Abstract

Background: Suppression of nonsense mutations using stop codon readthrough drugs is one of the promising treatments for various genetic disorders, including Duchenne muscular dystrophy. However, recent studies indicate that some functional proteins are produced by canonical stop codon readthrough in physiological conditions of human and other animals. Large myelin protein zero (L-MPZ) is one of these proteins. It contains extra 63 amino acids at C-terminus of myelin protein zero (P0), which is a major myelin protein in the peripheral nervous system. Adhesion activity of L-MPZ is less than that of P0, suggesting that the ratio of these two proteins in myelin is important for normal myelin structure and function.

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