Reserpine accerelates actin polymerization via interaction with G-actin
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چکیده
منابع مشابه
Gelsolin-actin interaction and actin polymerization in human neutrophils
The fraction of polymerized actin in human blood neutrophils increases after exposure to formyl-methionyl-leucyl-phenylalanine (fmlp), is maximal 10 s after peptide addition, and decreases after 300 s. Most of the gelsolin (85 +/- 11%) in resting ficoll-hypaque (FH)-purified neutrophils is in an EGTA resistant, 1:1 gelsolin-actin complex, and, within 5 s after 10(-7) M fmlp activation, the amou...
متن کاملThe interaction between ATP-actin and ADP-actin. A tentative model for actin polymerization.
The involvement of interactions between ATP-actin and ADP-actin in actin polymerization has been studied. It has been found that ATP-actin and ADP-actin can copolymerize and that the rate of nucleation is enhanced when both ATP-actin and ADP-actin are present in solution. The fact that the heterologous interaction between ATP-actin (T) and ADP-actin (D) is stronger than either of the homologous...
متن کاملDecavanadate interactions with actin: inhibition of G-actin polymerization and stabilization of decameric vanadate.
Decameric vanadate species (V10) inhibit the rate and the extent of G-actin polymerization with an IC50 of 68+/-22 microM and 17+/-2 microM, respectively, whilst they induce F-actin depolymerization at a lower extent. On contrary, no effect on actin polymerization and depolymerization was detected for 2mM concentration of "metavanadate" solution that contains ortho and metavanadate species, as ...
متن کاملPolymerization of ADP-actin
Using hexokinase, glucose, and ATP to vary reversibly the concentrations of ADP and ATP in solution and bound to Acanthamoeba actin, I measured the relative critical concentrations and elongation rate constants for ATP-actin and ADP-actin in 50 mM KCl, 1 mM MgCl2, 1 mM EGTA, 0.1 mM nucleotide, 0.1 mM CaCl2, 10 mM imidazole, pH 7. By both steady-state and elongation rate methods, the critical co...
متن کاملBidirectional polymerization of G-actin on the human erythrocyte membrane
The directional polymerization of actin on the erythrocyte membrane has been examined at various concentrations of G-actin by thin-section electron microscopy. For this purpose, a new experimental system using single-layered erythrocyte membranes with the cytoplasmic surfaces freely exposed was developed. The preformed actin filaments did not bind with the cytoplasmic surface of the erythrocyte...
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ژورنال
عنوان ژورنال: Japanese Journal of Pharmacology
سال: 1988
ISSN: 0021-5198
DOI: 10.1016/s0021-5198(19)57144-x