Siegel, R. L., Miller, Okay. D., Wagle, N. S. & Jemal, A. Most cancers statistics, 2023. CA Most cancers J. Clin. 73, 17–48 (2023).
Moreira, D. M. et al. Predicting time from metastasis to general survival in castration-resistant prostate most cancers: outcomes from SEARCH. Clin. Genitourin. Most cancers 15, 60–66. e62 (2017).
Chen, X., Comish, P. B., Tang, D. & Kang, R. Traits and biomarkers of ferroptosis. Entrance. Cell Dev. Biol. 9, 637162 (2021).
Yang, W. S. et al. Peroxidation of polyunsaturated fatty acids by lipoxygenases drives ferroptosis. Proc. Natl Acad. Sci. USA 113, E4966–E4975 (2016).
Lin, Z. et al. The lipid flippase SLC47A1 blocks metabolic vulnerability to ferroptosis. Nat. Commun. 13, 7965 (2022).
Catala, A. Lipid peroxidation of membrane phospholipids generates hydroxy-alkenals and oxidized phospholipids lively in physiological and/or pathological circumstances. Chem. Phys. Lipids 157, 1–11 (2009).
Gao, M. et al. Function of mitochondria in ferroptosis. Mol. Cell 73, 354–363 e353 (2019).
Park, M. W. et al. NOX4 promotes ferroptosis of astrocytes by oxidative stress-induced lipid peroxidation through the impairment of mitochondrial metabolism in Alzheimer’s illnesses. Redox Biol. 41, 101947 (2021).
Yan, B. et al. Membrane harm throughout ferroptosis is attributable to oxidation of phospholipids catalyzed by the oxidoreductases POR and CYB5R1. Mol. Cell 81, 355–369 e310 (2021).
Zhang, S. et al. Double-edge sword roles of iron in driving vitality manufacturing versus instigating ferroptosis. Cell Dying Dis. 13, 40 (2022).
von Krusenstiern, A. N. et al. Identification of important websites of lipid peroxidation in ferroptosis. Nat. Chem. Biol. 19, 719–730 (2023).
Yang, W. S. & Stockwell, B. R. Ferroptosis: loss of life by lipid peroxidation. Tendencies Cell Biol. 26, 165–176 (2016).
Conrad, M. & Friedmann Angeli, J. P. Glutathione peroxidase 4 (Gpx4) and ferroptosis: what’s so particular about it? Mol. Cell Oncol. 2, e995047 (2015).
Lu, S. C. Glutathione synthesis. Biochim. Biophys. Acta 1830, 3143–3153 (2013).
Du, Y. & Guo, Z. Latest progress in ferroptosis: inducers and inhibitors. Cell Dying Discov. 8, 501 (2022).
Li, Q. et al. Understanding sorafenib-induced ferroptosis and resistance mechanisms: implications for most cancers remedy. Eur. J. Pharmacol. 955, 175913 (2023).
Friedmann Angeli, J. P. et al. Inactivation of the ferroptosis regulator Gpx4 triggers acute renal failure in mice. Nat. Cell Biol. 16, 1180–1191 (2014).
Yan, H. F. et al. Ferroptosis: mechanisms and hyperlinks with illnesses. Sign. Transduct. Goal. Ther. 6, 49 (2021).
Mao, C. et al. DHODH-mediated ferroptosis defence is a targetable vulnerability in most cancers. Nature 593, 586–590 (2021).
Cirilli, I. et al. Function of coenzyme Q10 in well being and illness: an replace on the final 10 years (2010–2020). Antioxidants 10, 1325 (2021).
Bentinger, M., Tekle, M. & Dallner, G. Coenzyme Q — biosynthesis and capabilities. Biochem. Biophys. Res. Commun. 396, 74–79 (2010).
Kraft, V. A. N. et al. GTP cyclohydrolase 1/tetrahydrobiopterin counteract ferroptosis by way of lipid transforming. ACS Cent. Sci. 6, 41–53 (2020).
Lei, G., Zhuang, L. & Gan, B. Focusing on ferroptosis as a vulnerability in most cancers. Nat. Rev. Most cancers 22, 381–396 (2022).
Dixon, S. J. et al. Pharmacological inhibition of cystine-glutamate change induces endoplasmic reticulum stress and ferroptosis. Elife 3, e02523 (2014).
Jeong, S. D. et al. Enhanced immunogenic cell loss of life by apoptosis/ferroptosis hybrid pathway potentiates PD-L1 blockade most cancers immunotherapy. ACS Biomater. Sci. Eng. 8, 5188–5198 (2022).
Lei, G. et al. The position of ferroptosis in ionizing radiation-induced cell loss of life and tumor suppression. Cell Res. 30, 146–162 (2020).
Viswanathan, V. S. et al. Dependency of a therapy-resistant state of most cancers cells on a lipid peroxidase pathway. Nature 547, 453–457 (2017).
Tousignant, Okay. D. et al. Remedy-induced lipid uptake and transforming underpin ferroptosis hypersensitivity in prostate most cancers. Most cancers Metab. 8, 11 (2020).
