Species- and chamber-specific responses of 12 kDa FK506-binding protein to temperature in fish heart
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The sarcoplasmic reticulum (SR) Ca2+ release channel or ryanodine receptor (RyR) of the vertebrate heart is regulated by the FK506-binding proteins, FKBP12 and FKBP12.6. This study examines whether temperature-related changes in the SR function of fish hearts are associated with changes in FKBP12 expression. For this purpose, a polyclonal antibody against trout FKBP12 was used to compare FKPB12 expression in cold-acclimated (4 °C, CA) and warm-acclimated (18 °C, WA) rainbow trout (Oncorhynchus mykiss), burbot (Lota lota) and crucian carp (Carassius carassius) hearts. FKBP12 expression was modulated in a species- and tissue-specific manner. Temperature acclimation affected FKBP12 expression only in atrial tissue. Changes in the ventricular FKBP12 expression were not detected in any of the fish species. In the atria of rainbow trout and crucian carp, temperature acclimation produced opposite thermal responses: FKBP12 increased in the trout atrium and decreased in the crucian carp atrium under cold acclimation. In the burbot heart, chronic temperature changes did not affect cardiac FKBP12 levels. Expression of FKBP12 mRNA in rainbow trout and crucian carp hearts suggests that the transcript levels are higher in the ventricle than in the atrium and are elevated by cold acclimation in trout, but not in crucian carp. Since FKBP12 is known to increase the Ca2+ sensitivity of cardiac RyRs and thereby the opening frequency of the Ca2+ release channels, temperature-related changes in FKBP12 expression may modify the SR function in excitation–contraction coupling. The cold-induced increase in FKBP12 in the trout atrium and decrease in the crucian carp atrium are consistent with the previously noted increase and decrease, respectively, of SR Ca2+ stores in cardiac contraction in these species.
KeywordsCalcium-induced calcium release Thermal acclimation Fish heart Excitation–contraction coupling Sarcoplasmic reticulum
Skillful technical assistance of Anita Kervinen and Riitta Pietarinen is acknowledged. This research was supported by a Grant from The Academy of Finland (127192) to M.V.
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