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Characterization and Expression of the cDNA Coding for the Human Myelin/Oligodendrocyte Glycoprotein
Author(s) -
PhamDinh Danielle,
Allinquant Bernadette,
Ruberg Merle,
Della Gaspera Bruno,
Nussbaum JeanLouis,
Dautigny André
Publication year - 1994
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 - 10.1046/j.1471-4159.1994.63062353.x
Subject(s) - complementary dna , myelin oligodendrocyte glycoprotein , microbiology and biotechnology , biology , coding region , untranslated region , peptide sequence , signal peptide , oligodendrocyte , nucleic acid sequence , northern blot , myelin , gene , genetics , messenger rna , experimental autoimmune encephalomyelitis , immune system , neuroscience , central nervous system
We report here the characterization of a full‐length cDNA encoding the human myelin/oligodendrocyte glycoprotein (MOG). The sequence of the coding region of the human MOG cDNA is highly homologous to that of other previously cloned mouse, rat, and bovine MOG cDNAs, but the 3′ untranslated region differs by an insertion of an Alu sequence between nucleotides 1,590 and 1,924. Accordingly, northern blot analyzes with cDNA probes corresponding to the coding region or the 3′ untranslated Alu‐containing sequence revealed a single band of 2 kb, rather than the 1.6 kb of bovine, rat, or mouse MOG cDNA(s). Immunocytochemical analysis of HeLa cells transfected with human MOG cDNA, which was performed using a specific antibody raised against whole MOG, clearly indicated that MOG is expressed at the cell surface as an intrinsic protein. These data are in accordance with the predicted amino acid sequence, which contains a signal peptide and two putative transmembrane domains. The knowledge of the human MOG sequence should facilitate further investigations on its potential as a target antigen in autoimmune demyelinating diseases like multiple sclerosis.