Ultrastructural protein zero expression in Charcot-Marie-Tooth type 1B Disease

• Published in: Muscle & nerve 1999-01, Vol.22 (1), p.99-104
• Main Authors: Sindou, Philippe, Vallat, Jean-Michel, Chapon, Françoise, Archelos, Juan-José, Tabaraud, François, Anani, Thierry, Braund, Kyle G., Maisonobe, Thierry, Hauw, Jean-Jacques, Vandenberghe, Antoon
• Format: Article
• Language: English
• Subjects: Amino Acid Substitution; Biological and medical sciences; Biopsy; Charcot-Marie-Tooth Disease - genetics; Charcot-Marie-Tooth Disease - metabolism; Charcot-Marie-Tooth Disease - physiopathology; Charcot-Marie-Tooth disease 1B; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases; Electrophysiology; Female; Humans; immunocytochemical quantification; Immunohistochemistry; Medical sciences; Middle Aged; Myelin P0 Protein - biosynthesis; Myelin Sheath - metabolism; Nerve Fibers - pathology; Neural Conduction - physiology; Neurology; Point Mutation; protein zero; Sural Nerve - metabolism; Sural Nerve - pathology; ultracryomicrotomy
• ISSN: 0148-639X; 1097-4598
• DOI: 10.1002/(SICI)1097-4598(199901)22:1<99::AID-MUS14>3.0.CO;2-5

Charcot–Marie–Tooth type 1B (CMT 1B) disease, an inherited demyelinating peripheral neuropathy, results from different point mutations located in the P0 gene on chromosome 1 q21–23. We have quantified, at the ultrastructural level, the immunocytochemical expression of the P0 protein in two unrelated CMT 1B patients with mutations (Ser 78 to Leu and Asn 122 to Ser) located in two different exons in the extracellular domain of the protein. A twofold decrease in P0 expression was observed in compact myelin in each case, compared with age‐matched controls. The severity of the phenotypes showed no direct relationship to the levels of P0 protein expression in these 2 patients. © 1999 John Wiley & Sons, Inc. Muscle Nerve 22: 99–104, 1999