Intracellular Distribution of Myelin Protein Gene Products Is Altered in Oligodendrocytes of the taiep Rat

O'Connor, Lawrence T.; Goetz, Brian D.; Couve, Eduardo; Song, Jian; Duncan, Ian D.

doi:10.1006/mcne.2000.0889

Cited by 42 publications

(29 citation statements)

References 50 publications

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“…Numerous studies have been conducted to evaluate the developmental profile of Plp gene expression in the CNS at both the mRNA [14,15,19,20,55,69,[78][79][80][81][82][83][84][85][86][87][88][89][90][91][92][93] and protein [11, 55, 86, 94 -98] levels. The consensus of these studies is that in oligodendrocytes, the peak of Plp gene expression is coincident with the active myelination period of CNS development, which occurs about 3 weeks postnatally in rodents.…”

Section: Temporal Regulation Of Plp Gene Expressionmentioning

confidence: 99%

Where, when and how much: regulation of myelin proteolipid protein gene expression

Wight

Dobretsova

2004

Cellular and Molecular Life Sciences (CMLS)

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The myelin proteolipid protein (PLP) gene ( Plp) encodes the most abundant protein found in myelin from the central nervous system (CNS). Expression of the gene is regulated in a spatiotemporal manner with maximal levels of expression occurring in oligodendrocytes during the active myelination period of CNS development, although other cell types in the CNS as well as in the periphery can express the gene to a much lower degree. In oligodendrocytes, Plp gene expression is tightly regulated. Underexpression or overexpression of the gene has been shown to have adverse effects in humans and other vertebrates. In light of this strict control, this review provides an overview of the current knowledge of Plp gene regulation.

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Section: Temporal Regulation Of Plp Gene Expressionmentioning

confidence: 99%

Where, when and how much: regulation of myelin proteolipid protein gene expression

Wight

Dobretsova

2004

Cellular and Molecular Life Sciences (CMLS)

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“…The much greater reduction of MAG in comparison with other myelin proteins is probably related to the fact that it has the greatest distance to be transported to the distal periaxonal membrane. Interestingly, the deficit of MAG results in structural pathology at the periaxonal region similar to that in MAG-null mice [159]. Another murine mutant in which abnormalities of MAG are likely to have an important role is the quaking mouse, which is inherited as an autosomal recessive characterized by a myelin deficiency in both the CNS and PNS.…”

Section: Magmentioning

confidence: 99%

Myelin sheaths: glycoproteins involved in their formation, maintenance and degeneration

2002

CMLS, Cell. Mol. Life Sci.

137

124

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Myelin sheaths are formed around axons by extending, biochemically modifying and spiraling plasma membranes of Schwann cells in the peripheral nervous system (PNS) and oligodendrocytes in the central nervous system (CNS). Because glycoproteins are prominent components of plasma membranes, it is not surprising that they have important roles in the formation, maintenance and degeneration of myelin sheaths. The emphasis in this review is on four integral membrane glycoproteins. Two of them, protein zero (P0) and peripheral myelin protein-22 (PMP-22), are components of compact PNS myelin. The other two are preferentially localized in membranes of sheaths that are distinct from compact myelin. One is the myelin-associated glycoprotein, which is localized at the inside of sheaths where it functions in glia-axon interactions in both the PNS and CNS. The other is the myelin-oligodendrocyte glycoprotein, which is preferentially localized on the outside of CNS myelin sheaths and appears to be an important target antigen in autoimmune demyelinating diseases such as multiple sclerosis.

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“…An impaired vesicle transfer might block intracellular membrane sorting en route to the plasma membrane and thereby inhibit myelination. This interpretation is supported by the notion that PLP is associated with myelin specific lipids and the report that the cellular distribution of myelin components is altered in a hypo-and demyelinating rat model (O'Connor et al, 2000;Simons et al, 2000).…”

Section: Discussionmentioning

confidence: 54%

Rumpshaker‐like proteolipid protein (PLP) ratio in a mouse model with unperturbed structural and functional integrity of the myelin sheath and axons in the central nervous system

Uschkureit

Spörkel

Büssow

et al. 2001

Glia

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The gene plp on the X chromosome encodes the isoforms proteolipid protein (PLP) and DM(20), two dominant integral membrane proteins of central nervous system (CNS) myelin. DM(20) results from the activation of the cryptic splice site in exon III of the PLP gene. We inserted a sense-orientated loxP flanked neomycin-gene into intron III of the plp sequence, using homologous recombination in embryonic stem cells and generated the homozygous neoS mouse line. Unlike the previously described complete PLP/DM(20) ablation (plp(-/-)), which has been obtained by introducing a neo-gene in antisense-orientation in the same position of intron III, the plp expression surprisingly revealed reduced mRNA levels. The PLP isoform was reduced to 50%, but DM(20) expression was unaffected. This protein pattern resembles the expression profile of the PLP isoforms in the natural occurring rumpshaker mutant. Electron microscopic examination revealed a normal compaction of CNS-myelin and maintenance of axon integrity. PLP expression levels of the wt control were recovered by Cre excision of the neo-selection gene after intercrossing neoS mice and oligodendrocyte-specific Cre-mice. These data strongly hint at different functions of intron III in PLP/DM(20)-specific splicing and mRNA stability. Furthermore evidence is provided for functionally affected translation products of the PLP gene in the rumpshaker mutant, whereas no PLP-isoform occur in plp(-/-) mice generated by introducing a selectable marker into intron III in antisense orientation.

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Intracellular Distribution of Myelin Protein Gene Products Is Altered in Oligodendrocytes of the taiep Rat

Cited by 42 publications

References 50 publications

Where, when and how much: regulation of myelin proteolipid protein gene expression

Where, when and how much: regulation of myelin proteolipid protein gene expression

Myelin sheaths: glycoproteins involved in their formation, maintenance and degeneration

Rumpshaker‐like proteolipid protein (PLP) ratio in a mouse model with unperturbed structural and functional integrity of the myelin sheath and axons in the central nervous system

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