title: Tetraspan myelin protein PMP22 and demyelinating peripheral neuropathies: new facts and hypotheses.
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.
authors.affiliation: Molecular Neurobiology Laboratory, Department of Neurology and Center for Biological and Medical Research, Heinrich-Heine-University, Düsseldorf, Germany. mueller@neurologie.uni-duesseldorf.de
authors.forename: H W
authors.initials: HW
authors.lastname: Müller
mesh_terms: D000818:Animals; D002450:Cell Communication / Q000235:genetics; D002454:Cell Differentiation / Q000235:genetics; D002455:Cell Division / Q000235:genetics; D002607:Charcot-Marie-Tooth Disease / Q000235:genetics*; D003711:Demyelinating Diseases / Q000235:genetics* / Q000378:metabolism / Q000473:pathology; D015870:Gene Expression; D006801:Humans; D051379:Mice; D020125:Mutation, Missense; D018993:Myelin P0 Protein / Q000378:metabolism; D009185:Myelin Proteins / Q000096:biosynthesis / Q000235:genetics*; D009186:Myelin Sheath / Q000378:metabolism; D010523:Peripheral Nervous System Diseases / Q000235:genetics* / Q000378:metabolism; D017434:Protein Structure, Tertiary / Q000235:genetics; D012583:Schwann Cells / Q000166:cytology / Q000378:metabolism
chemical_list: D018993:Myelin P0 Protein; D009185:Myelin Proteins; C073687:PMP22 protein, human; C489545:Pmp22 protein, mouse