caa a22 4500 475744772 CHVBK 20180406123510.0 cr unu---uuuuu 170329e20000801xx s 000 0 eng 10.1023/A:1026542303629 doi (NATIONALLICENCE)springer-10.1023/A:1026542303629 Myostatin levels in regenerating rat muscles and in myogenic cell cultures [Elektronische Daten] [Luca Mendler, Ernö Zádor, Mark Heyen, László Dux, Frank Wuytack] Myostatin is a newly described member of the TGF-β superfamily acting as a secreted negative regulator of skeletal muscle mass in several species, but whose mode of action remains largely unknown. In the present work, we followed the myostatin mRNA and protein levels in rat soleus and extensor digitorum longus (EDL) muscles regenerating in vivo from notexin-induced necrosis, and the myostatin transcript levels in two different in vitro myogenic differentiation models: i.e. in mouse BC3H1 and C2C12 cultured cells. The in vivo regenerating rat skeletal muscles showed a characteristic time-dependent expression of myostatin mRNA. After notexin injection, the transcript levels dropped below the detection limit on day 1 in soleus and close to the detection limit on day 3 in EDL, then increased to a maximum on day 7 in soleus and after 28 days finally reached the control values in both types of muscles. In contrast, the myostatin protein levels increased dramatically on the first days of regeneration in both muscles, i.e. at the time when its transcript level was low. Later on the myostatin protein level gradually declined to normal in soleus while in EDL it stayed high some days longer and decreased to normal on days 21-28. In vitro proliferating myoblasts produced low level of myostatin mRNA, which increased upon induction of differentiation suggesting that functional innervation is no prerequisite for myostatin expression. Myostatin production in vitro seems not to be dependent on myocyte fusion either, since it is observed in differentiated BC3H1 cells, which are defective in myofiber formation. Kluwer Academic Publishers, 2000 Mendler Luca Institute of Biochemistry, Faculty of Medicine, University of Szeged, Dóm tér 9, P.O. Box 415, H-6701, Szeged, Hungary aut Zádor Ernö Institute of Biochemistry, Faculty of Medicine, University of Szeged, Dóm tér 9, P.O. Box 415, H-6701, Szeged, Hungary aut Heyen Mark Laboratorium voor Fysiologie, Katholieke Universiteit Leuven, Campus Gasthuisberg, B-3000, Leuven, Belgium aut Dux László Institute of Biochemistry, Faculty of Medicine, University of Szeged, Dóm tér 9, P.O. Box 415, H-6701, Szeged, Hungary aut Wuytack Frank Laboratorium voor Fysiologie, Katholieke Universiteit Leuven, Campus Gasthuisberg, B-3000, Leuven, Belgium aut Journal of Muscle Research & Cell Motility Kluwer Academic Publishers 21/6(2000-08-01), 551-563 0142-4319 21:6<551 2000 21 10974 https://doi.org/10.1023/A:1026542303629 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1026542303629 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Mendler Luca Institute of Biochemistry, Faculty of Medicine, University of Szeged, Dóm tér 9, P.O. Box 415, H-6701, Szeged, Hungary aut NATIONALLICENCE 700 1- Zádor Ernö Institute of Biochemistry, Faculty of Medicine, University of Szeged, Dóm tér 9, P.O. Box 415, H-6701, Szeged, Hungary aut NATIONALLICENCE 700 1- Heyen Mark Laboratorium voor Fysiologie, Katholieke Universiteit Leuven, Campus Gasthuisberg, B-3000, Leuven, Belgium aut NATIONALLICENCE 700 1- Dux László Institute of Biochemistry, Faculty of Medicine, University of Szeged, Dóm tér 9, P.O. Box 415, H-6701, Szeged, Hungary aut NATIONALLICENCE 700 1- Wuytack Frank Laboratorium voor Fysiologie, Katholieke Universiteit Leuven, Campus Gasthuisberg, B-3000, Leuven, Belgium aut NATIONALLICENCE 773 0- Journal of Muscle Research & Cell Motility Kluwer Academic Publishers 21/6(2000-08-01), 551-563 0142-4319 21:6<551 2000 21 10974 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer