Titlebook: Cell Biology and Pathology of Myelin; Evolving Biological Bernhard H. J. Juurlink,Richard M. Devon,Valerie M Book 1997 Springer Science+Bu

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Myelin/Oligodendrocyte Glycoproteind by compacted multilamellar membranes. A single oligodendrocyte in the central nervous system (CNS) has the capacity to extend numerous processes, which develop into elaborate specialized membranes that ensheathe multiple larger diameter axonal segments. Historically, CNS myelin had been characteri

Outspoken

Molecular Biology of Hereditary Motor and Sensory NeuropathiesS and in adulthood, the continuous bi-directional dialogue between axon and Schwann cell regulates a temporally and spatially precise pattern of myelin protein expression in the complex myelin structure as a prerequisite for the correct function of the various myelin proteins (reviewed by Snipes and

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Mutations of the Proteolipid Protein Geneelin component has been difficult to define. The primary structure of PLP has been determined by direct protein sequencing and through cDNA cloning: PLP comprises 276 residues and its primary translation product lacks a N-terminal signal peptide (Milner et al., 1985 and references herein). Four high

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Myelin Proteins as Mediators of Signal Transductionral nervous system (CNS), myelin is produced by oligodendrocytes. Because of the difficulty in studying myelin assembly in vivo, the elaboration of the myelin sheath is poorly understood. Current knowledge of the cytoarchitecture of oligodendrocyte membrane sheets has been obtained largely by studyi

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CNP in Myelination particular the elaboration of oligodendrocyte processes that sample the extracellular space and engage axons in order to initiate myelination. This protein is well known for its in vitro enzymatic activity, as yet of no known physiological importance, but which serves as a useful analytical marker

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The Role of the Gap Junction Protein Connexin32 in the Myelin Sheathfound, including deletions, insertions, missense, and nonsense mutations, and at least two mutations in the non-coding region. Different mutations appear to have different effects on the synthesis and localization of Cx32 protein. Both myelinating Schwann cells and oligodendrocytes express Cx32 mRNA

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