Abstract
It has been demonstrated that abnormal levels of PMP22 expression due to altered gene dosage in CMT1A neuropathy alters Schwann cell growth and differentiation. On the other hand, disease-related missense mutations within transmembrane domains of PMP22 disturb intracellular protein trafficking leading to accumulation of the mutant protein in the endoplasmic reticulum/Golgi compartment. Further, the recently reported association of PMP22 and P0 in peripheral myelin sheds new light on the almost identical phenotypes of CMT1A and CMT1B giving rise to a unifying hypothesis on disease mechanism.
Copyright 2000 Wiley-Liss, Inc.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Animals
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Cell Communication / genetics
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Cell Differentiation / genetics
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Cell Division / genetics
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Charcot-Marie-Tooth Disease / genetics*
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Demyelinating Diseases / genetics*
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Demyelinating Diseases / metabolism
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Demyelinating Diseases / pathology
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Gene Expression
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Humans
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Mice
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Mutation, Missense*
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Myelin P0 Protein / metabolism
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Myelin Proteins / biosynthesis
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Myelin Proteins / genetics*
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Myelin Sheath / metabolism
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Peripheral Nervous System Diseases / genetics*
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Peripheral Nervous System Diseases / metabolism
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Protein Structure, Tertiary / genetics
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Schwann Cells / cytology
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Schwann Cells / metabolism
Substances
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Myelin P0 Protein
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Myelin Proteins
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PMP22 protein, human
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Pmp22 protein, mouse