Cells positive for the O4 surface antigen isolated by cell sorting are able to differentiate into astrocytes or oligodendrocytes

Trotter, Jacqueline; Schachner, Melitta

doi:10.1016/0165-3806(89)90148-x

Cited by 143 publications

(91 citation statements)

References 24 publications

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“…Mixed glial cell cultures containing oligodendrocytes and astrocytes were produced from 1-d-old neonatal mice as described previously (McCarthy and de Vellis, 1980;Trotter and Schachner, 1989). Cultures were prepared with high-glucose DMEM supplemented with 10% fetal bovine serum and replenished on day 4 and every 3-4 d thereafter for 10 d with DMEM plus 10% heat-inactivated horse serum.…”

Section: Methodsmentioning

confidence: 99%

Truncated Prion Protein and Doppel Are Myelinotoxic in the Absence of Oligodendrocytic PrP^C

et al. 2005

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The cellular prion protein PrP C confers susceptibility to transmissible spongiform encephalopathies, yet its normal function is unknown. Although PrP C -deficient mice develop and live normally, expression of amino proximally truncated PrP C (⌬PrP) or of its structural homolog Doppel (Dpl) causes cerebellar degeneration that is prevented by coexpression of full-length PrP C . We now report that mice expressing ⌬PrP or Dpl suffer from widespread leukoencephalopathy. Oligodendrocyte-specific expression of full-length PrP C under control of the myelin basic protein (MBP) promoter repressed leukoencephalopathy and vastly extended survival but did not prevent cerebellar granule cell (CGC) degeneration. Conversely, neuron-specific PrP C expression under control of the neuron-specific enolase (NSE) promoter antagonized CGC degeneration but not leukoencephalopathy. PrP C was found in purified myelin and in cultured oligodendrocytes of both wild-type and MBP-PrP transgenic mice but not in NSE-PrP mice. These results identify white-matter damage as an extraneuronal PrP-associated pathology and suggest a previously unrecognized role of PrP C in myelin maintenance.

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Section: Methodsmentioning

confidence: 99%

Truncated Prion Protein and Doppel Are Myelinotoxic in the Absence of Oligodendrocytic PrP^C

et al. 2005

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“…Mixed glial cell cultures containing oligodendrocytes and astrocytes were produced from 1-day-old neonatal mice as described. 23,24 Cultures were prepared with high-glucose Dulbecco's modified Eagle medium supplemented with 10% fetal bovine serum and replenished on day 4 and every 3 to 4 days thereafter for 10 days, with Dulbecco's modified Eagle medium plus 10% heat-inactivated horse serum. Oligodendrocytes were purified from mixed glial cultures by differential detachment and negative selection of microglia by adherence to hydrophobic plastic.…”

Section: Preparation Of Cerebellar Granule Cells Oligodendrocytes Amentioning

confidence: 99%

Antiprion Prophylaxis by Gene Transfer of a Soluble Prion Antagonist

Genoud

Ott

Braun

et al. 2008

The American Journal of Pathology

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“…32,33 Shaken-off primary OPCs were cultured on poly-L-lysine-coated glass coverslips in SATO medium containing 1% horse serum (Gibco, Eggenstein, Germany), 10 ng/ml platelet-derived growth factor (Sigma, Munich, Germany), and 5 ng/ml basic fibroblast growth factor (Gibco). Reverse transcriptionpolymerase chain reaction (RT-PCR) experiments were performed by using the OliNeu cell line, 34 either as undifferentiated OPCs or 1 week after differentiation to OLs with 1 mmol/L cAMP (Sigma).…”

Section: Cell Culturementioning

confidence: 99%

Re-Expression of a Developmentally Restricted Potassium Channel in Autoimmune Demyelination

Herrero-Herranz¹,

Pardo²,

Bunt³

et al. 2007

The American Journal of Pathology

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Mechanisms of lesion repair in multiple sclerosis are incompletely understood. To some degree, remyelination can occur, associated with an increase of proliferating oligodendroglial cells. Recently, the expression of potassium channels has been implicated in the control of oligodendrocyte precursor cell proliferation in vitro. We investigated the expression of Kv1.4 potassium channels in myelin oligodendrocyte glycoprotein-induced experimental autoimmune encephalomyelitis, a model of multiple sclerosis. Confocal microscopy revealed expression of Kv1.4 in AN2-positive oligodendrocyte precursor cells and premyelinating oligodendrocytes in vitro but neither in mature oligodendrocytes nor in the spinal cords of healthy adult mice. After induction of myelin oligodendrocyte glycoprotein-induced experimental autoimmune encephalomyelitis, Kv1.4 immunoreactivity was detected in or around lesions already during disease onset with a peak early and a subsequent decrease in the late phase of the disease. Kv1.4 expression was confined to 2,3-cyclic nucleotide 3-phosphodiesterase-positive oligodendroglial cells, which were actively proliferating and ensheathed naked axons. After a demyelinating episode, the number of Kv1.4 and 2,3-cyclic nucleotide 3-phosphodiesterase double-positive cells was greatly reduced in ciliary neurotrophic factor knockout mice, a model with impaired lesion repair. In summary, the re-expression of an oligodendroglial potassium channel may have a functional implication on oligodendroglial cell cycle progression, thus influencing tissue repair in experimental autoimmune encephalomyelitis and multiple sclerosis.

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Cells positive for the O4 surface antigen isolated by cell sorting are able to differentiate into astrocytes or oligodendrocytes

Cited by 143 publications

References 24 publications

Truncated Prion Protein and Doppel Are Myelinotoxic in the Absence of Oligodendrocytic PrP^C

Truncated Prion Protein and Doppel Are Myelinotoxic in the Absence of Oligodendrocytic PrP^C

Antiprion Prophylaxis by Gene Transfer of a Soluble Prion Antagonist

Re-Expression of a Developmentally Restricted Potassium Channel in Autoimmune Demyelination

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Cells positive for the O4 surface antigen isolated by cell sorting are able to differentiate into astrocytes or oligodendrocytes

Cited by 143 publications

References 24 publications

Truncated Prion Protein and Doppel Are Myelinotoxic in the Absence of Oligodendrocytic PrPC

Truncated Prion Protein and Doppel Are Myelinotoxic in the Absence of Oligodendrocytic PrPC

Antiprion Prophylaxis by Gene Transfer of a Soluble Prion Antagonist

Re-Expression of a Developmentally Restricted Potassium Channel in Autoimmune Demyelination

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Product

Resources

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Truncated Prion Protein and Doppel Are Myelinotoxic in the Absence of Oligodendrocytic PrP^C

Truncated Prion Protein and Doppel Are Myelinotoxic in the Absence of Oligodendrocytic PrP^C