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Evolutionary and Physiological Variation in Cardiac Troponin C in Relation to Thermal Strategies of Fish

Striated muscle contraction is initiated when troponin C (TnC) binds Ca2+, which activates actinomyosin ATPase. We investigated (i) the variation between cardiac TnC (cTnC) primary structure within teleost fish and (ii) the pattern of TnC expression in response to temperature acclimation. There were few differences between rainbow trout (Oncorhynchus mykiss), yellowfin tuna (Thunnus albacares), yellow perch (Perca flavescens), goldfish (Carassius auratus), white sucker (Catostomus commersoni), and icefish (Chaenocephalus aceratus) in cTnC amino acid sequence. No variation existed in the regulatory Ca2+‐binding site (site 2). The site 3 and 4 substitutions were limited to residues not directly involved in Ca2+ coordination. Fish cTnC primary structure was highly conserved between species (93%–98%) and collectively divergent from the highly conserved sequence seen in birds and mammals. Northern blots and polymerase chain reaction showed that thermal acclimation of trout (3°, 18°C) did not alter the TnC isoform pattern. While cardiac and white muscle had the expected isoforms—cTnC and fast troponin C (fTnC), respectively—red muscle unexpectedly expressed primarily ftnC. Cold acclimation did not alter myofibrillar ATPase Ca2+ sensitivity, but maximal velocity increased by 60%. We found no evidence that TnC variants, arising between species or in response to thermal acclimation, play a major role in mitigating the effects of temperature on contractility of the adult fish heart.