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Beschreibung

A cell-permeable, beta-lactone acyl protein thioesterase 1 (APT1) inhibitor (IC50 = 0.67 µ,M, in an enzymatic assay) that is shown to specifically block Ras depalmitoylation, without affecting Ras acylation, in MDCK cells, both in vitro and in vivo. It induces a marked redistribution of NRas to endomembranes (1 µ,M) without notable cytotoxicity, and is shown to elicit a loss of the precise steady-state localization of palmitoylated Ras proteins in the same cell line. At 50 µ,M, this inhibitor displays a partial phenotypic reversion in oncogenic HRasG12V-transformed fibroblasts. Furthermore, it demonstrates selectivity for APT1 over phospholipase A1, A2, Cbeta and D. It's inhibitory effect is demonstrated to be consistent with that of APT1 downregulation by siRNA.