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PubMed · 6437697

Protein changes in activated human platelets.

C S Giometti·N G Anderson
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Abstract

Using two-dimensional electrophoresis, we mapped both the total and the cytoskeletal proteins of human platelets before and after activation with thrombin or the calcium ionophore A23187. Activation resulted in increased abundance of the phosphorylated form of myosin light chains with an approximate molecular mass of 20 kDa, decreased abundance of two proteins with molecular masses of approximately 18 and 25 kDa, and, in the case of activation with thrombin, the appearance of a new chain of protein spots (named "Thromb:1"). The latter, found associated with isolated detergent-insoluble cytoskeletons, reacted with antibody to human fibrinogen and thus were identified as gamma-gamma dimers of fibrin. The total number of proteins associated with the cytoskeleton increased after activation with either thrombin or A23187, but we observed some differences in which proteins were bound, and for how long.

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Blood PlateletsBlood ProteinsCalcimycinCytoskeletal ProteinsCytoskeletonElectrophoresis, Polyacrylamide GelFibrinogenHumansIsoelectric FocusingMolecular WeightMyosinsThrombinJournal ArticleResearch Support, U.S. Gov't, Non-P.H.S.

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C S Giometti, N G Anderson. 1984. Protein changes in activated human platelets.. https://pubmed.ncbi.nlm.nih.gov/6437697/

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