Davies G E
Biochim Biophys Acta. 1984 May 16;772(2):149-60. doi: 10.1016/0005-2736(84)90038-5.
Human platelet membrane-actin associations were studied by means of differential extraction of purified membranes and low-shear viscometry of membrane-F-actin mixtures. As indicated by resistance to extraction with 0.6 M potassium iodide, a significant amount of platelet actin appears to be tightly associated with the membrane. When tested by falling-ball viscometry, both whole and KI-extracted membranes increased the low-shear viscosity of preformed rabbit skeletal muscle F-actin at physiologically reasonable pH and ionic conditions. This membrane-associated actin gelation activity was dependent upon low free calcium concentration (10(-8)-10(-7) M). The results are consistent with specific associations between actin and platelet membranes and may be relevant to membrane-cytoskeletal interactions believed to occur in the intact cell.
