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.
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Yanagisawa, K., Sato, S., Miyatake, T. et al. Degradation of myelin proteins by cathepsin B and inhibition by E-64 analogue. Neurochem Res 9, 691–694 (1984). https://doi.org/10.1007/BF00964515
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DOI: https://doi.org/10.1007/BF00964515