ArticleThe Journal of biological chemistry2008
Opalin, a transmembrane sialylglycoprotein located in the central nervous system myelin paranodal loop membrane.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 64 citations in OpenAlex.
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- Embryonic origins of forebrain oligodendrocytes revisited by combinatorial genetic fate mapping.eLife · 2024Article
- OPALIN is an LGI1 receptor promoting oligodendrocyte differentiation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
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- Age-Dependent Increase in Schmidt-Lanterman Incisures and a Cadm4-Associated Membrane Skeletal Complex in Fatty Acid 2-hydroxylase Deficient Mice: a Mouse Model of Spastic Paraplegia SPG35.Molecular neurobiology · 2022Article
- TRPV2: A Key Player in Myelination Disorders of the Central Nervous System.International journal of molecular sciences · 2022Article
- Four specific biomarkers associated with the progression of glioblastoma multiforme in older adults identified using weighted gene co-expression network analysis.Bioengineered · 2021Article
- Ethanol effects on cerebellar myelination in a postnatal mouse model of fetal alcohol spectrum disorders.Alcohol (Fayetteville, N.Y.) · 2021Article
- Bone marrow mesenchymal stem cells and their derived exosomes resolve doxorubicin-induced chemobrain: critical role of their miRNA cargo.Stem cell research & therapy · 2021Article
- Review
- Modeling Cell-Cell Interactions from Spatial Molecular Data with Spatial Variance Component Analysis.Cell reports · 2019Article
- Microglial activation in an amyotrophic lateral sclerosis-like model caused by Ranbp2 loss and nucleocytoplasmic transport impairment in retinal ganglion neurons.Cellular and molecular life sciences : CMLS · 2019Article
- TMEM10 Promotes Oligodendrocyte Differentiation and is Expressed by Oligodendrocytes in Human Remyelinating Multiple Sclerosis Plaques.Scientific reports · 2019Article
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- Remarkable Stability of Myelinating Oligodendrocytes in Mice.Cell reports · 2017Article
- A high resolution atlas of gene expression in the domestic sheep (Ovis aries).PLoS genetics · 2017Article
- The Brain NO Levels and NOS Activities Ascended in the Early and Middle Stages and Descended in the Terminal Stage in Scrapie-Infected Animal Models.Molecular neurobiology · 2017Article
- Partial Immunoblotting of 2D-Gels: A Novel Method to Identify Post-Translationally Modified Proteins Exemplified for the Myelin Acetylome.Proteomes · 2017Article
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Authors and funding
13 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In contrast to compact myelin, the series of paranodal loops located in the outermost lateral region of myelin is non-compact; the intracellular space is filled by a continuous channel of cytoplasm, the extracellular surfaces between neighboring loops keep a definite distance, but the loop membranes have junctional specializations. Although the proteins that form compact myelin have been well studied, the protein components of paranodal loop membranes are not fully understood. This report describes the biochemical characterization and expression of Opalin as a novel membrane protein in paranodal loops. Mouse Opalin is composed of a short N-terminal extracellular domain (amino acid residues 1-30), a transmembrane domain (residues 31-53), and a long C-terminal intracellular domain (residues 54-143). Opalin is enriched in myelin of the central nervous system, but not that of the peripheral nervous system of mice. Enzymatic deglycosylation showed that myelin Opalin contained N- and O-glycans, and that the O-glycans, at least, had negatively charged sialic acids. We identified two N-glycan sites at Asn-6 and Asn-12 and an O-glycan site at Thr-14 in the extracellular domain. Site-directed mutations at the glycan sites impaired the cell surface localization of Opalin. In addition to the somata and processes of oligodendrocytes, Opalin immunoreactivity was observed in myelinated axons in a spiral fashion, and was concentrated in the paranodal loop region. Immunogold electron microscopy demonstrated that Opalin was localized at particular sites in the paranodal loop membrane. These results suggest a role for highly sialylglycosylated Opalin in an intermembranous function of the myelin paranodal loops in the central nervous system.
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