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February 3, 2007The Journal of PhysiologyOpen Access

Regulation and function of Ca2+–calmodulin‐dependent protein kinase II of fast‐twitch rat skeletal muscle

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Key result

CaMKII inhibition during ex vivo contraction of fast-twitch rat skeletal muscle resulted in greater fatigue and blunted phosphorylation of trisk95.

Population

Fast-twitch rat skeletal muscle (gastrocnemius muscle)

Comparison

Muscle contractions in situ and ex vivo, with… vs Resting contralateral muscles

Design

Preclinical

Authors

ARAdam J. RoseTAThomas J. AlstedJKJ. Bjarke Kobberø

Discussion

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Overview

Highlights CaMKII's protective role against fatigue in fast-twitch fibers; leaves open translation to human exercise or cardiac muscle.

Structured PICO

P
Population
Fast-twitch rat skeletal muscle (gastrocnemius muscle)
I
Intervention
Muscle contractions in situ and ex vivo, with and without CaMKII inhibition
C
Comparator
Resting contralateral muscles
O
Outcome
CaMKII autonomous activity, phosphorylation at Thr287, and phosphorylation of trisk95/triadinsurrogate

CaMKII activation is rapid and sustained during skeletal muscle contraction and may signal through trisk95 to modulate Ca2+ release.

Cite This Study

Rose et al. (2007) studied Muscle contraction and fatigue in rat skeletal muscle. CaMKII inhibition vs. Uninhibited/control muscle was evaluated on CaMKII activity, phosphorylation, and muscle fatigue. CaMKII inhibition during ex vivo contraction of fast-twitch rat skeletal muscle resulted in greater fatigue and blunted phosphorylation of trisk95.

synapsesocial.com/papers/6a9cb58c8662eb246c417a92https://doi.org/10.1113/jphysiol.2006.127464
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