Ghoochani, A. et al. Ferroptosis inducers are a novel therapeutic method for superior prostate most cancers. Most cancers Res. 81, 1583–1594 (2021).
Yang, Y. et al. Ferroptosis inducer erastin downregulates androgen receptor and its splice variants in castration-resistant prostate most cancers. Oncol. Rep. 45, 25 (2021).
Mathur, D. et al. PTEN regulates glutamine flux to pyrimidine synthesis and sensitivity to dihydroorotate dehydrogenase inhibition. Most cancers Discov. 7, 380–390 (2017).
Lv, Z. et al. Figuring out a ferroptosis-related gene signature for predicting biochemical recurrence of prostate most cancers. Entrance. Cell Dev. Biol. 9, 666025 (2021).
Mao, C., Liu, X., Yan, Y., Olszewski, Okay. & Gan, B. Reply to: DHODH inhibitors sensitize to ferroptosis by FSP1 inhibition. Nature 619, E19–E23 (2023).
Mishima, E. et al. DHODH inhibitors sensitize to ferroptosis by FSP1 inhibition. Nature 619, E9–E18 (2023).
Yoo, S. E. et al. Gpx4 ablation in grownup mice leads to a deadly phenotype accompanied by neuronal loss in mind. Free. Radic. Biol. Med. 52, 1820–1827 (2012).
Mei, J., Webb, S., Zhang, B. & Shu, H. B. The p53-inducible apoptotic protein AMID isn’t required for regular improvement and tumor suppression. Oncogene 25, 849–856 (2006).
Doll, S. et al. ACSL4 dictates ferroptosis sensitivity by shaping mobile lipid composition. Nat. Chem. Biol. 13, 91–98 (2017).
Rodriguez, R., Schreiber, S. L. & Conrad, M. Persister most cancers cells: iron habit and vulnerability to ferroptosis. Mol. Cell 82, 728–740 (2022).
Scheinberg, T., Mak, B., Butler, L., Selth, L. & Horvath, L. G. Focusing on lipid metabolism in metastatic prostate most cancers. Ther. Adv. Med. Oncol. 15, 17588359231152839 (2023).
Mah, C. Y., Nassar, Z. D., Swinnen, J. V. & Butler, L. M. Lipogenic results of androgen signaling in regular and malignant prostate. Asian J. Urol. 7, 258–270 (2020).
Poulose, N. et al. Genetics of lipid metabolism in prostate most cancers. Nat. Genet. 50, 169–171 (2018).
Scaglia, N., Frontini-Lopez, Y. R. & Zadra, G. Prostate most cancers development: as a matter of fat. Entrance. Oncol. 11, 719865 (2021).
Castelli, S., De Falco, P., Ciccarone, F., Desideri, E. & Ciriolo, M. R. Lipid catabolism and ROS in most cancers: a bidirectional liaison. Cancers 13, 5484 (2021).
Iglesias-Gato, D. et al. The proteome of main prostate most cancers. Eur. Urol. 69, 942–952 (2016).
Magtanong, L. et al. Exogenous monounsaturated fatty acids promote a ferroptosis-resistant cell state. Cell Chem. Biol. 26, 420–432 e429 (2019).
Das, U. N. Saturated fatty acids, MUFAs and PUFAs regulate ferroptosis. Cell Chem. Biol. 26, 309–311 (2019).
Yuan, H., Li, X., Zhang, X., Kang, R. & Tang, D. Identification of ACSL4 as a biomarker and contributor of ferroptosis. Biochem. Biophys. Res. Commun. 478, 1338–1343 (2016).
Yang, Y. et al. ACSL3 and ACSL4, distinct roles in ferroptosis and cancers. Cancers 14, 5896 (2022).
Doll, S. & Conrad, M. Iron and ferroptosis: a nonetheless ill-defined liaison. IUBMB Life 69, 423–434 (2017).
Ma, Y. et al. Lengthy-chain Acyl-CoA synthetase 4-mediated fatty acid metabolism sustains androgen receptor pathway-independent prostate most cancers. Mol. Most cancers Res. 19, 124–135 (2021).
Marques, R. B. et al. Modulation of androgen receptor signaling in hormonal therapy-resistant prostate most cancers cell strains. PLoS ONE 6, e23144 (2011).
Wu, X. et al. ACSL4 promotes prostate most cancers development, invasion and hormonal resistance. Oncotarget 6, 44849–44863 (2015).
Wang, M. E. et al. RB1-deficient prostate tumor development and metastasis are weak to ferroptosis induction through the E2F/ACSL4 axis. J. Clin. Make investments. 133, e166647 (2023).
Orlando, U. D. et al. Acyl-CoA synthetase-4 is implicated in drug resistance in breast most cancers cell strains involving the regulation of energy-dependent transporter expression. Biochem. Pharmacol. 159, 52–63 (2019).
Sanchez-Martinez, R., Cruz-Gil, S., Garcia-Alvarez, M. S., Reglero, G. & Ramirez de Molina, A. Complementary ACSL isoforms contribute to a non-Warburg advantageous energetic standing characterizing invasive colon most cancers cells. Sci. Rep. 7, 11143 (2017).
