A platelet inhibitor protein with cytochalasin-like activity against actin polymerization in vitro.

We have obtained an inhibitor fraction containing cytochalasin-like activity from human platelets. Using a procedure involving DEAE-cellulose, hydroxyapatite and gel filtration column chromatography, we obtained a fraction from human platelets which apparently can compete with 3H--cytochalasin B for binding to spectrin-actin complexes from human erythrocytes. The inhibitor activity is nondialyzable, sensitive to heat and to trypsin and has a Stoke's radius of 40 A. This fraction stops nuclei-induced actin polymerization in 0.4 mM MgCl2 and reduces the viscosity of F actin to that of G actin, which suggests depolymerization of the filaments. These results suggest that the inhibitor fraction contains a protein which interacts with actin filaments and nuclei in a manner similar to that of cytochalasin B. It is possible that such a protein is involved in the control of cell motility by affecting assembly and disassembly of actin-containing microfilaments in vivo.