Abstract
The deteriorating effect of microM order of Ca2+ on skinned frog skeletal muscle fibres was studied from the view point of the digestion of proteins by calcium-activated neutral protease (CANP). Tension developed in solutions containing no MgATP (rigor solution) decreased irreversibly with the addition of Ca2+ in quantities of more than 0.1 microM. Low temperature was seen to suppress (Q10 greater than 4), and neutral pH to maximize, this decrease in tension. In rigor solution containing Ca2+, SDS electrophoresis indicated that a 95 k dalton component (alpha-actinin) was released from the fibre; electron micrography showed the disappearance of Z-lines. These results suggest that one of the causes for decrease in rigor tension is the proteolytic activity of CANP, and its inhibitors were shown to be quite useful in experiments on skinned fibre.
MeSH Terms
Animals
Antipain/pharmacology
Calcium/pharmacology
Cysteine Proteinase Inhibitors/pharmacology
Dose-Response Relationship, Drug
Electrophoresis, Polyacrylamide Gel
Hydrogen-Ion Concentration
Iodoacetates/pharmacology
Iodoacetic Acid
Leucine/analogs & derivatives,pharmacology
Leupeptins/pharmacology
Microscopy, Electron
Muscle Contraction/drug effects,physiology
Muscles/drug effects,physiopathology,ultrastructure
Rana catesbeiana
Temperature
Chemicals
Cysteine Proteinase Inhibitors
Iodoacetates
Leupeptins
Antipain
Leucine
E 64
Calcium
Iodoacetic Acid
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Kasuga N
Department of Physiology, Jikei University School of Medicine, Tokyo, Japan.
Umazume Y
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21 references, click to expand
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