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The purpose of editorial this study is to identify the molecular mechanisms utilized during seasonal changes that allow cardiac function. Two of the specific strategies under investigation are the roles of protein phosphorylation, due to ß-adrenergic stimulation, and the editorial expression of alternate protein isoforms better suited to function under the physiological conditions. Thermal acclimation of a number of species, including trout, goldfish and killifish will be used to determine how the functional properties of the cardiac trabeculae respond to such manipulation. Two-dimensional gels and mass spectrometry are used to characterize both the phosphorylation state of the contractile proteins and editorial the protein isoforms expressed in the hearts. In vitro phosphorylation of the Tn complex, prior to exchange into the trabeculae, and/or the use of site directed mutagenesis to mimic phosphorylation of specific residues will also used to establish the role phosphorylation may play in maintaining function at different temperatures.
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