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Rapid Communication: Human Peripheral Myelin Protein‐22 Carries the L2/HNK‐1 Carbohydrate Adhesion Epitope
Author(s) -
Snipes G. Jackson,
Suter Ueli,
Shooter Eric M.
Publication year - 1993
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1993.tb09840.x
Subject(s) - epitope , myelin , gene , biology , peripheral myelin protein 22 , immunology , microbiology and biotechnology , genetics , phenotype , antigen , central nervous system , neuroscience
Molecular genetic studies have established that mutations in the gene encoding the 22‐kDa peripheral myelin protein (PMP‐22) are responsible for hereditary peripheral neuropathies in the trembler mouse and in a subset of humans with Charcot‐Marie‐Tooth disease, type 1a. The function of the PMP‐22 protein remains unknown. Several studies on myelin proteins in the PNS have indicated that the L2/HNK‐1 epitope, which is believed to be both a ligand for cellular adhesion and a target for autoimmune monoclonal IgM neuritis, may be found on heretofore unidentified proteins with a molecular mass of 19–28 kDa. In this report, we provide immunological evidence that at least one of these proteins is PMP‐22.