Abstract
Myelin basic protein (MBP) plays an essential adhesive role in the formation of compact myelin in the central nervous system (CNS), but not in the peripheral nervous system (PNS). Morphologic data suggest that MBP controls the number of cytoplasmic channels or Schmidt–Lanterman incisures (SLI) present in PNS myelin. The levels of connexin-32 (Cx32) and myelin-associated glycoprotein (MAG), two components of the incisures, are inversely proportional to the levels of MBP in sciatic nerves of mice affected by the shiverer (shi) mutation, while protein zero (P0) and peripheral membrane protein 22 (PMP22), two structural components of compact myelin, remain constant. The levels of P0, PMP22, Cx32, and MAG mRNA do not vary in relationship to the levels of MBP. This indicates that MBP exerts its effect on Cx32 and MAG at a posttranscriptional level and suggests a new function for MBP in regulating gene expression in the PNS.
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