Key result
A trace amount of caldesmon significantly increased precipitations and intrinsic tryptophan fluorescence intensity of myosin compared to base controls (P < 0.01).
p-value: p=<0.01
A trace amount of caldesmon can efficiently interact with myosin, though its in vivo significance requires further investigation.
Supports trace caldesmon-myosin interaction in vitro; leaves open in vivo cardiac relevance pending further study.
Caldesmon (CaD) is known as an actin binding protein. In this study, we proposed that a trace amount of caldesmon (TACD) could highly, efficiently, interact with myosin by producing a 'domino-like cascade' and characterized that TACD (lowest caldesmon/myosin molar ratio: 1/10,000) significantly increased precipitations and intrinsic tryptophan fluorescence intensity of myosin in both phosphorylated and unphosphorylated states compared to the base controls (P < 0.01). Actin-blocked TACD-myosin interaction, suggesting that it functioned as a negative regulator. Since CaD is not an enzyme, the in vivo significance of the highly efficient TACD-myosin interaction needs further investigation.
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Zhang et al. (2011) studied this question. Trace amount of caldesmon (TACD) vs. Base controls was evaluated on Precipitations and intrinsic tryptophan fluorescence intensity of myosin (p=<0.01). A trace amount of caldesmon significantly increased precipitations and intrinsic tryptophan fluorescence intensity of myosin compared to base controls (P < 0.01).
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