Triadins are not triad-specific proteins: two new skeletal muscle triadins possibly involved in the architecture of sarcoplasmic reticulum.
2005
Vassilopoulos, Stéphane | Thevenon, Dominique | Rezgui, Sophia Smida | Brocard, Julie | Chapel, Agnès | Lacampagne, Alain | Lunardi, Joël | de Waard, Michel | Marty, Isabelle | 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) | Département réponse et dynamique cellulaire (DRDC) ; Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS) | Physiopathologie cardiovasculaire ; Université Montpellier 1 (UM1)-IFR3 ; Université Montpellier 1 (UM1)-Institut National de la Santé et de la Recherche Médicale (INSERM) | Hôpital Arnaud de Villeneuve [CHU Montpellier] ; Centre Hospitalier Régional Universitaire [Montpellier] (CHRU Montpellier) | Association Française contre les Myopathies; GIS-Institut des Maladies Rares; INSERM; CEA; French Ministry of Research
International audience
اظهر المزيد [+] اقل [-]إنجليزي. We have cloned two new triadin isoforms from rat skeletal muscle, Trisk 49 and Trisk 32, which were named according to their theoretical molecular masses (49 and 32 kDa, respectively). Specific antibodies directed against each protein were produced to characterize both new triadins. Both are expressed in adult rat skeletal muscle, and their expression in slow twitch muscle is lower than that in fast twitch muscle. Using double immunofluorescent labeling, the localization of these two triadins was studied in comparison to well-characterized proteins such as ryanodine receptor, calsequestrin, desmin, Ca(2+)-ATPase, and titin. None of these two triadins are localized within the rat skeletal muscle triad. Both are instead found in different parts of the longitudinal sarcoplasmic reticulum. We attempted to identify partners for each isoform: neither is associated with ryanodine receptor; Trisk 49 could be associated with titin or another sarcomeric protein; and Trisk 32 could be associated with IP(3) receptor. These results open further fields of research concerning the functions of these two proteins; in particular, they could be involved in the set up and maintenance of a precise sarcoplasmic reticulum structure.
اظهر المزيد [+] اقل [-]الكلمات المفتاحية الخاصة بالمكنز الزراعي (أجروفوك)
المعلومات البيبليوغرافية
تم تزويد هذا السجل من قبل Institut national de la recherche agronomique