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Membrane topology of the myelin/oligodendrocyte glycoprotein.
- Source :
-
European journal of biochemistry [Eur J Biochem] 1998 Dec 01; Vol. 258 (2), pp. 478-84. - Publication Year :
- 1998
-
Abstract
- Myelin/oligodendrocyte glycoprotein (MOG), a specific component of the mammalian central nervous system, is located on the surface of the oligodendrocyte plasma membrane and the outermost lamellae of mature myelin; it is expressed during the latter steps of myelinogenesis. It has been shown that MOG may play a pathological role in autoimmune demyelinating diseases of the central nervous system, although its physiological function remains unknown. MOG is an integral membrane glycoprotein with an extracellular immunoglobulin-like domain and two hydrophobic segments which were predicted to be membrane-spanning on the basis of hydropathy analysis. As a first step in elucidation of MOG function, we have investigated its membrane topology, combining immunofluorescence studies on cultured oligodendrocytes and MOG-transfected Chinese hamster ovary cells with biochemical analyses, including in vitro translation, membrane insertion and protease-digestion assays. Our results indicate that the C-terminal tail of MOG is located into the cytoplasm, and that only the first hydrophobic region of MOG spans the membrane whereas the second hydrophobic region appears to be semi-embedded in the lipid bilayer, lying partially buried in the membrane with its N-terminal and C-terminal boundaries facing the cytoplasm.
- Subjects :
- Amino Acid Sequence
Animals
CHO Cells
Carboxypeptidases metabolism
Cathepsin A
Cricetinae
Endopeptidase K metabolism
Humans
Immunohistochemistry
Membrane Glycoproteins chemistry
Microsomes metabolism
Molecular Sequence Data
Mutagenesis, Site-Directed genetics
Myelin Proteins
Myelin-Associated Glycoprotein genetics
Myelin-Oligodendrocyte Glycoprotein
Nerve Tissue Proteins chemistry
Oligodendroglia chemistry
Protein Biosynthesis genetics
Transcription, Genetic genetics
Transfection genetics
Myelin-Associated Glycoprotein chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0014-2956
- Volume :
- 258
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- European journal of biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 9874214
- Full Text :
- https://doi.org/10.1046/j.1432-1327.1998.2580478.x