Diphtheria toxin inhibits the synthesis of myelin proteolipid and basic proteins by peripheral nerve in vitro.
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Abstract Diphtheria toxin (DT) did not produce measurable degradation of myelin proteins or sulphatide in sciatic nerves of chick embryos after incubation in vitro for 4 h. In contrast, DT inhibited the in vitro incorporation of L[U14C]leucine into myelin proteins by the nerves after a delay of 1 h. Separation of the myelin proteins by SDSpolyacrylamide gel electrophoresis indicated that the synthesis of Wolfgram proteins and proteins not entering the gel was inhibited by 2122 per cent, whereas synthesis of myelin proteolipid and basic proteins was inhibited by 7988 per cent. Incorporation of 35SO4 into myelin [35S]sulphatide was also inhibited by DT after a delay of 2 h. The inhibition of [35S]sulphatide incorporation into myelin caused by DT differed from that observed with puromycin in that it did not depend on depletion of an intracellular transport lipoprotein. Instead, the inhibition seemed to be secondary to the decreased synthesis of myelin proteolipid and basic proteins. Copyright 1973, Wiley Blackwell. All rights reserved
author list (cited authors)
Pleasure, D. E., Feldmann, B., & Prockop, D. J.
complete list of authors
Pleasure, DE||Feldmann, B||Prockop, DJ