain myelin was isolated, heat-treated to inactivate the endogenous proteolytic activity and incubated with cathepsin B purified from rat liver, at pH 6.0. Incubation resulted in a marked reduction of myelin basic protein (BP) and partial breakdown of proteolipid protein or Wolfgram protein. Degradation of myelin proteins was inhibited by E-64 analogue (E-64-a). E-64 is a specific thiol protease inhibitor isolated from a solid culture of Aspergillus japonicus. The present study suggests that cathepsin B may play some role in demyelination.