Structural and functional comparison of a 22 kDa protein from internal human platelet membranes with cardiac...

We have shown that a platelet 22 kDa phosphoprotein is similar to the cardiac regulator phospholamban, in that both are phosphorylated by cAMP- and calmodulin-dependent protein kinases, and that both can be phosphorylated simultaneously by these two classes of protein kinases to yield an additive stimulation of the respective Ca2+ pumps (Adunyah, S.E. and Dean, W.L. (1987) Biochim. Biophys. Acta 930, 401-409). However, whereas phosphorylation of phospholamban increases the affinity of the cardiac Ca2+-ATPase for Ca2+, phosphorylation of the platelet 22 kDa protein increased the Vmax of the pump. In addition, antibodies raised against canine phospholamban did not crossreact with the human platelet 22 kDa protein. Finally, it was not possible to dissociate the platelet protein into lower-molecular-weight subunits by boiling in sodium dodecylsulfate which is characteristic of cardiac phospholamban. These results show that although phosphorylation of low-molecular-weight membrane-associated regulator proteins in cardiac muscle and platelets appears to stimulate the respective Ca2+ pumps, these proteins have different chemical and physical properties.