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Cytochalasin B is a cell-permeable mycotoxin binding to the barbed end of actin filaments, disrupting the formation of actin polymers, with Kd value of 1.4-2.2 nM for F-actin.

Cytochalasin B is a cell-permeable mycotoxin binding to the barbed end of actin filaments, inhibits the enlongation and shortening of actin filaments, with Kds of 2.2 nM and 1.4 nM for F-actin in the presence of MgCl2 (2 mM) or MgCl2 (2 mM) plus KCl, respectively[1]. Cytochalasin B (0.1-10 μM) shows inhibitory effect on multiple murine cancer cell lines, with IC50s of 2.56 μM (M109c), 10.46 μM (B16BL6), 105.5 μM (P388/ADR), 51.9 μM (P388/S) and IC80s of 12.23 μM (M109c), 44.86 μM (B16BL6), 188.4 μM (P388/ADR), 84.1 μM (P388/S) after treatment for 3 h, with IC50s of 0.25 μM (M109c), 0.37 μM (B16F10), 0.87 μM (B16BL6), and IC80s of 0.75 μM (M109c), 1.21 μM (B16F10), 10.41 μM (B16BL6) after treatment for 4 days[2]. Cytochalasin B (6 μM) increases the myofibrillar fragmentation index (MFI), which is attributed to the intensely breaking of myofibrillar proteins into short segments. Cytochalasin B also accelerates the disruption of actin filaments. In addition, Cytochalasin B accelerates the transformation from F-actin to G-actin, lowering the content of F-actin and significantly increasing G-actin bands during postmortem conditioning[3].

Cytochalasin B (10, 25, 50 mg/kg, i.p.) dose-dependently increases the life expectancy of Balb/c mice bearing with P388/ADR leukemias. Cytochalasin B at 50 mg/kg produces 10 % long-term survival in the multidrug resistant P388/ADR cohort, and 40 % long-term survival in the drug sensitive P388/S cohort[2].

[1]. Theodoropoulos PA, et al. Cytochalasin B may shorten actin filaments by a mechanism independent of barbed end capping. Biochem Pharmacol. 1994 May 18;47(10):1875-81. [2]. Trendowski M, et al. Chemotherapy with cytochalasin congeners in vitro and in vivo against murine models. Invest New Drugs. 2015 Apr;33(2):290-9. [3]. Zhou C, et al. The effect of Cytochalasin B and Jasplakinolide on depolymerization of actin filaments in goose muscles during postmortem conditioning. Food Res Int. 2016 Dec;90:1-7.

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