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Perchlorate and the relationship between charge movement and contractile activation in frog skeletal muscle fibres.
Author(s) -
Csernoch L,
Kovács L,
Szücs G
Publication year - 1987
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.1987.sp016695
Subject(s) - chemistry , perchlorate , biophysics , skeletal muscle , rheobase , grenouille , membrane potential , ion , anatomy , biochemistry , biology , organic chemistry , xenopus , salientia , gene
1. The effects of perchlorate ions (1‐8 mM) on intramembrane charge movement, myoplasmic Antipyrylazo III Ca2+ transients and contractile activation were examined in voltage‐clamped cut skeletal muscle fibres of the frog. 2. Perchlorate shifted both the voltage dependence of charge movement and the rheobase of the strength‐duration relation for contraction threshold towards more negative membrane potentials. 3. Both charge movements and myoplasmic Ca2+ transients were much slower at the new rheobase in the presence of perchlorate than in the control solution but there was no change in the threshold amount of charge or in the calculated peak binding of Ca2+ to troponin C. 4. The peak release rate had a steeper voltage dependence than the non‐linear charge, but a lower concentration (2 mM) of perchlorate shifted both voltage dependences equally without altering the maxima in the amount of charge and in the rate of Ca2+ release. 5. The voltage dependence of the difference between total charge and charge at the threshold of Ca2+ transients agreed well with the voltage dependence of the rate of Ca2+ release in both the presence and absence of perchlorate. 6. It is concluded that the effect of perchlorate on contractile activation can be accounted for by its action on the intramembrane charge movement responsible for contraction, without significant effects on subsequent Ca2+ release from the sarcoplasmic reticulum or on Ca2+ binding to regulatory sites of troponin C.