Potential Mechanisms for Thrombocytopenia Development with Trastuzumab Emtansine (T-DM1)

Hirdesh Uppal(Genentech), Estelle Doudement(Genentech), Kaushiki Mahapatra(Genentech), Walter C. Darbonne(Gene Therapy Laboratory), Daniela Bumbaca, Ben‐Quan Shen, Xiaoyan Du(Gene Therapy Laboratory), Ola M. Saad(Bioanalytica (Switzerland)), Kristin Harden Bowles(PDL BioPharma (United States)), Steve Olsen(Atotech (United States)), Gail D. Lewis Phillips(Molecular Oncology (United States)), Dylan P. Hartley(Genentech), Mark X. Sliwkowski(Molecular Oncology (United States)), Sandhya Girish(Atotech (United States)), Donna M. Dambach(Major League Baseball), Vanitha Ramakrishnan(Project Management Institute)
Clinical Cancer Research
November 4, 2014
Cited by 208

Abstract

PURPOSE: Trastuzumab-emtansine (T-DM1) is an antibody-drug conjugate (ADC) comprising the cytotoxic agent DM1 conjugated to trastuzumab with a stable linker. Thrombocytopenia was the dose-limiting toxicity in the phase I study, and grade ≥3 thrombocytopenia occurred in up to 13% of patients receiving T-DM1 in phase III studies. We investigated the mechanism of T-DM1-induced thrombocytopenia. EXPERIMENTAL DESIGN: The effect of T-DM1 on platelet function was measured by aggregometry, and by flow cytometry to detect the markers of activation. The effect of T-DM1 on differentiation and maturation of megakaryocytes (MK) from human hematopoietic stem cells was assessed by flow cytometry and microscopy. Binding, uptake, and catabolism of T-DM1 in MKs, were assessed by various techniques including fluorescence microscopy, scintigraphy to detect T-[H(3)]-DM1 and (125)I-T-DM1, and mass spectrometry. The role of FcγRIIa was assessed using blocking antibodies and mutant constructs of trastuzumab that do not bind FcγR. RESULTS: T-DM1 had no direct effect on platelet activation and aggregation, but it did markedly inhibit MK differentiation via a cytotoxic effect. Inhibition occurred with DM1-containing ADCs but not with trastuzumab demonstrating a role for DM1. MKs internalized these ADCs in a HER2-independent, FcγRIIa-dependent manner, resulting in intracellular release of DM1. Binding and internalization of T-DM1 diminished as MKs matured; however, prolonged exposure of mature MKs to T-DM1 resulted in a disrupted cytoskeletal structure. CONCLUSIONS: These data support the hypothesis that T-DM1-induced thrombocytopenia is mediated in large part by DM1-induced impairment of MK differentiation, with a less pronounced effect on mature MKs.


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