Several studies have shown a role for antibodies against MOG in the pathogenesis of MS, though most of them were written before the discovery of NMO-IgG and the NMO spectrum of diseases.Īnti-MOG status is different depending whether it is measured by ELISA or by microarray ( CBA). MOG has received much of its laboratory attention in studies dealing with MS. Main article: antiMOG associated encephalomyelitis Anti-MOG associated inflammatory demyelinating diseases
Some of them are not-inflammatory, such as adrenoleukodystrophy, vanishing white matter disease, and Rubella induced mental retardation. Interest in MOG has centered on its role in demyelinating diseases. Role in disease Non-inflammatory demyelinating diseases Also, MOG was shown to dimerize in solution, and the shape complementarity index is high at the dimer interface, suggesting a "biologically relevant MOG dimer." Synthesis ĭevelopmentally, MOG is formed "very late on oligodendrocytes and the myelin sheath". Several features of the protein structure suggest MOG has a role as an "adhesin in the completion and/or compaction of the myelin sheath." There is a "significant strip" of electronegative charge beginning near the N-terminus and running about half the length of the molecule.
The beta strands are within two antiparallel beta sheets that form an immunoglobulin-like beta-sandwich fold. The dssp secondary structure of the protein is 6% helical and 43% beta sheet: there are three short helical segments and ten beta strands. This protein is 139 residues long, and is a member of the immunoglobulin superfamily. The crystal structure of myelin oligodendrocyte glycoprotein was determined by x-ray diffraction at a resolution of 1.45 Angstrom, using protein from the Norway rat. The introns "contain numerous reptitive DNA " sequences, among which is "14 Alu sequences within 3 introns", and have a range varying from 242 to 6484 bp.īecause of alternatively spliced from human mRNA of MOG gene forming at least nine isoforms. The MOG "primary nuclear transcript … is 15,561 nucleotides in length" and, for humans, it has eight exons which are "separated by seven introns". and therefore easily accessible for autoantibodies. "A single Ig-domain is exposed to the extracellular space" and consequently allows autoantibodies easy access.
"MOG is a quantitatively minor type I transmembrane protein, and is found exclusively in the CNS. It is a transmembrane protein expressed on the surface of oligodendrocyte cell and on the outermost surface of myelin sheaths. The gene for MOG, found on chromosome 6 p21.3-p22, was first sequenced in 1995. This suggests "an important biological role for this protein". MOG's cDNA coding region in humans have been shown to be "highly homologous" to rats, mice, and bovine, and hence highly conserved. More specifically, MOG is speculated to be "necessary" as an "adhesion molecule" on the myelin sheath of the CNS to provide the structural integrity of the myelin sheath. While the primary molecular function of MOG is not yet known, its likely role with the myelin sheath is either in sheath "completion and/or maintenance".
0 kommentar(er)
