Chloroquine myopathy suggests that tau is degraded in lysosomes: implication for the formation of paired helical filaments in Alzheimer's disease
Identifieur interne : 002771 ( Main/Exploration ); précédent : 002770; suivant : 002772Chloroquine myopathy suggests that tau is degraded in lysosomes: implication for the formation of paired helical filaments in Alzheimer's disease
Auteurs : Fumitaka Oyama [Japon] ; Nobuyuki Murakami [Nouvelle-Zélande, Japon] ; Yasuo Ihara [Japon]Source :
- Neuroscience Research [ 0168-0102 ] ; 1998.
English descriptors
- Teeft :
- Acta neuropathol, Autophagic vacuoles, Bers, Biol, Cell biol, Chem, Chloroquine, Chloroquine myopathy, Cuervo, Cytosolic, Cytosolic proteins, Degenerating neurons, Degradation, Degraded, Early phase, Goedert, Helical, Ihara, Immunoreactivity, Intracellular, Isoforms, Late phase, Liver lysosomes, Lysosomal, Lysosomal degradation, Lysosomal membrane, Lysosome, Microtubule, Mrna, Murakami, Myopathy, Neuron, Neuropathol, Neuropil threads, Neurosci, Neuroscience, Neuroscience research, Oyama, Phosphorylated, Phosphorylation, Rimmed, Rimmed vacuoles, Selective uptake, Tubulin, Vacuole.
Abstract
Abstract: We have found that amorphous tau deposits in chloroquine myopathy (CM), a vacuolar myopathy induced by the administration of chloroquine, a well-known lysosomotropic agent. The dynamics of tau in CM and immunocytochemistry strongly suggest that the accumulation of tau is due to defective tau degradation in the lysosomal compartment in the muscle. This observation may offer a new view on the formation of paired helical filaments in Alzheimer's disease: this selective protein degradation pathway may be defective and result in intracellular accumulation of tau, thereby forming the unusual filaments.
Url:
DOI: 10.1016/S0168-0102(98)00020-0
Affiliations:
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The dynamics of tau in CM and immunocytochemistry strongly suggest that the accumulation of tau is due to defective tau degradation in the lysosomal compartment in the muscle. This observation may offer a new view on the formation of paired helical filaments in Alzheimer's disease: this selective protein degradation pathway may be defective and result in intracellular accumulation of tau, thereby forming the unusual filaments.</div></front></TEI><affiliations><list><country><li>Japon</li><li>Nouvelle-Zélande</li></country><region><li>Région de Kantō</li></region><settlement><li>Tokyo</li></settlement><orgName><li>Université de Tokyo</li></orgName></list><tree><country name="Japon"><region name="Région de Kantō"><name sortKey="Oyama, Fumitaka" sort="Oyama, Fumitaka" uniqKey="Oyama F" first="Fumitaka" last="Oyama">Fumitaka Oyama</name></region><name sortKey="Ihara, Yasuo" sort="Ihara, Yasuo" uniqKey="Ihara Y" first="Yasuo" last="Ihara">Yasuo Ihara</name><name sortKey="Ihara, Yasuo" sort="Ihara, Yasuo" uniqKey="Ihara Y" first="Yasuo" last="Ihara">Yasuo Ihara</name><name sortKey="Ihara, Yasuo" sort="Ihara, Yasuo" uniqKey="Ihara Y" first="Yasuo" last="Ihara">Yasuo Ihara</name><name sortKey="Murakami, Nobuyuki" sort="Murakami, Nobuyuki" uniqKey="Murakami N" first="Nobuyuki" last="Murakami">Nobuyuki Murakami</name></country><country name="Nouvelle-Zélande"><noRegion><name sortKey="Murakami, Nobuyuki" sort="Murakami, Nobuyuki" uniqKey="Murakami N" first="Nobuyuki" last="Murakami">Nobuyuki Murakami</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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