Oligodendroglial Maturation Is Dependent on Intracellular Protein Shuttling
Identifieur interne : 002193 ( Ncbi/Curation ); précédent : 002192; suivant : 002194Oligodendroglial Maturation Is Dependent on Intracellular Protein Shuttling
Auteurs : Peter Göttle [Allemagne] ; Jennifer K. Sabo [Australie] ; André Heinen [Allemagne] ; Gene Venables [Australie] ; Klintsy Torres [Allemagne] ; Nevena Tzekova [Allemagne] ; Carlos M. Parras [France] ; David Kremer [Allemagne] ; Hans-Peter Hartung [Allemagne] ; Holly S. Cate [Australie] ; Patrick Küry [Allemagne]Source :
- The Journal of Neuroscience [ 0270-6474 ] ; 2015.
Descripteurs français
- KwdFr :
- Animaux, Cellules cultivées, Cortex cérébelleux (métabolisme), Différenciation cellulaire (physiologie), Facteurs de transcription à motif basique hélice-boucle-hélice (métabolisme), Gaine de myéline (métabolisme), Humains, Inhibiteur p57 de kinase cycline-dépendante (métabolisme), Kinase-2 cycline-dépendante (métabolisme), Lim Kinases (métabolisme), Noyau de la cellule (métabolisme), Oligodendroglie (cytologie), Oligodendroglie (métabolisme), Protéines de répression (métabolisme), Rat Wistar, Rats, Sclérose en plaques (métabolisme), Souris, Transport de protéines (physiologie), Transport nucléaire actif.
- MESH :
- cytologie : Oligodendroglie.
- métabolisme : Cortex cérébelleux, Facteurs de transcription à motif basique hélice-boucle-hélice, Gaine de myéline, Inhibiteur p57 de kinase cycline-dépendante, Kinase-2 cycline-dépendante, Lim Kinases, Noyau de la cellule, Oligodendroglie, Protéines de répression, Sclérose en plaques.
- physiologie : Différenciation cellulaire, Transport de protéines.
- Animaux, Cellules cultivées, Humains, Rat Wistar, Rats, Souris, Transport nucléaire actif.
English descriptors
- KwdEn :
- Active Transport, Cell Nucleus, Animals, Basic Helix-Loop-Helix Transcription Factors (metabolism), Cell Differentiation (physiology), Cell Nucleus (metabolism), Cells, Cultured, Cerebellar Cortex (metabolism), Cyclin-Dependent Kinase 2 (metabolism), Cyclin-Dependent Kinase Inhibitor p57 (metabolism), Humans, Lim Kinases (metabolism), Mice, Multiple Sclerosis (metabolism), Myelin Sheath (metabolism), Oligodendroglia (cytology), Oligodendroglia (metabolism), Protein Transport (physiology), Rats, Rats, Wistar, Repressor Proteins (metabolism).
- MESH :
- chemical , metabolism : Basic Helix-Loop-Helix Transcription Factors, Cyclin-Dependent Kinase 2, Cyclin-Dependent Kinase Inhibitor p57, Lim Kinases, Repressor Proteins.
- cytology : Oligodendroglia.
- metabolism : Cell Nucleus, Cerebellar Cortex, Multiple Sclerosis, Myelin Sheath, Oligodendroglia.
- physiology : Cell Differentiation, Protein Transport.
- Active Transport, Cell Nucleus, Animals, Cells, Cultured, Humans, Mice, Rats, Rats, Wistar.
