Reversible association of myosin with the platelet cytoskeleton

Details Reversible association of myosin with the platelet cytoskeleton Reversible association of myosin with the platelet cytoskeleton

Jan 1985

adsabs.harvard.edu/cgi-bin/nph-data_query?bibcode=1985natur.313...70n&link_type=abstract

Nature, Volume 313, Issue 5997, pp. 70-72 (1985).

Physics

Scientific paper

Platelets circulating in the human blood stream are smooth disk-shaped structures. The disks change within seconds of exposure to ADP or thrombin to irregular spheres bearing filopodia and pseudopodia. It is well-established that platelets also change shape (although more slowly) when chilled to 5°C1-5 and revert to disks on rewarming1,3. This cold-induced shape change may be due to the depolymerization of the submembranous microtubule ring. However, we found that chilling in the presence of Taxol, which stabilizes the microtubules, still results in shape change. Chilled platelets show an increase in the amount of myosin in the Triton-X insoluble residue or `cytoskeleton'6-9 which is correlated in time both with phosphorylation of the myosin regulatory light chain and with the induced shape change. We suggest here that the slow cold-induced change from disks to spheres is due primarily to a gradual activation of myosin.

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