| First Author | Gardinier MV | Year | 1993 |
| Journal | Trans Am Soc Neurochem | Volume | 24 |
| Pages | 209 (Abstr.) | Mgi Jnum | J:37131 |
| Mgi Id | MGI:84559 | Citation | Gardinier MV, et al. (1993) Murine and human MOG are highly conserved: cDNA analysis. Trans Am Soc Neurochem 24:209 (Abstr.) |
| abstractText | Full text of Abstract: MURINE AND HUMAN MOG ARE HIGHLY CONSERVED: cDNA ANALYSIS. Gardinier, M.V.1 and Matthieu, J.-M.2. 1Pathology Department, Northwestern University Medical School, 303 E. Chicago Ave., Chicago, IL 60611 and 2Laboratoire de Neurochimie, Service de Pediatrie, CHUV, Lausanne, Switzerland CH-1011 Myelin/oligodendrocyte glycoprotein (MOG) is a membrane protein expressed specifically by CNS oligodendrocytes. MOG's localization on the external surface of the myelin sheath makes it an ideal target antigen, and previous studies have shown that MOG is involved in autoimmune demyelination. Our recent investigations of rat MOG cDNAs demonstrated that this protein contains a single variable region Ig-like loop and may be a novel member of the immunoglobulin superfamily. Using a rat MOG cDNA, we have also isolated several MOG-specific clones from mouse brain and human brain- stem cDNA libraries. Sequence analysis of these clones has revealed that MOG protein is highly conserved between these three species (>/=90%). As compared to rat MOG (218 amino acids), mouse MOG exhibits only 9 amino acid changes, and preliminary data suggest 23 amino acid differences between human and rat MOG. The two hydrophobic domains noted in rat MOG were also identified in mouse and human MOG. Most strikingly, the C-terminal domain (beyond the second hydrophobic stretch) is 100% conserved between these species, suggestive of an important functional role for this region. With these molecular tools, we now undertake extensive investigations into MOG function and gene structure. |