Abstract
Multiple sclerosis is an autoimmune disease of the CNS resulting in degeneration of myelin sheaths and loss of oligodendrocytes, which means that protection and electrical insulation of axons and rapid signal propagation are impaired, leading to axonal damage and permanent disabilities. Partial replacement of lost oligodendrocytes and remyelination can occur as a result of activation and recruitment of resident oligodendroglial precursor cells. However, the overall remyelination capacity remains inefficient because precursor cells often fail to generate new oligodendrocytes. Increasing evidence points to the existence of several molecular inhibitors that act on these cells and interfere with their cellular maturation. The
Url:
DOI: 10.1523/JNEUROSCI.1423-14.2015
PubMed: 25609610
PubMed Central: 4300332
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PMC:4300332Le document en format XML
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<term>Cell Differentiation (physiology)</term>
<term>Cell Nucleus (metabolism)</term>
<term>Cells, Cultured</term>
<term>Cerebellar Cortex (metabolism)</term>
<term>Cyclin-Dependent Kinase 2 (metabolism)</term>
<term>Cyclin-Dependent Kinase Inhibitor p57 (metabolism)</term>
<term>Humans</term>
<term>Lim Kinases (metabolism)</term>
<term>Mice</term>
<term>Multiple Sclerosis (metabolism)</term>
<term>Myelin Sheath (metabolism)</term>
<term>Oligodendroglia (cytology)</term>
<term>Oligodendroglia (metabolism)</term>
<term>Protein Transport (physiology)</term>
<term>Rats</term>
<term>Rats, Wistar</term>
<term>Repressor Proteins (metabolism)</term>
</keywords>
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<term>Cellules cultivées</term>
<term>Cortex cérébelleux (métabolisme)</term>
<term>Différenciation cellulaire (physiologie)</term>
<term>Facteurs de transcription à motif basique hélice-boucle-hélice (métabolisme)</term>
<term>Gaine de myéline (métabolisme)</term>
<term>Humains</term>
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<term>Kinase-2 cycline-dépendante (métabolisme)</term>
<term>Lim Kinases (métabolisme)</term>
<term>Noyau de la cellule (métabolisme)</term>
<term>Oligodendroglie (cytologie)</term>
<term>Oligodendroglie (métabolisme)</term>
<term>Protéines de répression (métabolisme)</term>
<term>Rat Wistar</term>
<term>Rats</term>
<term>Sclérose en plaques (métabolisme)</term>
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<term>Transport nucléaire actif</term>
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<term>Repressor Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Oligodendroglie</term>
</keywords>
<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Oligodendroglia</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cell Nucleus</term>
<term>Cerebellar Cortex</term>
<term>Multiple Sclerosis</term>
<term>Myelin Sheath</term>
<term>Oligodendroglia</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cortex cérébelleux</term>
<term>Facteurs de transcription à motif basique hélice-boucle-hélice</term>
<term>Gaine de myéline</term>
<term>Inhibiteur p57 de kinase cycline-dépendante</term>
<term>Kinase-2 cycline-dépendante</term>
<term>Lim Kinases</term>
<term>Noyau de la cellule</term>
<term>Oligodendroglie</term>
<term>Protéines de répression</term>
<term>Sclérose en plaques</term>
</keywords>
<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Différenciation cellulaire</term>
<term>Transport de protéines</term>
</keywords>
<keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Cell Differentiation</term>
<term>Protein Transport</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Active Transport, Cell Nucleus</term>
<term>Animals</term>
<term>Cells, Cultured</term>
<term>Humans</term>
<term>Mice</term>
<term>Rats</term>
<term>Rats, Wistar</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Cellules cultivées</term>
<term>Humains</term>
<term>Rat Wistar</term>
<term>Rats</term>
<term>Souris</term>
<term>Transport nucléaire actif</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><p>Multiple sclerosis is an autoimmune disease of the CNS resulting in degeneration of myelin sheaths and loss of oligodendrocytes, which means that protection and electrical insulation of axons and rapid signal propagation are impaired, leading to axonal damage and permanent disabilities. Partial replacement of lost oligodendrocytes and remyelination can occur as a result of activation and recruitment of resident oligodendroglial precursor cells. However, the overall remyelination capacity remains inefficient because precursor cells often fail to generate new oligodendrocytes. Increasing evidence points to the existence of several molecular inhibitors that act on these cells and interfere with their cellular maturation. The <italic>p57kip2</italic>
gene encodes one such potent inhibitor of oligodendroglial differentiation and this study sheds light on the underlying mode of action. We found that subcellular distribution of the p57kip2 protein changed during differentiation of rat, mouse, and human oligodendroglial cells both <italic>in vivo</italic>
and <italic>in vitro</italic>
. Nuclear export of p57kip2 was correlated with promoted myelin expression, higher morphological phenotypes, and enhanced myelination <italic>in vitro</italic>
. In contrast, nuclear accumulation of p57kip2 resulted in blocked oligodendroglial differentiation. Experimental evidence suggests that the inhibitory role of p57kip2 depends on specific interactions with binding proteins such as LIMK-1, CDK2, Mash1, and Hes5 either by controlling their site of action or their activity. Because functional restoration in demyelinating diseases critically depends on the successful generation of oligodendroglial cells, a therapeutic need that is currently unmet, the regulatory mechanism described here might be of particular interest for identifying suitable drug targets and devising novel therapeutic approaches.</p>
</div>
</front>
</TEI>
</record>
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