Myelin‐specific domain on the plasmalemma of oligodendroglia: Differential expression in the rat and hypomyelinating mouse mutants jimpy and quaking

Gard, Anthony L.; Dutton, Gary R.

doi:10.1002/jnr.490170403

Cited by 8 publications

(8 citation statements)

References 45 publications

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“…For staining of the extracellular epitope corresponding to aa 202-223 of both PLP and DM20, the cells were first incubated with antibody 1A9 (1:200) (Gard and Dutton, 1987;Gow et al, 1997; a gift from A.L. Gard, Mobile, AL) and then fixed in 4% paraformaldehyde for 20 min.…”

Section: Immunofluorescent Stainingmentioning

confidence: 99%

“…In addition, PLP and GalCer were coexpresssed in these cells to examine the influence of GalCer on PLP transport. Furthermore, PLP transport to and insertion into the plasma membrane was examined in the absence of sulfatide in cultured oligodendrocytes by using an anti-PLP antibody directed to the second extracellular domain of PLP (Gard and Dutton, 1987;Gow et al, 1997). Our results demonstrate that PLP is not specifically associated with glycolipid domains and that the protein can be transported to the plasma membrane independently of galacto-sphingolipids.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Transport of proteolipid protein to the plasma membrane does not depend on glycosphingolipid cotransport in oligodendrocyte cultures

et al. 1998

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The possibility that transport of proteolipid protein (PLP) from its site of synthesis to the plasma membrane is dependent on cotransport with (sulfo)galacto-cerebrosides was investigated in primary cultured oligodendrocytes and Chinese hamster ovary (CHO) cells expressing PLP. Sulfation was inhibited by growing oligodendrocytes in the presence of a competitive inhibitor of this process, sodium chlorate. Under these circumstances, sulfatide synthesis was inhibited by 85%. Nevertheless, PLP was still delivered to the plasma membrane in quantitative amounts. Furthermore, when PLP was expressed in CHO cells, which normally synthesize very low amounts of galactosyl ceramide (GalCer) and no sulfatide, PLP was transported to the plasma membrane. Moreover, in CHO cells coexpressing PLP and ceramide galactosyl transferase, PLP cell surface labeling was unaltered. Noting that it has been demonstrated that proteins destined for the apical surface of epithelial cells colocalize with glycolipid-enriched microdomains, we isolated detergent-insoluble membrane complexes from cultured oligodendrocytes. We found, however, that most of the PLP is present in the detergent-soluble fraction and, furthermore, that PLP could not be chased into or out of the insoluble fraction. Taken together, these data make it very likely that in oligodendrocytes PLP transport takes place irrespective of the presence of glycosphingolipids GalCer and sulfatide.

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Section: Immunofluorescent Stainingmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Transport of proteolipid protein to the plasma membrane does not depend on glycosphingolipid cotransport in oligodendrocyte cultures

et al. 1998

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“…Mouse monoclonal antibody MOG 8-18C5 was used at 1:50 dilution (Dr. C. Linington, Max Planck Institute for Neurobiology, Martinsried, Germany). Rat monoclonal antibody to PLP was a generous gift from Dr. A. Gard (University of South Alabama, Mobile, AL) (Gard and Dutton, 1987). Secondary conjugated antibodies were purchased from Jackson ImmunoResearch (West Grove, PA).…”

Section: Methodsmentioning

confidence: 99%

The Microtubule-Associated Protein Tumor Overexpressed Gene/Cytoskeleton-Associated Protein 5 Is Necessary for Myelin Basic Protein Expression in Oligodendrocytes

Francone¹,

Maggipinto²,

Kosturko³

et al. 2007

J. Neurosci.

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Tumor overexpressed gene (TOG) protein, encoded by cytoskeleton-associated protein CKAP5, is a microtubule-associated protein that binds to heterogeneous nuclear ribonucleoprotein (hnRNP) A2. hnRNP A2 is an RNA trafficking factor that associates with myelin basic protein (MBP) mRNA. In oligodendrocytes, TOG, hnRNP A2, and MBP mRNA colocalize in granules that assemble in the perikaryon and are transported to the peripheral network of processes that extends from it. MBP accumulates preferentially in the membrane of the medial and distal portions of these cellular processes. MBP expression was reduced when TOG level was lowered by short-hairpin (sh) RNA. The reduction in TOG did not affect overall cell morphology or the assembly, transport, localization, or number of MBP mRNAcontaining granules. Reduced levels of TOG did not affect another oligodendrocyte-specific component, myelin oligodendrocyte glycoprotein, which is expressed at the same time as MBP but translated from mRNA localized in the cell body. Expression in a neural cell line of a green fluorescent protein (GFP)-MBP fusion protein derived from a construct containing GFP and the full-length cDNA for the rat 14 kDa MBP was reduced when TOG level was lowered by shRNA treatment. Expression of GFP, derived from GFP mRNA containing the hnRNP A2 binding element of MBP mRNA, was similarly reduced in cells with low TOG levels. These data indicate that TOG is necessary for efficient translation of MBP mRNA and suggest that this role is mediated by its interaction with hnRNP A2.

