Involvement of ryanodine receptor in skeletal muscle fatigue
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چکیده
منابع مشابه
Ryanodine receptor purified from crayfish skeletal muscle.
The ryanodine receptor was isolated from the sarcoplasmic reticulum of crayfish skeletal muscle. Ryanodine binding to the native fraction was measured by Scatchard analysis and values of 60 nmol/l and 9 pmol/mg were obtained for KD and Bmax respectively. The identity of purified receptor was confirmed by electron microscopy, electrophoresis and incorporation into planar lipid bilayers. At least...
متن کاملA Skeletal Muscle Ryanodine Receptor Interaction Domain in Triadin
Excitation-contraction coupling in skeletal muscle depends, in part, on a functional interaction between the ligand-gated ryanodine receptor (RyR1) and integral membrane protein Trisk 95, localized to the sarcoplasmic reticulum membrane. Various domains on Trisk 95 can associate with RyR1, yet the domain responsible for regulating RyR1 activity has remained elusive. We explored the hypothesis t...
متن کاملRyanodine receptor isoforms of non-Mammalian skeletal muscle.
Whereas mammalian skeletal muscles express primarily a single isoform of ryanodine receptor (RyR) as the Ca2+ releasing channel, many non-mammalian vertebrate skeletal muscles express two isoforms in almost similar amount, alpha- and beta-RyR which are homologues of mammalian isoforms RyR1 and 3, respectively. alpha-RyR is believed to be directly involved in excitation-contraction coupling in s...
متن کاملFunctional Impact of the Ryanodine Receptor on the Skeletal Muscle
L-type Ca 2 1 channel (L-channel) activity of the skeletal muscle dihydropyridine receptor is markedly enhanced by the skeletal muscle isoform of the ryanodine receptor (RyR1) (Nakai, J., R.T. Dirksen, H.T. Nguyen, I.N. Pessah, K.G. Beam, and P.D. Allen. 1996. Nature. 380:72–75.). However, the dependence of the biophysical and pharmacological properties of skeletal L-current on RyR1 has yet to ...
متن کاملStructural determinants of skeletal muscle ryanodine receptor gating.
Ryanodine receptor type 1 (RyR1) releases Ca(2+) from intracellular stores upon nerve impulse to trigger skeletal muscle contraction. Effector binding at the cytoplasmic domain tightly controls gating of the pore domain of RyR1 to release Ca(2+). However, the molecular mechanism that links effector binding to channel gating is unknown due to lack of structural data. Here, we used a combination ...
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ژورنال
عنوان ژورنال: Japanese Journal of Physical Fitness and Sports Medicine
سال: 2018
ISSN: 0039-906X,1881-4751
DOI: 10.7600/jspfsm.67.207