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Biology subjects

Hay, M. P.

Publications and source records attributed to Hay, M. P..

3 recordsLinked to original sources

Systemic CYP3A inhibition by ritonavir enables selective targeting of hypoxic tumour cells by prodrugs of DNA-PK inhibitors

Hypoxic tumour cells are resistant to many forms of cancer therapy, particularly radiotherapy. Hypoxia-activated prodrugs (HAPs) can potentially address this problem through selective release of drugs ( effectors) in oxygen-deficient microenvironments, via metabolic reduction of a nitro(hetero)aromatic trigger moiety. While many such HAPs show marked selectivity for hypoxia in cell culture, none have yet been approved for clinical use. Here, we report HAPs that release a novel inhibitor of the DNA repair enzyme DNA-dependent protein kinase (DNA-PK) which, like hypoxia, is a major contributor to radioresistance. These ether-linked HAPs provide hypoxia-dependent radiosensitisation in cell culture, but in mice systemic generation of the DNA-PK inhibitor is observed. Using in vitro hepatic metabolism models we demonstrate hypoxia-independent metabolic activation of HAP 4 via oxidation of its linker, which is mediated exclusively by CYP3A. We extend this finding to HAPs with other triggers, linkers and effectors. The clinically used CYP3A-specific inhibitor ritonavir suppressed hepatic metabolism of 4 under oxia without interfering with its hypoxia-dependent activation. In mice, ritonavir markedly enhanced oral bioavailability of the HAP, suppressed systemic formation of the DNA-PK inhibitor, and selectively radiosensitised HCT116 tumours but not the gastrointestinal tract in the radiation field. This combination offers the prospect of increasing the therapeutic ratio of DNA-PK inhibitor-mediated radiosensitisation in patients.

pharmacology and toxicology↗

RaDRI: A computational model for radiosensitisation by DNA double strand break repair inhibitors

Repair of radiation-induced DNA double strand breaks (DSB) is a major contributor to radioresistance and an important target for tumour radiosensitisation. DNA-dependent protein kinase (DNA-PK) plays key roles in non-homologous end-joining (NHEJ), the dominant DSB repair pathway in human cells, and DNA-PK inhibitors (DNA-PKi) are highly effective radiosensitisers. However, many questions remain concerning tumour selectivity, mechanisms of enhancement of cell killing, interaction with other repair pathways and cell cycle checkpoints and the required duration of DNA-PK inhibition. Here, we develop an agent-based computational model for Radiosensitisation by DSB Repair Inhibitors (RaDRI) with a level of complexity suitable for use in pharmacokinetic/pharmacodynamic models, and use it to investigate a potent and selective DNA-PKi, SN39536. RaDRI utilises analytical solutions for the spatial distribution of radiation-induced DSB, and their repair by NHEJ, from the Medras model (McMahon et al. Sci Rep 6:33290, 2016). Features include: (1) cell cycle progression and checkpoints are explicit; (2) probability of assignment of DSB to homologous recombination repair decreases with time post-replication, reflecting chromatin maturation, and is radiation dose-dependent; (3) Misjoining (ligation of ends from different DSBs), leading to chromosome aberrations, increases with time due to active DSB clustering. The model is parameterised using flow cytometry and clonogenic survival datasets for low-LET irradiation of HCT116 cells, with and without the DNA-PKi. Clonogenic survival is computed as a function of the number of remaining DSBs and misjoins at mitosis. RaDRI demonstrates known radiobiological features including a near linear-quadratic dose dependence for killing by radiation, almost exclusively due to DSB misjoining, but predicts a distinct mechanism of radiosensitisation by SN39536 in which failure to resolve DSBs before mitosis becomes a significant driver of radiosensitisation. The model predicts that exposure to the DNA-PKi is required for [~]9 hours to achieve 90% of maximal radiosensitisation of DSB repair-proficient human cells in log-phase growth.

cancer biology↗

Megakaryocyte maturation involves activation of the IRE1α-dependent adaptive unfolded protein response

Endoplasmic reticulum stress triggers the unfolded protein response (UPR) to promote cell survival or apoptosis. Transient endoplasmic reticulum stress activation has been reported to trigger megakaryocyte production, and UPR activation has been reported as a feature of megakaryocytic cancers. However, the role of UPR signaling in megakaryocyte biology is not fully understood. We studied the involvement of UPR in human megakaryocytic differentiation using PMA (phorbol 12-myristate 13-acetate)-induced maturation of megakaryoblastic cell lines and thrombopoietin-induced differentiation of human peripheral blood-derived progenitors. Our results demonstrate that an adaptive UPR is a feature of megakaryocytic differentiation, and that this response is not associated with ER stress-induced apoptosis. Differentiation did not alter the response to the canonical endoplasmic reticulum stressors DTT or thapsigargin. However, thapsigargin, but not DTT, inhibited differentiation, consistent with the involvement of Ca2+ signaling in megakaryocyte differentiation.

cell biology↗