Triadin (Trisk 95) overexpression blocks excitation-contraction coupling in rat skeletal myotubes
| Autor: | Isabelle Marty, Stéphane Vassilopoulos, Jean Claude Platel, Michel De Waard, Alexandre Bouron, Sarah Oddoux, Christophe Arnoult, Luis Garcia, Julie Brocard, Sophia Smida Rezgui |
|---|---|
| Přispěvatelé: | Canaux calciques , fonctions et pathologies, Université Joseph Fourier - Grenoble 1 (UJF)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM), Généthon, Association Française contre les Myopathies (AFM), GIS-Institut des Maladies Rares, INSERM, CEA, French ministry of research, Roux-Buisson, Nathalie |
| Jazyk: | angličtina |
| Rok vydání: | 2005 |
| Předmět: |
MESH: Muscle Contraction
Muscle Fibers Skeletal Gene Expression Muscle Proteins [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC] Biochemistry Membrane Potentials MESH: Ryanodine Receptor Calcium Release Channel 0302 clinical medicine MESH: Animals Cells Cultured Calcium signaling 0303 health sciences MESH: Calcium Channels L-Type MESH: Muscle Fibers Skeletal MESH: Electrophysiology Myogenesis Ryanodine receptor Dihydropyridine Intracellular Signaling Peptides and Proteins Cell biology Electrophysiology medicine.anatomical_structure medicine.symptom medicine.drug Muscle contraction Muscle Contraction MESH: Cells Cultured medicine.medical_specialty MESH: Gene Expression Calcium Channels L-Type MESH: Rats chemistry.chemical_element MESH: Carrier Proteins Calcium Biology Transfection MESH: Calcium Signaling Article 03 medical and health sciences MESH: Muscle Proteins Internal medicine [SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular Biology [SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC] medicine Animals MESH: Membrane Potentials [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Calcium Signaling Molecular Biology 030304 developmental biology MESH: Transfection Skeletal muscle Ryanodine Receptor Calcium Release Channel Cell Biology MESH: Multiprotein Complexes Rats Endocrinology chemistry Triadin Multiprotein Complexes Carrier Proteins 030217 neurology & neurosurgery |
| Zdroj: | Journal of Biological Chemistry Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2005, 280 (47), pp.39302-8. ⟨10.1074/jbc.M506566200⟩ Journal of Biological Chemistry, 2005, 280 (47), pp.39302-8. ⟨10.1074/jbc.M506566200⟩ |
| ISSN: | 0021-9258 1083-351X |
| DOI: | 10.1074/jbc.M506566200⟩ |
| Popis: | International audience; To identify the function of triadin in skeletal muscle, adenovirus-mediated overexpression of Trisk 95 or Trisk 51, the two major skeletal muscle isoforms, was induced in rat skeletal muscle primary cultures, and the physiological behavior of the modified cells was analyzed. Overexpression did not modify the expression level of their protein partners ryanodine receptor, dihydropyridine receptor, and the other triadin. Caffeine-induced calcium release was also unaffected by triadin overexpression. Nevertheless, in the absence of extracellular calcium, depolarization-induced calcium release was almost abolished in Trisk 95 overexpressing myotubes (T95 myotubes), and not modified in Trisk 51 overexpressing myotubes (T51 myotubes). This was not because of a modification of dihydropyridine receptors, as depolarization in presence of external calcium still induced a calcium release, and the activation curve of dihydropyridine receptor was unchanged, in both T95 and T51 myotubes. The calcium release complex was also maintained in T95 myotubes as Trisk 95, ryanodine receptor, dihydropyridine receptor, and Trisk 51 were still co-localized. The effect of Trisk 95 overexpression on depolarization-induced calcium release was reversed by a simultaneous infection with an antisense Trisk 95 adenovirus, indicating the specificity of this effect. Thus, the level of Trisk 95 and not Trisk 51 is important on regulating the calcium release complex, and an excess of this protein can lead to an inhibition of the physiological function of the complex. |
| Databáze: | OpenAIRE |
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