The State of Actin in Activated Human Platelets
- 1 May 1981
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 116 (2) , 293-296
- https://doi.org/10.1111/j.1432-1033.1981.tb05332.x
Abstract
The state of platelet actin was determined using a fluorescent method of DNase I inhibition. Activation of human platelets resulted in mobilization of DNase-available actin. When platelets were activated with ADP the change in the state of actin was gradual and preceded the secretion. When thrombin was used as an activator, a sharp and rapid decrease in the DNase-available actin was observed which paralleled the secretion. Inhibition of ADP-induced aggregation (and secretion) by EDTA resulted in a decrease in the rate of change on actin. Inhibition of the thrombin-induced aggregation (but not secretion) by EDTA did not affect the change in the state of actin.This publication has 12 references indexed in Scilit:
- Reorganization of actin in platelets stimulated by thrombin as measured by the DNase I inhibition assay.Proceedings of the National Academy of Sciences, 1979
- Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease ICell, 1978
- Platelet actin: Sub‐cellular distribution and association with profilinFEBS Letters, 1978
- Human platelets contain profilin, a potential regulator of actin polymerisabilityFEBS Letters, 1978
- Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cellsJournal of Molecular Biology, 1977
- Depolymerization of F-actin by deoxyribonuclease ICell, 1976
- A Specific 1:1 G‐actin: DNAase I complex formed by the action of DNAase I on F‐actinFEBS Letters, 1975
- Platelet 5-HT uptake and release stopped rapidly by formaldehydeNature, 1975
- Ultrastructure of Thrombosthenin, the Contractile Protein of Human Blood PlateletsScience, 1967