Changes in myosin heavy-chain isoform synthesis of chronically stimulated rat fast-twitch muscle.
Changes in myosin heavy-chain isoform synthesis of chronically stimulated rat fast-twitch muscle.
复制标题
长期刺激大鼠快肌的肌球蛋白重链亚型合成的变化。
DOI:
10.1111/j.1432-1033.1992.tb16669.x
复制
发表时间:
1992
期刊:
影响因子:
--
通讯作者:
D. Pette
中科院分区:
文献类型:
--
作者:
A. Termin;D. Pette
Chronic low-frequency stimulation was used for studying the adaptive potential of rat fast-twitch muscle to increased neuromuscular activity. The sequential exchange of myosin heavy chain isoforms HCIIb with HCIId and HCIIa was studied at the translational level using an in-vivo-labeling technique with [35S]methionine. Alterations in heavy chain isoform synthesis, i.e. a decrease in the labeling of HCIIb concomitant with an enhanced labeling of HCIId/IIa, were detectable already two days after the onset of stimulation. This time course corresponds to the previously observed alterations in the amounts of HCIIb and HCIIa mRNAs. However, significant changes in the relative protein amounts of HCIIb and HCIId/IIa were recorded only after an 8-day stimulation period. This delay at the protein level was interpreted to relate to the slow turnover of HCIIb which was estimated from its decay in long-term stimulated muscles with an approximate value of 14.7 days. Therefore, protein degradation seems to be an important post-translational regulatory step in the remodeling process of the thick filament.
DOI:
10.1016/s0021-9258(18)77444-9
发表时间:
1990-08
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
B. Kirschbaum;H. Kucher;A. Termin;A. Kelly;D. Pette
通讯作者:
B. Kirschbaum;H. Kucher;A. Termin;A. Kelly;D. Pette