Journal
MOLECULAR AND CELLULAR NEUROSCIENCE
Volume 15, Issue 4, Pages 343-354Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1006/mcne.1999.0829
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- NICHD NIH HHS [N01-HD-7-3263] Funding Source: Medline
- NINDS NIH HHS [NS19943] Funding Source: Medline
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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 (PO) and peripheral membrane protein 22 (PMP22), two structural components of compact myelin, remain constant. The levels of PO, 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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