Wu, X. et al. Lengthy chain fatty Acyl-CoA synthetase 4 is a biomarker for and mediator of hormone resistance in human breast most cancers. PLoS ONE 8, e77060 (2013).
Xia, H. et al. Simultaneous silencing of ACSL4 and induction of GADD45B in hepatocellular carcinoma cells amplifies the synergistic therapeutic impact of aspirin and sorafenib. Cell Dying Discov. 3, 17058 (2017).
Mashima, T., Seimiya, H. & Tsuruo, T. De novo fatty-acid synthesis and associated pathways as molecular targets for most cancers remedy. Br. J. Most cancers 100, 1369–1372 (2009).
Sena, L. A. & Denmeade, S. R. Fatty acid synthesis in prostate most cancers: vulnerability or epiphenomenon? Most cancers Res. 81, 4385–4393 (2021).
Cerami, E. et al. The cBio most cancers genomics portal: an open platform for exploring multidimensional most cancers genomics information. Most cancers Discov. 2, 401–404 (2012).
Swinnen, J. V., Brusselmans, Okay. & Verhoeven, G. Elevated lipogenesis in most cancers cells: new gamers, novel targets. Curr. Opin. Clin. Nutr. Metab. Care 9, 358–365 (2006).
Swinnen, J. V., Esquenet, M., Goossens, Okay., Heyns, W. & Verhoeven, G. Androgens stimulate fatty acid synthase within the human prostate most cancers cell line LNCaP. Most cancers Res. 57, 1086–1090 (1997).
Heemers, H. V., Verhoeven, G. & Swinnen, J. V. Androgen activation of the sterol regulatory element-binding protein pathway: present insights. Mol. Endocrinol. 20, 2265–2277 (2006).
Butler, L. M., Centenera, M. M. & Swinnen, J. V. Androgen management of lipid metabolism in prostate most cancers: novel insights and future functions. Endocr. Relat. Most cancers 23, R219–227, (2016).
Han, L. Q., Gao, T. Y., Yang, G. Y. & Loor, J. J. Overexpression of SREBF chaperone (SCAP) enhances nuclear SREBP1 translocation to upregulate fatty acid synthase (FASN) gene expression in bovine mammary epithelial cells. J. Dairy. Sci. 101, 6523–6531 (2018).
Rossi, S. et al. Fatty acid synthase expression defines distinct molecular signatures in prostate most cancers. Mol. Most cancers Res. 1, 707–715 (2003).
Shah, U. S. et al. Fatty acid synthase gene overexpression and replica quantity acquire in prostate adenocarcinoma. Hum. Pathol. 37, 401–409 (2006).
Epstein, J. I., Carmichael, M. & Partin, A. W. OA-519 (fatty acid synthase) as an unbiased predictor of pathologic state in adenocarcinoma of the prostate. Urology 45, 81–86 (1995).
Track, X. et al. PDK4 dictates metabolic resistance to ferroptosis by suppressing pyruvate oxidation and fatty acid synthesis. Cell Rep. 34, 108767 (2021).
Li, C. et al. LKB1-AMPK axis negatively regulates ferroptosis by inhibiting fatty acid synthesis. Sign. Transduct. Goal. Ther. 5, 187 (2020).
Lee, H. et al. Vitality-stress-mediated AMPK activation inhibits ferroptosis. Nat. Cell Biol. 22, 225–234 (2020).
Bartolacci, C. et al. Focusing on de novo lipogenesis and the Lands cycle induces ferroptosis in KRAS-mutant lung most cancers. Nat. Commun. 13, 4327 (2022).
Hardie, D. G., Ross, F. A. & Hawley, S. A. AMPK: a nutrient and vitality sensor that maintains vitality homeostasis. Nat. Rev. Mol. Cell Biol. 13, 251–262 (2012).
Park, H. U. et al. AMP-activated protein kinase promotes human prostate most cancers cell development and survival. Mol. Most cancers Ther. 8, 733–741 (2009).
Tennakoon, J. B. et al. Androgens regulate prostate most cancers cell development through an AMPK-PGC-1ɑ-mediated metabolic change. Oncogene 33, 5251–5261 (2014).
Lin, C. et al. Inhibition of CAMKK2 impairs autophagy and castration-resistant prostate most cancers through suppression of AMPK-ULK1 signaling. Oncogene 40, 1690–1705 (2021).
Khan, A. S. & Frigo, D. E. A spatiotemporal speculation for the regulation, position, and focusing on of AMPK in prostate most cancers. Nat. Rev. Urol. 14, 164–180 (2017).
Frigo, D. E. et al. CaM kinase kinase beta-mediated activation of the expansion regulatory kinase AMPK is required for androgen-dependent migration of prostate most cancers cells. Most cancers Res. 71, 528–537 (2011).
Enoch, H. G., Catala, A. & Strittmatter, P. Mechanism of rat liver microsomal stearyl-CoA desaturase. Research of the substrate specificity, enzyme-substrate interactions, and the perform of lipid. J. Biol. Chem. 251, 5095–5103 (1976).
