Cycloleucine-induced vacuolation of myelin is associated with inhibition of protein methylation.
Chickens injected with cycloleucine developed vacuolation of myelin similar to that seen in humans with vitamin B12 deficiency. Cycloleucine, an inhibitor of the formation of S-adenosylmethionine, decreased the incorporation of methyl groups into methylarginine in myelin basic protein in vivo. The need for methylcobalamin for the conversion of homocysteine to methionine and the requirement that myelin basic protein may be methylated, offer a rational explanation for the myelin lesions observed in cases of vitamin B12 deficiency where there is increasing evidence that methyl-, rather than adenosylcobalamin is required to prevent dysmyelination.
D000596:Amino Acids / Q000494:pharmacology*; D000818:Animals; D001120:Arginine / Q000378:metabolism; D001921:Brain / Q000187:drug effects* / Q000502:physiology; D002645:Chickens; D003515:Cycloleucine / Q000494:pharmacology*; D008745:Methylation; D004676:Myelin Basic Protein / Q000378:metabolism*; D009186:Myelin Sheath / Q000187:drug effects* / Q000648:ultrastructure; D009940:Organoids / Q000187:drug effects*; D011484:Protein-Arginine N-Methyltransferases / Q000037:antagonists & inhibitors; D014617:Vacuoles / Q000187:drug effects*
D000596:Amino Acids; D004676:Myelin Basic Protein; D003515:Cycloleucine; D001120:Arginine; D011484:Protein-Arginine N-Methyltransferases