Effect of adrenaline on the post-tetanic potentiation in mouse skeletal muscle

Citation
V. Decostre et al., Effect of adrenaline on the post-tetanic potentiation in mouse skeletal muscle, J MUSCLE R, 21(3), 2000, pp. 247-254
Citations number
36
Categorie Soggetti
Cell & Developmental Biology
Journal title
JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
ISSN journal
01424319 → ACNP
Volume
21
Issue
3
Year of publication
2000
Pages
247 - 254
Database
ISI
SICI code
0142-4319(200004)21:3<247:EOAOTP>2.0.ZU;2-4
Abstract
We report the influence of adrenergic stimulation on the amplitude and time course of post-tetanic potentiation of twitch contraction. This was comple mented by measurements of the peak of [Ca2+](i) transients in twitches and of the level of myosin light chain 2 (LC2) phosphorylation, before, 20 and 300 s after the conditioning tetanus. Soon after the tetanus, twitch potent iation and increases of LC2 phosphorylation and of [Ca2+](i) peak were simi lar in control conditions and in the presence of adrenaline. In control con ditions, twitch potentiation, LC2 phosphorylation and [Ca2+](i) peak return ed to, or close to, pre-tetanic values in 300 s. On the contrary, in the pr esence of adrenaline, twitch potentiation and LC2 phosphorylation were part ially or fully maintained respectively, while the increase of [Ca2+](i) pea k was not. This situation allowed us to analyse the relative contributions of elevated LC2 phosphorylation and [Ca2+](i) peak in the twitch post-tetan ic potentiation phenomenon. Moreover, it was shown that the increase of LC2 phosphorylation (up to 0.5 mol P/mol LC2) affected neither the kinetic par ameters of the twitch nor the maximal velocity of shortening. It is propose d that the maintenance of LC2 phosphorylation in the presence of adrenaline results from the inhibition of myosin light chain phosphatase. This could be achieved through the production of the active, phosphorylated form of th e inhibitor-1, an endogenous inhibitor, which binds to the catalytic sub-un its common to class 1 protein phosphatases.