Proteins calcium-regulatory

Hasenfuss, G. 1998, Alterations of calcium-regulatory proteins in heart failure. Cardiovasc Res, 37(2), pp 279-89. 

Bigelow, D. J., and Squier, T. C. 2005. Redox modulation of cellular signaling and metabolism through reversible oxidation of methionine sensors in calcium regulatory proteins. Biochim. Biophys. Acta 1703 121-134. 

Fig. 11. Effect of in vivo aluminum exposure on calcium regulatory protein, PKC. Values are mean S.D. of 8 animals/group. P < 0.05, P < 0.001, statistically significant from control group...

In this section, properties of calcium regulatory proteins from vertebrate skeletal muscle were reviewed with particular reference to the physiological structure and function that have been the major interest since the discovery of native tropomyosin. 

Calmodulin. As mentioned in the introduction it has recently been demonstrated that calcium regulation of a number of enzyme systems and other cellular events is mediated by a low molecular weight protein termed calmodulin. There is presently good evidence that calmodulin is an ubiquitous calcium regulatory protein whose primary sequence is highly conserved throughout all eucaryotic cells(3). 

Herzberg, O., James, M.N.G. Structure of the calcium regulatory muscle protein troponin-C at 2.8 A resolution. Nature 313 653-659, 1985. 

The calcium mediated contraction of smooth muscle, which unlike striated muscle does not contain troponin, is quite different and requires a particular calcium-binding protein called calmodulin. Calmodulin (CM) is a widely distributed regulatory protein able to bind, with high affinity, four Ca2+ per protein molecule. The calcium—calmodulin (CaCM) complex associates with, and activates, regulatory proteins, usually enzymes, in many different cell types in smooth muscle the target regulatory proteins are caldesmon (CDM) and the enzyme myosin light chain kinase (MLCK). As described below, CaCM impacts on both actin and myosin filaments. 

A calcium-regulated actin regulatory protein that binds to and severs actin hlaments, thereby controlling the gel-sol transitions of the actin cytoskeleton. After severing... 

Bredt, D. S., Ferris, C. D., and Snyder, S. H. (1992). Nitric oxide synthase regulatory sites. Phosphorylation by cyclic AMP-dependent protein kinase, protein kinase C, and calcium/calmodulin protein kinase identification of flavin and calmodulin binding sites. . Biol. Chem. 267, 10976-10981. 

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