Opposite effects of cooling on twitch contractions of skeletal muscle isolated from tropical toads (Leptodactylidae) and northern frogs (Ranidae)

• Published in: Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology Vol. 168; no. 8; pp. 600 - 610
• Main Authors: Caputo, C, Gerday, C, Lopez, J R, Taylor, S R, Bolaños, P
• Format: Journal Article
• Language: English
• Published: Germany 01.12.1998
• Subjects: Animals; Anura - physiology; Caffeine - pharmacology; Calcium - physiology; Cold Temperature; Electric Stimulation - methods; Electrophysiology; In Vitro Techniques; Membranes - physiology; Microscopy, Electron; Muscle Contraction - physiology; Muscle, Skeletal - drug effects; Muscle, Skeletal - physiology; Muscle, Skeletal - ultrastructure; Potassium - pharmacology; Rana pipiens - physiology; Rana temporaria - physiology; Ranidae - physiology; Rest
• ISSN: 0174-1578; 1432-136X
• DOI: 10.1007/s003600050182

Cooling increases the twitch force of frog skeletal muscle (Rana temporaria; Rana pipiens), but decreases the twitch force of tropical toad muscle (Leptodactylus insularis). Action potentials and intramembranous charge movement in frog and toad fibers were slowed identically by cooling. Cooling increased the integral of twitch Ca2+ detected by aequorin in frog fibers (1.4-fold), while also decreasing the peak and slowing the rate of decay. Conversely, cooling decreased the integral (0.6-fold) and the peak of twitch Ca2+ in toad fibers, without affecting the rate of decay. The difference in entire Ca2+ transients may account for cold-induced twitch potentiation in frogs and twitch paralysis in toads. In sustained contractions of toad fibers, cooling markedly decreased maximum force caused by: (i) tetanic stimulation, (ii) two-microelectrode voltage clamp steps, (iii) high [K+], or (iv) caffeine. Maximum force in sustained contractions was decreased moderately by cooling frog fibers. Rapid rewarming and simultaneous removal of high [K+] or caffeine during a sustained contraction, caused toad muscle force to rise towards the value corresponding to the warm temperature. This did not occur after removing high [K+] or caffeine from toad fibers kept in the cold. Transmission electron micrographs showed no relevant structural differences. Parvalbumins are thought to promote relaxation of frog muscle in the cold. The unique parvalbumin isoforms in toad muscle apparently lack this property.