Amezaga, J. et al. Altered pink blood cell membrane fatty acid profile in most cancers sufferers. Vitamins 10, 1853 (2018).
Chavarro, J. E. et al. Blood ranges of saturated and monounsaturated fatty acids as markers of de novo lipogenesis and danger of prostate most cancers. Am. J. Epidemiol. 178, 1246–1255 (2013).
Fritz, V. et al. Abrogation of de novo lipogenesis by stearoyl-CoA desaturase 1 inhibition interferes with oncogenic signaling and blocks prostate most cancers development in mice. Mol. Most cancers Ther. 9, 1740–1754 (2010).
Yi, J., Zhu, J., Wu, J., Thompson, C. B. & Jiang, X. Oncogenic activation of PI3K-AKT-mTOR signaling suppresses ferroptosis through SREBP-mediated lipogenesis. Proc. Natl Acad. Sci. USA 117, 31189–31197 (2020).
Tesfay, L. et al. Stearoyl-CoA desaturase 1 protects ovarian most cancers cells from ferroptotic cell loss of life. Most cancers Res. 79, 5355–5366 (2019).
Kagan, V. E. et al. Oxidized arachidonic and adrenic PEs navigate cells to ferroptosis. Nat. Chem. Biol. 13, 81–90 (2017).
D’Angelo, S., Motti, M. L. & Meccariello, R. ω-3 and ω-6 polyunsaturated fatty acids, weight problems and most cancers. Vitamins 12, 2751 (2020).
Lee, J. M., Lee, H., Kang, S. & Park, W. J. Fatty acid desaturases, polyunsaturated fatty acid regulation, and biotechnological advances. Vitamins 8, 23 (2016).
Lee, J. Y. et al. Polyunsaturated fatty acid biosynthesis pathway determines ferroptosis sensitivity in gastric most cancers. Proc. Natl Acad. Sci. USA 117, 32433–32442 (2020).
Yamane, D. et al. FADS2-dependent fatty acid desaturation dictates mobile sensitivity to ferroptosis and permissiveness for hepatitis C virus replication. Cell Chem. Biol. 29, 799–810 e794 (2022).
Xu, H. et al. ELOVL5-mediated lengthy chain fatty acid elongation contributes to enzalutamide resistance of prostate most cancers. Cancers 13, 3957 (2021).
Centenera, M. M. et al. ELOVL5 is a crucial and targetable fatty acid elongase in prostate most cancers. Most cancers Res. 81, 1704–1718 (2021).
Schlaepfer, I. R. & Joshi, M. CPT1A-mediated fats oxidation, mechanisms, and therapeutic potential. Endocrinology 161, bqz046 (2020).
Flaig, T. W. et al. Lipid catabolism inhibition sensitizes prostate most cancers cells to antiandrogen blockade. Oncotarget 8, 56051–56065 (2017).
Joshi, M. et al. CPT1A helps castration-resistant prostate most cancers in androgen-deprived circumstances. Cells 8, 115 (2019).
Nassar, Z. D. et al. Human DECR1 is an androgen-repressed survival issue that regulates PUFA oxidation to guard prostate tumor cells from ferroptosis. Elife 9, e54166 (2020).
Gao, M., Monian, P., Quadri, N., Ramasamy, R. & Jiang, X. Glutaminolysis and transferrin regulate ferroptosis. Mol. Cell 59, 298–308 (2015).
Philpott, C. C. et al. Iron-tracking methods: chaperones seize iron within the cytosolic labile iron pool. Entrance. Mol. Biosci. 10, 1127690 (2023).
Yanatori, I., Richardson, D. R., Imada, Okay. & Kishi, F. Iron export by way of the transporter ferroportin 1 is modulated by the iron chaperone PCBP2. J. Biol. Chem. 291, 17303–17318 (2016).
Donovan, A. et al. The iron exporter ferroportin/Slc40a1 is important for iron homeostasis. Cell Metab. 1, 191–200 (2005).
Nemeth, E. & Ganz, T. The position of hepcidin in iron metabolism. Acta Haematol. 122, 78–86 (2009).
Hubert, N. & Hentze, M. W. Beforehand uncharacterized isoforms of divalent metallic transporter (DMT)-1: implications for regulation and mobile perform. Proc. Natl Acad. Sci. USA 99, 12345–12350 (2002).
Dai, E., Meng, L., Kang, R., Wang, X. & Tang, D. ESCRT-III-dependent membrane restore blocks ferroptosis. Biochem. Biophys. Res. Commun. 522, 415–421 (2020).
Vela, D. Iron metabolism in prostate most cancers; from fundamental science to new therapeutic methods. Entrance. Oncol. 8, 547 (2018).
Torti, S. V., Manz, D. H., Paul, B. T., Blanchette-Farra, N. & Torti, F. M. Iron and most cancers. Annu. Rev. Nutr. 38, 97–125 (2018).
Brown, R. A. M. et al. Altered iron metabolism and impression in most cancers biology, metastasis, and immunology. Entrance. Oncol. 10, 476 (2020).
Deng, Z., Manz, D. H., Torti, S. V. & Torti, F. M. Iron-responsive element-binding protein 2 performs a necessary position in regulating prostate most cancers cell development. Oncotarget 8, 82231–82243 (2017).
