The Oligodendrocyte-Myelin Glycoprotein of Mouse: Primary Structure and Gene Structure

Mikol, Daniel D.; Rongnoparut, Pornpimol; Allwardt, Brenda A.; Marton, Linda S.; Stefansson, K.

doi:10.1006/geno.1993.1379

Cited by 25 publications

(17 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Developmentally, when white matter tracts are formed, cellular adhesion molecules play an important role in axon guidance along tracts, and in holding tracts together. There is some evidence that OMgp has the potential to function as an adhesion molecule [58], [59], and thus may be affected by NF1 mutation. OMgp expression across development coincides with the progression of myelination, which moves in a caudal to rostral direction [59], and it may have a particularly important effect in thalamocortical tracts (such as the ATR found to be significantly affected in the current study) [60].…”

Section: Discussionmentioning

confidence: 99%

“…There is some evidence that OMgp has the potential to function as an adhesion molecule [58], [59], and thus may be affected by NF1 mutation. OMgp expression across development coincides with the progression of myelination, which moves in a caudal to rostral direction [59], and it may have a particularly important effect in thalamocortical tracts (such as the ATR found to be significantly affected in the current study) [60]. Furthermore, neurofibromin itself has been shown to regulate not only Ras, but also Akt and focal adhesion kinase (FAK), which impacts cell adhesion, migration, and survival [61], [62].…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Alterations in White Matter Microstructure in Neurofibromatosis-1

et al. 2012

View full text Add to dashboard Cite

Neurofibromatosis (NF1) represents the most common single gene cause of learning disabilities. NF1 patients have impairments in frontal lobe based cognitive functions such as attention, working memory, and inhibition. Due to its well–characterized genetic etiology, investigations of NF1 may shed light on neural mechanisms underlying such difficulties in the general population or other patient groups. Prior neuroimaging findings indicate global brain volume increases, consistent with neural over-proliferation. However, little is known about alterations in white matter microstructure in NF1. We performed diffusion tensor imaging (DTI) analyses using tract-based spatial statistics (TBSS) in 14 young adult NF1 patients and 12 healthy controls. We also examined brain volumetric measures in the same subjects. Consistent with prior studies, we found significantly increased overall gray and white matter volume in NF1 patients. Relative to healthy controls, NF1 patients showed widespread reductions in white matter integrity across the entire brain as reflected by decreased fractional anisotropy (FA) and significantly increased absolute diffusion (ADC). When radial and axial diffusion were examined we found pronounced differences in radial diffusion in NF1 patients, indicative of either decreased myelination or increased space between axons. Secondary analyses revealed that FA and radial diffusion effects were of greatest magnitude in the frontal lobe. Such alterations of white matter tracts connecting frontal regions could contribute to the observed cognitive deficits. Furthermore, although the cellular basis of these white matter microstructural alterations remains to be determined, our findings of disproportionately increased radial diffusion against a background of increased white matter volume suggest the novel hypothesis that one potential alteration contributing to increased cortical white matter in NF1 may be looser packing of axons, with or without myelination changes. Further, this indicates that axial and radial diffusivity can uniquely contribute as markers of NF1-associated brain pathology in conjunction with the typically investigated measures.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Alterations in White Matter Microstructure in Neurofibromatosis-1

et al. 2012

View full text Add to dashboard Cite

show abstract

“…Our rabbit anti-OMgp pAb was previously described (Mikol and Stefansson, 1988). In addition, we generated rabbit pAb against a multiple antigenic peptide (Posnett and Tam, 1989) of OMgp (OMgp-pep) that is 100% conserved between mouse (Mikol et al, 1993) and human (Mikol et al, 1990b) (accession numbers Q63912 and X51694.1, respectively). OMgp-pep (LLDKSDTAYQWNLKYLDVSKN, residues 89-109) was generated in the University of Michigan Protein Structure Core Facility.…”

Section: Materials and Methods Antibodiesmentioning

confidence: 99%

Oligodendrocyte‐myelin glycoprotein is present in lipid rafts and caveolin‐1‐enriched membranes

