Tau expression in denervated rat muscles
Identifieur interne : 002636 ( Main/Exploration ); précédent : 002635; suivant : 002637Tau expression in denervated rat muscles
Auteurs : Shin-Ichiro Nagao [Japon] ; Toshihide Kumamoto [Japon] ; Tomoko Masuda [Japon] ; Hidetsugu Ueyama [Japon] ; Itaru Toyoshima [Japon] ; Tomiyasu Tsuda [Japon]Source :
- Muscle & Nerve [ 0148-639X ] ; 1999-01.
English descriptors
- Teeft :
- Alkaline phosphatase, Alkaline phosphatase treatment, Autophagic, Autophagic vacuoles, Chloroquine, Chloroquine treatment, Degraded, Denervated, Denervated muscle, Denervated muscles, Denervated soleus muscles, Denervation, Diphosphopyridine nucleotide dehydrogenase, Helical filaments, Immunoblotting, Innervated, Innervated muscles, January, Lysosomal, Lysosomal system, Microtubule, Muscle fibers, Muscle nerve, Muscle nerve january, Myofibrillar, Myofibrillar fraction, Myofibrillar fractions, Neurofibrillary tangles, Normal muscle, Phosphatase, Phosphorylated, Positive reaction, Proc natl acad, Rimmed vacuoles, Room temperature, Sarcoplasm, Sarcoplasmic, Scanning densitometry, Skeletal muscle, Skeletal muscles, Soleus, Soleus muscles, Soluble sarcoplasmic fraction, Soluble sarcoplasmic fractions, Tubulin, Vacuole, Western blot analysis.
Abstract
We studied whether denervation affects the expression of tau, in particular phosphorylated tau, and how it is degraded in rat soleus muscles. Immunoblot analysis showed a high molecular weight, approximately 110 kDa (big tau), in normal muscle. Tau levels increased significantly in denervated muscles treated with chloroquine (a lysosomotrophic agent) and in untreated ones, as compared to levels of similarly treated contralateral, innervated muscles. Most of the tau in the innervated and denervated muscles was phosphorylated. Immunohistochemically, tau and β‐tubulin colocated in the sarcoplasm of innervated, saline‐treated (intact) muscle, but the staining intensities were very weak. Both proteins, however, were expressed extensively in these areas in the denervated muscles from saline‐treated rats. In the denervated muscle of chloroquine‐treated rats there were numerous autophagic vacuoles in the sarcoplasm, and phosphorylated‐tau accumulation was marked within these vacuoles, indicative that tau first was taken into autophagic, vacuoles by nonselective autophagy then degraded via the lysosomal as well as the nonlysosomal calpain system. Our findings suggest that phosphorylated big tau accumulates with β‐tubulin in denervated muscular atrophy, possibly in order to maintain or preserve the integrity of the muscle fiber during progressive atrophy or regeneration. © 1999 John Wiley & Sons, Inc. Muscle Nerve 22: 61–70, 1999
Url:
DOI: 10.1002/(SICI)1097-4598(199901)22:1<61::AID-MUS10>3.0.CO;2-Y
Affiliations:
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wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Correspondence address: Third Department of Internal Medicine, Oita Medical University, Hasama 1‐1, Oita 879‐5593</wicri:regionArea><wicri:noRegion>Oita 879‐5593</wicri:noRegion></affiliation></author><author><name sortKey="Masuda, Tomoko" sort="Masuda, Tomoko" uniqKey="Masuda T" first="Tomoko" last="Masuda">Tomoko Masuda</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Third Department of Internal Medicine, Oita Medical University, Hasama 1‐1, Oita 879‐5593</wicri:regionArea><wicri:noRegion>Oita 879‐5593</wicri:noRegion></affiliation></author><author><name sortKey="Ueyama, Hidetsugu" sort="Ueyama, Hidetsugu" uniqKey="Ueyama H" first="Hidetsugu" last="Ueyama">Hidetsugu Ueyama</name><affiliation wicri:level="1"><country xml:lang="fr">Japon</country><wicri:regionArea>Third Department of Internal Medicine, Oita Medical University, Hasama 1‐1, Oita 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AND NERVE</title><idno type="ISSN">0148-639X</idno><idno type="eISSN">1097-4598</idno><imprint><biblScope unit="vol">22</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="61">61</biblScope><biblScope unit="page" to="70">70</biblScope><biblScope unit="page-count">10</biblScope><publisher>John Wiley & Sons, Inc.