Keer, H. N. et al. Elevated transferrin receptor content material in human prostate most cancers cell strains assessed in vitro and in vivo. J. Urol. 143, 381–385 (1990).
Kuvibidila, S., Gauthier, T., Warrier, R. P. & Rayford, W. Elevated ranges of serum transferrin receptor and serum transferrin receptor/log ferritin ratios in males with prostate most cancers and the implications for body-iron shops. J. Lab. Clin. Med. 144, 176–182 (2004).
Xue, D., Zhou, C. X., Shi, Y. B., Lu, H. & He, X. Z. Decreased expression of ferroportin in prostate most cancers. Oncol. Lett. 10, 913–916 (2015).
Burnell, S. E. A. et al. STEAP2 knockdown reduces the invasive potential of prostate most cancers cells. Sci. Rep. 8, 6252 (2018).
Hou, W. et al. Autophagy promotes ferroptosis by degradation of ferritin. Autophagy 12, 1425–1428 (2016).
Winterbourn, C. C. Toxicity of iron and hydrogen peroxide: the Fenton response. Toxicol. Lett. 82-83, 969–974 (1995).
Dhur, A., Galan, P. & Hercberg, S. Results of various levels of iron deficiency on cytochrome P450 advanced and pentose phosphate pathway dehydrogenases within the rat. J. Nutr. 119, 40–47 (1989).
Pistorius, E. Okay. & Axelrod, B. Iron, an integral part of lipoxygenase. J. Biol. Chem. 249, 3183–3186 (1974).
Yauger, Y. J. et al. Iron accentuated reactive oxygen species launch by NADPH oxidase in activated microglia contributes to oxidative stress in vitro. J. Neuroinflammation 16, 41 (2019).
Bordini, J. et al. Induction of iron extra restricts malignant plasma cells enlargement and potentiates bortezomib impact in fashions of a number of myeloma. Leukemia 31, 967–970 (2017).
Campanella, A. et al. Iron will increase the susceptibility of a number of myeloma cells to bortezomib. Haematologica 98, 971–979 (2013).
Bordini, J. et al. Iron induces cell loss of life and strengthens the efficacy of antiandrogen remedy in prostate most cancers fashions. Clin. Most cancers Res. 26, 6387–6398 (2020).
Maccarinelli, F. et al. Iron supplementation enhances RSL3-induced ferroptosis to deal with naive and forestall castration-resistant prostate most cancers. Cell Dying Discov. 9, 81 (2023).
Liu, Y. et al. Liposomes embedded with PEGylated iron oxide nanoparticles allow ferroptosis and mixture remedy in most cancers. Natl Sci. Rev. 10, nwac167 (2023).
Fernandez-Acosta, R. et al. Novel iron oxide nanoparticles induce ferroptosis in a panel of most cancers cell strains. Molecules 27, 3970 (2022).
Bonvin, D. et al. Tuning properties of iron oxide nanoparticles in aqueous synthesis with out ligands to enhance MRI relaxivity and SAR. Nanomaterials 7, 225 (2017).
Hajikarimi, Z., Khoei, S., Khoee, S. & Mahdavi, S. R. Analysis of the cytotoxic results of PLGA coated iron oxide nanoparticles as a service of 5- fluorouracil and mega-voltage X-ray radiation in DU145 prostate most cancers cell line. IEEE Trans. Nanobiosci. 13, 403–408 (2014).
Kader, A. et al. Iron oxide nanoparticles for visualization of prostate most cancers in MRI. Cancers 14, 2909 (2022).
Cluntun, A. A., Lukey, M. J., Cerione, R. A. & Locasale, J. W. Glutamine metabolism in most cancers: understanding the heterogeneity. Tendencies Most cancers 3, 169–180 (2017).
Gong, T. et al. Glutamine metabolism in cancers: focusing on the oxidative homeostasis. Entrance. Oncol. 12, 994672 (2022).
Wang, Q. et al. Focusing on ASCT2-mediated glutamine uptake blocks prostate most cancers development and tumour improvement. J. Pathol. 236, 278–289 (2015).
Wang, Q. et al. Androgen receptor and nutrient signaling pathways coordinate the demand for elevated amino acid transport throughout prostate most cancers development. Most cancers Res. 71, 7525–7536 (2011).
Cardoso, H. J. et al. Glutaminolysis is a metabolic route important for survival and development of prostate most cancers cells and a goal of 5ɑ-dihydrotestosterone regulation. Cell Oncol. 44, 385–403 (2021).
Serpa, J. Cysteine as a carbon supply, a scorching spot in most cancers cells survival. Entrance. Oncol. 10, 947 (2020).
Poltorack, C. D. & Dixon, S. J. Understanding the position of cysteine in ferroptosis: progress & paradoxes. FEBS J. 289, 374–385 (2022).
Yang, J., Dai, X., Xu, H., Tang, Q. & Bi, F. Regulation of ferroptosis by amino acid metabolism in most cancers. Int. J. Biol. Sci. 18, 1695–1705 (2022).
