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Articles
University of Joensuu, Faculty of Biosciences, Joensuu, Finland
Submitted March 3, 2009 ; accepted in final form August 13, 2009
Ryanodine (Ry) sensitivity of cardiac contraction differs between teleost species, between atrium and ventricle, and according to the thermal history of the fish. The hypothesis that variability in Ry sensitivity of contraction is due to species-specific, chamber-specific, and temperature-related differences in the sarcoplasmic reticulum (SR) Ca2+ content, was tested by comparing steady-state (SS) and maximal (Max) Ca2+ loads of the SR in three teleost fish, rainbow trout (Oncorhynchus mykiss), burbot (Lota lota), and crucian carp (Carassius carassius), which differ in the extent of SR contribution to excitation-contraction coupling. Fish were acclimated at 4°C (cold-acclimation, CA) or 18°C (warm-acclimation, WA), and SR Ca2+ content was released by a rapid application of 10 mM caffeine to single cardiac myocytes; its amount was determined from the Na+-Ca2+ exchange current at 18°C. SS Ca2+ load was larger in atrial (304–915 µmol/l) than ventricular (224–540 µmol/l) myocytes in all fish species (P < 0.05), and the same was true for Max SR Ca2+ content: 550–1,522 µmol/l and 438–840 µmol/l for atrial and ventricular myocytes, respectively (P < 0.05). Consistent with the hypothesis, acclimation to cold increased Ca2+ load of the cardiac SR in the burbot heart, but contrary to the hypothesis, temperature acclimation did not affect SR Ca2+ content in rainbow trout and crucian carp hearts. Furthermore, there was an inverse relation between SR Ca2+ content and Ry sensitivity of contraction force: the species with the smallest SR Ca2+ content (burbot) is most sensitive to Ry. Collectively, these findings show that SR Ca2+ content of fish cardiac myocytes is several times larger than that in mammalian cardiac SR.
excitation-contraction coupling; sarcoplasmic reticulum calcium load; caffeine; sodium-calcium exchange current
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