</publisher><pubPlace>New York</pubPlace><date type="published" when="1999-01">1999-01</date></imprint><idno type="ISSN">0148-639X</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0148-639X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Alkaline phosphatase</term><term>Alkaline phosphatase treatment</term><term>Autophagic</term><term>Autophagic vacuoles</term><term>Chloroquine</term><term>Chloroquine treatment</term><term>Degraded</term><term>Denervated</term><term>Denervated muscle</term><term>Denervated muscles</term><term>Denervated soleus muscles</term><term>Denervation</term><term>Diphosphopyridine nucleotide dehydrogenase</term><term>Helical filaments</term><term>Immunoblotting</term><term>Innervated</term><term>Innervated muscles</term><term>January</term><term>Lysosomal</term><term>Lysosomal system</term><term>Microtubule</term><term>Muscle fibers</term><term>Muscle nerve</term><term>Muscle nerve january</term><term>Myofibrillar</term><term>Myofibrillar fraction</term><term>Myofibrillar fractions</term><term>Neurofibrillary tangles</term><term>Normal muscle</term><term>Phosphatase</term><term>Phosphorylated</term><term>Positive reaction</term><term>Proc natl acad</term><term>Rimmed vacuoles</term><term>Room temperature</term><term>Sarcoplasm</term><term>Sarcoplasmic</term><term>Scanning densitometry</term><term>Skeletal muscle</term><term>Skeletal muscles</term><term>Soleus</term><term>Soleus muscles</term><term>Soluble sarcoplasmic fraction</term><term>Soluble sarcoplasmic fractions</term><term>Tubulin</term><term>Vacuole</term><term>Western blot analysis</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We studied whether denervation affects the expression of tau, in particular phosphorylated tau, and how it is degraded in rat soleus muscles. Immunoblot analysis showed a high molecular weight, approximately 110 kDa (big tau), in normal muscle. Tau levels increased significantly in denervated muscles treated with chloroquine (a lysosomotrophic agent) and in untreated ones, as compared to levels of similarly treated contralateral, innervated muscles. Most of the tau in the innervated and denervated muscles was phosphorylated. Immunohistochemically, tau and β‐tubulin colocated in the sarcoplasm of innervated, saline‐treated (intact) muscle, but the staining intensities were very weak. Both proteins, however, were expressed extensively in these areas in the denervated muscles from saline‐treated rats. In the denervated muscle of chloroquine‐treated rats there were numerous autophagic vacuoles in the sarcoplasm, and phosphorylated‐tau accumulation was marked within these vacuoles, indicative that tau first was taken into autophagic, vacuoles by nonselective autophagy then degraded via the lysosomal as well as the nonlysosomal calpain system. Our findings suggest that phosphorylated big tau accumulates with β‐tubulin in denervated muscular atrophy, possibly in order to maintain or preserve the integrity of the muscle fiber during progressive atrophy or regeneration. © 1999 John Wiley & Sons, Inc. Muscle Nerve 22: 61–70, 1999</div></front></TEI><affiliations><list><country><li>Japon</li></country></list><tree><country name="Japon"><noRegion><name sortKey="Nagao, Shin Chiro" sort="Nagao, Shin Chiro" uniqKey="Nagao S" first="Shin-Ichiro" last="Nagao">Shin-Ichiro Nagao</name></noRegion><name sortKey="Kumamoto, Toshihide" sort="Kumamoto, Toshihide" uniqKey="Kumamoto T" first="Toshihide" last="Kumamoto">Toshihide Kumamoto</name><name sortKey="Kumamoto, Toshihide" sort="Kumamoto, Toshihide" uniqKey="Kumamoto T" first="Toshihide" last="Kumamoto">Toshihide Kumamoto</name><name sortKey="Masuda, Tomoko" sort="Masuda, Tomoko" uniqKey="Masuda T" first="Tomoko" last="Masuda">Tomoko Masuda</name><name sortKey="Toyoshima, Itaru" sort="Toyoshima, Itaru" uniqKey="Toyoshima I" first="Itaru" last="Toyoshima">Itaru Toyoshima</name><name sortKey="Tsuda, Tomiyasu" sort="Tsuda, Tomiyasu" uniqKey="Tsuda T" first="Tomiyasu" last="Tsuda">Tomiyasu Tsuda</name><name sortKey="Ueyama, Hidetsugu" sort="Ueyama, Hidetsugu" uniqKey="Ueyama H" first="Hidetsugu" last="Ueyama">Hidetsugu Ueyama</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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