Zhong, W. et al. Extracellular redox state shift: a novel method to focus on prostate most cancers invasion. Free. Radic. Biol. Med. 117, 99–109 (2018).
Doxsee, D. W. et al. Sulfasalazine-induced cystine hunger: potential use for prostate most cancers remedy. Prostate 67, 162–171 (2007).
Cramer, S. L. et al. Systemic depletion of L-cyst(e)ine with cyst(e)inase will increase reactive oxygen species and suppresses tumor development. Nat. Med. 23, 120–127 (2017).
Mandigo, A. C. et al. RB/E2F1 as a grasp regulator of most cancers cell metabolism in superior illness. Most cancers Discov. 11, 2334–2353 (2021).
Nikfar, S., Rahimi, R., Rezaie, A. & Abdollahi, M. A meta-analysis of the efficacy of sulfasalazine as compared with 5-aminosalicylates within the induction of enchancment and upkeep of remission in sufferers with ulcerative colitis. Dig. Dis. Sci. 54, 1157–1170 (2009).
Rains, C. P., Noble, S. & Faulds, D. Sulfasalazine. A evaluate of its pharmacological properties and therapeutic efficacy within the remedy of rheumatoid arthritis. Medicine 50, 137–156 (1995).
Kavallaris, M. Microtubules and resistance to tubulin-binding brokers. Nat. Rev. Most cancers 10, 194–204 (2010).
Ogura, T., Tanaka, Y., Tamaki, H. & Harada, M. Docetaxel induces Bcl-2- and pro-apoptotic caspase-independent loss of life of human prostate most cancers DU145 cells. Int. J. Oncol. 48, 2330–2338 (2016).
Darshan, M. S. et al. Taxane-induced blockade to nuclear accumulation of the androgen receptor predicts scientific responses in metastatic prostate most cancers. Most cancers Res. 71, 6019–6029 (2011).
de Bono, J. S. et al. Prednisone plus cabazitaxel or mitoxantrone for metastatic castration-resistant prostate most cancers progressing after docetaxel remedy: a randomised open-label trial. Lancet 376, 1147–1154 (2010).
Galsky, M. D., Dritselis, A., Kirkpatrick, P. & Oh, W. Okay. Cabazitaxel. Nat. Rev. Drug. Discov. 9, 677–678 (2010).
Chen, X. et al. Ferroptosis induction improves the sensitivity of docetaxel in prostate most cancers. Oxid. Med. Cell. Longev. 2022, 1–16 (2022).
Jiang, X. et al. TFAP2C-mediated lncRNA PCAT1 inhibits ferroptosis in docetaxel-resistant prostate most cancers by way of c-Myc/miR-25-3p/SLC7A11 signaling. Entrance. Oncol. 12, 862015 (2022).
He, S. et al. ChaC glutathione particular γ-glutamylcyclotransferase 1 inhibits cell viability and will increase the sensitivity of prostate most cancers cells to docetaxel by inducing endoplasmic reticulum stress and ferroptosis. Exp. Ther. Med. 22, 997 (2021).
Ogawa, T. et al. CHAC1 overexpression in human gastric parietal cells with Helicobacter pylori an infection within the secretory canaliculi. Helicobacter 24, e12598 (2019).
Takeda, D. Y. et al. A somatically acquired enhancer of the androgen receptor is a noncoding driver in superior prostate most cancers. Cell 174, 422–432 e413 (2018).
Schweizer, M. T. & Yu, E. Y. Persistent androgen receptor habit in castration-resistant prostate most cancers. J. Hematol. Oncol. 8, 128 (2015).
Abida, W. et al. Genomic correlates of scientific final result in superior prostate most cancers. Proc. Natl Acad. Sci. USA 116, 11428–11436 (2019).
Watson, P. A., Arora, V. Okay. & Sawyers, C. L. Rising mechanisms of resistance to androgen receptor inhibitors in prostate most cancers. Nat. Rev. Most cancers 15, 701–711 (2015).
Cattrini, C. et al. Apalutamide, darolutamide and enzalutamide for nonmetastatic castration-resistant prostate most cancers (nmCRPC): a crucial evaluate. Cancers 14, 1492 (2022).
Desai, Okay., McManus, J. M. & Sharifi, N. Hormonal remedy for prostate most cancers. Endocr. Rev. 42, 354–373 (2021).
Clarke, N. W. et al. Abiraterone and olaparib for metastatic castration-resistant prostate most cancers. NEJM Evid. 1, EVIDoa2200043 (2022).
Chi, Okay. N. et al. Niraparib and abiraterone acetate for metastatic castration-resistant prostate most cancers. J. Clin. Oncol. 41, 3339–3351 (2023).
Hong, T. et al. PARP inhibition promotes ferroptosis through repressing SLC7A11 and synergizes with ferroptosis inducers in BRCA-proficient ovarian most cancers. Redox Biol. 42, 101928 (2021).
Sugiura, M. et al. Identification of AR-V7 downstream genes generally focused by AR/AR-V7 and particularly focused by AR-V7 in castration resistant prostate most cancers. Transl. Oncol. 14, 100915 (2021).