Boyanapalli

Kottis

Lahoud

et al. 2005

Glia

Self Cite

View full text Add to dashboard Cite

The oligodendrocyte-myelin glycoprotein is a ligand of the neuronal Nogo receptor and a potent inhibitor of neurite outgrowth, but its physiological function remains to be elucidated. The oligodendrocyte-myelin glycoprotein is anchored solely in the outer leaflet of the plasma membrane via its glycosylphosphatidylinositol anchor, and through its leucine-rich repeat domain, it likely interacts with other proteins. In the present study, we compare its buoyancy and detergent solubility characteristics with those of other myelin proteins. Based on its detergent solubility profile and membrane fractionation using established ultracentrifugation procedures, we conclude that the oligodendrocyte-myelin glycoprotein is a lipid raft component that is closely associated with the axolemma. Moreover, it associates with caveolin-1 and caveolin-1-enriched membranes. We postulate that, by virtue of its concentration in lipid rafts and perhaps through interactions with caveolin-1, the oligodendrocyte-myelin glycoprotein may influence signaling pathways.

show abstract

“…In addition, we identified two proteins as F3 and CD55. The oligodendrocyte myelin glycoprotein has a molecular mass of 120 kDa, which is reduced to 105 kDa after PI-PLC cleavage (50,51) and may also be included in our preparations. Other candidate molecules for some of the observed components are the ciliary neurotrophic factor receptor ␣ subunit and prion protein, which have been reported to be expressed by oligodendrocyte lineage cells (29,52).…”

Section: Identification Of Oligodendrocyte and Myelin Gpi-anchoredmentioning

confidence: 99%

Oligodendrocytes Direct Glycosyl Phosphatidylinositol-anchored Proteins to the Myelin Sheath in Glycosphingolipid-rich Complexes

Krämer¹,

Koch²,

Niehaus

et al. 1997

Journal of Biological Chemistry

118

127

View full text Add to dashboard Cite

The myelin sheath synthesized by oligodendrocytes insulates central nervous system axons and is a specialized subdomain of the plasma membrane, containing a restricted pattern of proteins and lipids. Myelin is enriched in glycosphingolipids and cholesterol, a lipid environment favored by glycosylphosphatidylinositol (GPI)-anchored proteins, which associate with these lipids in detergent-insoluble complexes in many cell types. Since proteins regulating oligodendroglia-neuron interaction are largely unknown and GPI-anchored proteins are often involved in cell-cell interactions, we examined oligodendrocytes and myelin for their expression of these proteins. Oligodendrocyte precursors and maturing oligodendrocytes express a similar pattern of GPIanchored proteins, which unlike the majority of oligodendrocyte plasma membrane proteins, accumulate in myelin. To elucidate mechanisms underlying the expression of GPI-anchored proteins in myelin, we analyzed detergent-insoluble complexes from cells and myelin using TX-100 extraction and sucrose density gradients. In precursor cells, the GPI-anchored proteins are not incorporated in detergent-insoluble complexes. In contrast, GPI-anchored proteins from maturing oligodendrocytes and from myelin were isolated as complexes associated with glycosphingolipids and cholesterol. These results show a specific association of GPI-anchored proteins with glycosphingolipids and cholesterol during oligodendrocyte maturation and suggest sorting of these macromolecular complexes to myelin.

show abstract

The Oligodendrocyte-Myelin Glycoprotein of Mouse: Primary Structure and Gene Structure

Cited by 25 publications

References 0 publications

Alterations in White Matter Microstructure in Neurofibromatosis-1

Alterations in White Matter Microstructure in Neurofibromatosis-1

Oligodendrocyte‐myelin glycoprotein is present in lipid rafts and caveolin‐1‐enriched membranes

Oligodendrocytes Direct Glycosyl Phosphatidylinositol-anchored Proteins to the Myelin Sheath in Glycosphingolipid-rich Complexes

Contact Info

Product

Resources

About