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“…This marker recognizes an epitope of myelin and the plasmalemma of live OCs that is undetectable in jp (Gard and Dutton, 1987) and configured within a native ectodomain shared by PLP and DM-20 (Gow et al, 1997). The absence of 1A9 staining readily identified mutants (Fig.…”

Section: Immunopanning Captures Viable Obs From Postnatal Jp Brainstemmentioning

confidence: 96%

“…In mixed cell type cultures of postnatal jp brain, relatively normal numbers of OCs make myelin-associated glycolipids (Gard and Dutton, 1987;Ghandour and Skoff, 1988) but only rarely mature , as evidenced by their significantly decreased levels of myelin basic protein (MBP) and MBP mRNA (Zeller et al, 1989;Knapp et al, 1996) and their failure to stain with OC-specific monoclonal antibodies (mabs) (Gard and Dutton, 1987) which recognize a native ectodomain of DM-20/PLP (Gow et al, 1997). However, jp OCs enriched by secondary culture can express detectable levels of PLP mRNA and truncated PLP protein within the cytoplasm (Feutz et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

In vitro death of jimpy oligodendrocytes: Correlation with onset of DM-20/PLP expression and resistance to oligodendrogliotrophic factors

Williams¹,

Gard²

1997

J. Neurosci. Res.

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Severe hypomyelination in the jimpy (jp) mouse mutation results from premature death of most oligodendrocytes (OCs). We have applied an immunopanning technique to successfully purify oligodendroblasts (OBs) directly from neonatal jp brainstem in order to determine if their death during differentiation into OCs is preventable in culture by diffusible oligodendrogliotrophic factors. No significant differences in the yield (0.9-1.1 x 10(5) cells/brainstem) or viability (approximately 90%) of OB populations from jp and wild-type (wt) littermates were observed, indicating that cell death occurs at a later stage in the mutant lineage. When cultured in a basally defined, insulin-containing medium, wt and jp OBs died 1-2 days later as their differentiation into GalC+ OCs began. Survival was not enhanced by known trophic factors (ciliary neurotrophic factor, leukemia inhibitory factor, neurotrophin-3) for differentiating rat OCs. In medium conditioned by neonatally derived rat or wt mouse astrocytes, however, wt OBs survived terminal OC differentiation, expressing first GalC, then DM-20/PLP on their surface 1-2 days later, before elaborating myelin-like membrane. By contrast, jp OBs in sister cultures survived differentiation initially as well as their normal counterparts did but rapidly died thereafter, beginning at the time when PLP/DM-20 immunoreactivity became detectable on premature wt GalC+ OCs. Additionally under these conditions, there survived a minor population (<5%) of jp cells, including mature OCs, which expressed stunted membranes and DM-20/PLP immunoreactivity in their cytoplasm, and undifferentiated progenitors. This model supports the concept that OC death in jp is effected by an intrinsic program, one mechanistically related to jp PLP/DM-20 gene expression and refractory to trophic cues in the environment.

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Myelin‐specific domain on the plasmalemma of oligodendroglia: Differential expression in the rat and hypomyelinating mouse mutants jimpy and quaking

Cited by 8 publications

References 45 publications

Transport of proteolipid protein to the plasma membrane does not depend on glycosphingolipid cotransport in oligodendrocyte cultures

Transport of proteolipid protein to the plasma membrane does not depend on glycosphingolipid cotransport in oligodendrocyte cultures

The Microtubule-Associated Protein Tumor Overexpressed Gene/Cytoskeleton-Associated Protein 5 Is Necessary for Myelin Basic Protein Expression in Oligodendrocytes

In vitro death of jimpy oligodendrocytes: Correlation with onset of DM-20/PLP expression and resistance to oligodendrogliotrophic factors

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