Yang, F. et al. Ferroptosis heterogeneity in triple-negative breast most cancers reveals an modern immunotherapy mixture technique. Cell Metab. 35, 84–100.e8 (2023).
Solar, R. et al. Androgen receptor variants confer castration resistance in prostate most cancers by counteracting antiandrogen-induced ferroptosis. Most cancers Res. 83, 3192–3204 (2023).
Liang, D. et al. Ferroptosis surveillance unbiased of GPX4 and differentially regulated by intercourse hormones. Cell 186, 2748–2764 e2722 (2023).
Ma, D. et al. Crystal construction of a membrane-bound O-acyltransferase. Nature 562, 286–290 (2018).
Masumoto, N. et al. Membrane sure O-acyltransferases and their inhibitors. Biochem. Soc. Trans. 43, 246–252 (2015).
Hodi, F. S. et al. Improved survival with ipilimumab in sufferers with metastatic melanoma. N. Engl. J. Med. 363, 711–723 (2010).
Runcie, Okay. D. & Dallos, M. C. Prostate most cancers immunotherapy — lastly in from the chilly? Curr. Oncol. Rep. 23, 88 (2021).
Graff, J. N. et al. Section II examine of ipilimumab in males with metastatic prostate most cancers with an incomplete response to androgen deprivation remedy. Entrance. Oncol. 10, 1381 (2020).
Fizazi, Okay. et al. Last evaluation of the ipilimumab versus placebo following radiotherapy section III trial in postdocetaxel metastatic castration-resistant prostate most cancers identifies an extra of long-term survivors. Eur. Urol. 78, 822–830 (2020).
Cabel, L. et al. Lengthy-term full remission with Ipilimumab in metastatic castrate-resistant prostate most cancers: case report of two sufferers. J. Immunother. Most cancers 5, 31 (2017).
Sharma, P. et al. Nivolumab plus ipilimumab for metastatic castration-resistant prostate most cancers: preliminary evaluation of sufferers within the checkmate 650 trial. Most cancers Cell 38, 489–499 e483 (2020).
Fizazi, Okay. et al. Nivolumab plus rucaparib for metastatic castration-resistant prostate most cancers: outcomes from the section 2 CheckMate 9KD trial. J. Immunother. Most cancers 10, e004761 (2022).
Fizazi, Okay. et al. Nivolumab plus docetaxel in sufferers with chemotherapy-naive metastatic castration-resistant prostate most cancers: outcomes from the section II CheckMate 9KD trial. Eur. J. Most cancers 160, 61–71 (2022).
Petrylak, D. P. et al. KEYNOTE-921: section III examine of pembrolizumab plus docetaxel for metastatic castration-resistant prostate most cancers. Future Oncol. 17, 3291–3299 (2021).
Antonarakis, E. S. et al. Pembrolizumab for treatment-refractory metastatic castration-resistant prostate most cancers: multicohort, open-label section II KEYNOTE-199 examine. J. Clin. Oncol. 38, 395–405 (2020).
Petrylak, D. P. et al. Security and scientific exercise of atezolizumab in sufferers with metastatic castration-resistant prostate most cancers: a section I examine. Clin. Most cancers Res. 27, 3360–3369 (2021).
Powles, T. et al. Atezolizumab with enzalutamide versus enzalutamide alone in metastatic castration-resistant prostate most cancers: a randomized section 3 trial. Nat. Med. 28, 144–153 (2022).
Rodriguez-Vida, A. et al. Security and efficacy of avelumab plus carboplatin in sufferers with metastatic castration-resistant prostate most cancers in an open-label Section Ib examine. Br. J. Most cancers 128, 21–29 (2023).
Kwan, E. M. et al. Avelumab mixed with stereotactic ablative physique radiotherapy in metastatic castration-resistant prostate most cancers: the section 2 ICE-PAC scientific trial. Eur. Urol. 81, 253–262 (2022).
Karzai, F. et al. Exercise of durvalumab plus olaparib in metastatic castration-resistant prostate most cancers in males with and with out DNA harm restore mutations. J. Immunother. Most cancers 6, 141 (2018).
Kantoff, P. W. et al. Sipuleucel-T immunotherapy for castration-resistant prostate most cancers. N. Engl. J. Med. 363, 411–422 (2010).
Shore, N. D. et al. CD8+ T cells impression rising PSA in biochemically relapsed most cancers sufferers utilizing immunotherapy focusing on tumor-associated antigens. Mol. Ther. 28, 1238–1250 (2020).
Kyriakopoulos, C. E. et al. Multicenter section I trial of a DNA vaccine encoding the androgen receptor ligand-binding area (pTVG-AR, MVI-118) in sufferers with metastatic prostate most cancers. Clin. Most cancers Res. 26, 5162–5171 (2020).
Singh, P., Pal, S. Okay., Alex, A. & Agarwal, N. Growth of PROSTVAC immunotherapy in prostate most cancers. Future Oncol. 11, 2137–2148 (2015).
