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• W2109995176 abstract "Cancer cells have varying levels of susceptibility to chemotherapeutic agents, and the proteins that direct drug susceptibility are promising targets for intervention in cancer. Hpr6 (heme-1 domain protein)/PGRMC1 (progesterone receptor membrane component 1) is overexpressed in tumors, and Hpr6 is the human homolog of a budding yeast damage resistance gene called Dap1p. Cells lacking Dap1p are damage-sensitive, and we have found that inhibition of Hpr6 expression by RNA inhibition (RNAi) increases sensitivity of breast cancer cells to chemotherapeutic drugs. Hpr6 is composed largely of a cytochrome <i>b</i>₅-related heme-1 domain, and we have found that purified Hpr6 binds to heme, similar to its yeast and rodent homologues. We generated an aspartate 120-to-glycine (D120G) mutant of Hpr6 at a highly conserved site in the heme-1 domain and demonstrated that Hpr6-D120G cannot bind to heme. The Hpr6-D120G mutant was named Hpr6<i>^hbd</i> for heme binding defective. We prepared an adenovirus encoding Hpr6<i>^hbd</i> and found that adenovirus Hpr6<i>^hbd</i> increases susceptibility of breast cancer cells to doxorubicin and camptothecin. Our findings support a model in which Hpr6, similar to its yeast homolog, binds to heme and regulates susceptibility to damaging agents." @default.
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• W2109995176 date "2005-10-18" @default.
• W2109995176 modified "2023-09-26" @default.
• W2109995176 title "Hpr6 (Heme-1 Domain Protein) Regulates the Susceptibility of Cancer Cells to Chemotherapeutic Drugs" @default.
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• W2109995176 doi "https://doi.org/10.1124/jpet.105.094631" @default.
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