Molecular cell pharmacology on Novel calcium signaling

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The calcium signal is transmitted into the intracellular response in part via families of calcium-binding proteins which are thought to regulate a variety of biological processes. These calcium-binding protein families become of major interest because of their different expression in each disease. But it has not been reported about relation disease to S100C we first purified. we already cloned cDNA for S100C and decided the first structure of S100C.So we studied about physiological, pharmacological and pathological roles of S100C in diseases.The cardioprotective effect of propranolol is now believed to be independent on its BETA-blocking effect and exert through the direct interaction wuth cardiac muscle, but the pathway of its action remains unclear. We found that S100C bound to propranolol and that the concentrations of propranolol for binding with S100C was similar in which propranolol was reported to exert cardioprotective effects. The concentration of propranolol was lower than those to need to interact with other calcium-binding proteins, such as calmodulin or troponin c. It sugested that S100C might be intracellular target molecule of propranolol and share other actions than B-blockade action. we also found that the gene expression of S100C was changed in the heart of myocardial infarction model rats compared with normal rats. Theses results sugest that S100C might have an important role in heart disease. And we demonstrated that S100L was a novel selective eosinophilic chemotactic factor, and had a most potent chemotactic activity on guinea pig eosinophils of all the chemotactic proteins. C.W.Heizmann found differential expression of S100L in tumor cells and normal cells and we found cell-cycle dependent differential gene expression of S100C.Thus, S100C and S100L might be thought to play an important role in many diseases.