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• W2022101841 abstract "Cellular signal transduction responses to drugs are not always identical; rather, they depend on concentration, administration method, and time after administration. To monitor drug-induced signaling, we produced “reverse-phase” protein arrays (RPPAs) using cell lysates from three anticancer drugs (5FU, CIS, CPT), two administration methods (sustained, Sus; temporal, Tem), and three concentrations (High, Medium, Low) of drug administration over a 24-hour period. The combination of drug types, concentrations, and administration methods collectively yielded 18 unique drug administration conditions. Each RPPA was individually probed with 37 primary antibodies from our antibody panel; these antibodies recognize the proteins involved in genotoxic stress response. The quantitative readout was then analyzed to see if there was: (i) a general trend in protein dynamics in response to each drug condition; and (ii) significance in those proteins that exhibited similar dynamics. We first classified 666 time-course protein dynamics. About 38% of the protein dynamics showed an increasing trend, whereas about 32% showed a decreasing trend. Proteins exhibited earlier peaks when stimulated by Low or Medium concentrations for all drugs, while proteins exhibited later peaks when stimulated by High concentrations. Clustering analysis of protein dynamics induced by drugs revealed that each dynamic class included proteins of diverse functions. Hence, it is unlikely for cells to respond to particular drugs in a defined pattern. Subsequently, to clarify whether any functional associations are prioritized in drug responses, we evaluated the similarities between the protein dynamics by distance correlation (DC, which is known to have a higher value the tighter the association), to see if any pair of protein dynamics demonstrated a geometric similarity associated with its known interaction. It appeared that apoptosis-related proteins tended to show high DC to other proteins when anticancer drugs were administrated at high enough concentrations to induce apoptosis. We also found that structural cell proteins, such as keratins, showed high DC to apoptosis-related proteins, and confirmed that when these two functional protein groups interact, what results is degradation in the progression of drug-induced apoptosis.These observations indicate that high-dimensional drug response protein dynamic monitoring by RPPAs may offer a unique opportunity to find drug-specific general dynamic trends and potentially novel protein interactions unique to drug administrative conditions such as dose. Citation Format: Satoshi S. Nishizuka, Kazushige Ishida, Go Wakabayashi. Differential anticancer drug response by high-dimensional protein monitoring. [abstract]. In: Proceedings of the 104th Annual Meeting of the American Association for Cancer Research; 2013 Apr 6-10; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2013;73(8 Suppl):Abstract nr 5240. doi:10.1158/1538-7445.AM2013-5240" @default.
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• W2022101841 date "2013-04-15" @default.
• W2022101841 modified "2023-09-25" @default.
• W2022101841 title "Abstract 5240: Differential anticancer drug response by high-dimensional protein monitoring." @default.
• W2022101841 doi "https://doi.org/10.1158/1538-7445.am2013-5240" @default.
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