Structure of the Human Myelin/Oligodendrocyte Glycoprotein Gene and Multiple Alternative Spliced Isoforms
Myelin/oligodendrocyte glycoprotein (MOG), a specific component of the central nervous system localized on the outermost lamellae of mature myelin, is a member of the immunoglobulin superfamily. We report here the organization of the humanMOGgene, which spans approximately 17 kb, and the characteriz...
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Published in | Genomics (San Diego, Calif.) Vol. 29; no. 2; pp. 345 - 352 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
San Diego, CA
Elsevier Inc
20.09.1995
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | Myelin/oligodendrocyte glycoprotein (MOG), a specific component of the central nervous system localized on the outermost lamellae of mature myelin, is a member of the immunoglobulin superfamily. We report here the organization of the humanMOGgene, which spans approximately 17 kb, and the characterization of six MOG mRNA splicing variants. The intron/exon structure of the humanMOGgene confirmed the splicing pattern, supporting the hypothesis that mRNA isoforms could arise by alternative splicing of a single gene. In addition to the eight exons coding for the major MOG isoform, the humanMOGgene also contains, in the 3′ region, a previously unknown alternatively spliced coding exon, VIA. Alternative utilization of two acceptor splicing sites for exon VIII could produce two different C-termini. The nucleotide sequences presented here may be a useful tool to study further possible involvement of theMOGgene in hereditary neurological disorders. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0888-7543 1089-8646 |
DOI: | 10.1006/geno.1995.9995 |