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Separable assembly of platelet pseudopodal and contractile cytoskeletons

Authors
Journal
Cell
0092-8674
Publisher
Elsevier
Publication Date
Volume
30
Issue
2
Identifiers
DOI: 10.1016/0092-8674(82)90236-7
Disciplines
  • Biology

Abstract

Abstract Unactivated platelets contain about 69% G actin and less than 10% of the contractile proteins in a cytoskeletal core resistant to extraction with 1% Triton X-100. Activation by thrombin leads, within 1 min, to the formation of pseudopodia and contractile gels, accompanied by the reduction of the Gactin content to about 22% and the development of cytoskeletal cores containing 70%–80% of the total actin and 60%–80% of the total myosin and actinbinding protein. Inhibition of pseudopodal formation by pretreatment with cytochalasin B before thrombin activation results in the loss of most of the actin-binding protein and about one third of the actin from the cytoskeletal core. Myosin incorporation and contractile gel formation are unaltered by this treatment. Conversely, activation with phorbol 12-myristate 13-acetate leads to pseudopodal but not contractile gel formation, with cytoskeletal cores containing mostly actin and actin-binding protein. These results demonstrate that there are separable cytoskeletal assembly processes in platelets for pseudopodal and contractile gel formation.

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