Degradation of myelin proteins by cathepsin B and inhibition by E-64 analogue.
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.
D002401:Cathepsin B; D002403:Cathepsins / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006358:Hot Temperature; D006801:Humans; D066298:In Vitro Techniques; D007930:Leucine / Q000031:analogs & derivatives* / Q000494:pharmacology; D009185:Myelin Proteins / Q000378:metabolism*; D011510:Proteolipids / Q000378:metabolism
D009185:Myelin Proteins; D011510:Proteolipids; C028312:Wolfgram proteins; D002403:Cathepsins; D002401:Cathepsin B; D007930:Leucine; C024974:E 64