Ipi mocap crack 4
Safety was evaluated during the study through monitoring of adverse events (AEs) and clinical laboratory data. Toxicity assessments were performed on the day of each treatment using the Common Terminology Criteria for Adverse Events (CTCAE) of the National Cancer Institute (NCI) version 3.0. In the absence of treatment-limiting toxicities, patients could continue on treatment until the time of disease progression. This starting dose was chosen based on several phase 1 studies 11 in which 400 mg/m 2 twice-weekly was found to be at or below the maximum tolerated dose of IPI-504 as a single agent. IPI-504 (400 mg/m 2) was administered as a 30-minute intravenous infusion on days 1, 4, 8, and 11 of a 21-day cycle.
IPI MOCAP CRACK 4 TRIAL
7 Based on the scientific rationale for Hsp90 inhibition in advanced prostate cancer, favorable pharmacologic properties of IPI-504, 9 and significant preclinical activity, 10 an open label, multi-center, phase II trial of IPI-504 was initiated in patients with CRPC. 7, 8 17-AAG is subsequently reduced back to the hydroquinone via cellular reductase enzymes, such that the two moieties exist in a dynamic equilibrium in vivo.
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6 Once delivered to the systemic circulation, IPI-504 is deprotonated under physiologic conditions, and the free base hydroquinone is oxidized to the quinone moiety (17-AAG) under physiologic conditions. IPI-504 (retaspimycin hydrochloride) is a novel, water-soluble hydroquinone hydrochloride salt derivative of 17-AAG and a potent Hsp90 inhibitor. 1, 3 Clinical trials of 17-AAG in patients with CRPC have demonstrated negligible antitumor activity 4 however, the drug is highly insoluble 5 and has complex pharmacokinetics, raising questions of the adequacy of drug delivery. 2 Solit et al demonstrated dose-dependent growth inhibition of both androgen-dependent and androgen-independent prostate cancer xenografts after treatment with the Hsp90 inhibitor 17-allylamine-17-demethoxygeldanamycin (17-AAG). 1 Inhibition of Hsp90 may disrupt multiple mitogenic pathways simultaneously. Many of the proteins implicated in the pathogenesis of castration-resistant prostate cancer (CRPC) are clients for the chaperone protein heat shock protein 90 (Hsp90).