Gulley, J. L. et al. Section III trial of PROSTVAC in asymptomatic or minimally symptomatic metastatic castration-resistant prostate most cancers. J. Clin. Oncol. 37, 1051–1061 (2019).
van den Eertwegh, A. J. et al. Mixed immunotherapy with granulocyte-macrophage colony-stimulating factor-transduced allogeneic prostate most cancers cells and ipilimumab in sufferers with metastatic castration-resistant prostate most cancers: a section 1 dose-escalation trial. Lancet Oncol. 13, 509–517 (2012).
Small, E. J. et al. Granulocyte macrophage colony-stimulating factor-secreting allogeneic mobile immunotherapy for hormone-refractory prostate most cancers. Clin. Most cancers Res. 13, 3883–3891 (2007).
Higano, C. S. et al. Section 1/2 dose-escalation examine of a GM-CSF-secreting, allogeneic, mobile immunotherapy for metastatic hormone-refractory prostate most cancers. Most cancers 113, 975–984 (2008).
Tschernia, N. P., Norberg, S. M. & Gulley, J. L. CAR T cells attain scientific milestone in prostate most cancers. Nat. Med. 28, 635–636 (2022).
Perera, M. P. J. et al. Chimeric antigen receptor T-cell remedy in metastatic castrate-resistant prostate most cancers. Cancers 14, 503 (2022).
Narayan, V. et al. PSMA-targeting TGFβ-insensitive armored CAR T cells in metastatic castration-resistant prostate most cancers: a section 1 trial. Nat. Med. 28, 724–734 (2022).
Yunger, S. et al. Tumor-infiltrating lymphocytes from human prostate tumors reveal anti-tumor reactivity and potential for adoptive cell remedy. Oncoimmunology 8, e1672494 (2019).
Karbach, J. et al. Tumor-infiltrating lymphocytes mediate full and sturdy remission in a affected person with NY-ESO-1 expressing prostate most cancers. J. Immunother. Most cancers 11, e005847 (2023).
Kamat, N. V., Yu, E. Y. & Lee, J. Okay. BiTE-ing into prostate most cancers with bispecific T-cell engagers. Clin. Most cancers Res. 27, 2675–2677 (2021).
Hummel, H. D. et al. Pasotuxizumab, a BiTE® immune remedy for castration-resistant prostate most cancers: section I, dose-escalation examine findings. Immunotherapy 13, 125–141 (2021).
Wang, W. et al. CD8+ T cells regulate tumour ferroptosis throughout most cancers immunotherapy. Nature 569, 270–274 (2019).
Liao, P. et al. CD8+ T cells and fatty acids orchestrate tumor ferroptosis and immunity through ACSL4. Most cancers Cell 40, 365–378.e6 (2022).
Jiang, Z. et al. TYRO3 induces anti-PD-1/PD-L1 remedy resistance by limiting innate immunity and tumoral ferroptosis. J. Clin. Make investments. 131, e139434 (2021).
Efimova, I. et al. Vaccination with early ferroptotic most cancers cells induces environment friendly antitumor immunity. J. Immunother. Most cancers 8, e001369 (2020).
Tang, D., Kepp, O. & Kroemer, G. Ferroptosis turns into immunogenic: implications for anticancer therapies. Oncoimmunology 10, 1862949 (2020).
Wen, Q., Liu, J., Kang, R., Zhou, B. & Tang, D. The discharge and exercise of HMGB1 in ferroptosis. Biochem. Biophys. Res. Commun. 510, 278–283 (2019).
Yu, B., Choi, B., Li, W. & Kim, D. H. Magnetic area boosted ferroptosis-like cell loss of life and responsive MRI utilizing hybrid vesicles for most cancers immunotherapy. Nat. Commun. 11, 3637 (2020).
Wu, Z. et al. The panorama of immune cells infiltrating in prostate most cancers. Entrance. Oncol. 10, 517637 (2020).
Martin, A. M. et al. Paucity of PD-L1 expression in prostate most cancers: innate and adaptive immune resistance. Prostate Most cancers Prostatic Dis. 18, 325–332 (2015).
Matsushita, M. et al. T cell lipid peroxidation induces ferroptosis and prevents immunity to an infection. J. Exp. Med. 212, 555–568 (2015).
Ma, X. et al. CD36-mediated ferroptosis dampens intratumoral CD8+ T cell effector perform and impairs their antitumor potential. Cell Metab. 33, 1001–1012.e5 (2021).
Zhou, X. et al. Abrogation of HnRNP L enhances anti-PD-1 remedy efficacy through diminishing PD-L1 and selling CD8+ T cell-mediated ferroptosis in castration-resistant prostate most cancers. Acta Pharm. Sin. B 12, 692–707 (2022).
Sindhu, Okay. Okay., Nehlsen, A. D. & Inventory, R. G. Radium-223 for metastatic castrate-resistant prostate most cancers. Pract. Radiat. Oncol. 12, 312–316 (2022).
Parker, C. et al. Alpha emitter radium-223 and survival in metastatic prostate most cancers. N. Engl. J. Med. 369, 213–223 (2013).
Violet, J. et al. Dosimetry of 177Lu-PSMA-617 in metastatic castration-resistant prostate most cancers: correlations between pretherapeutic imaging and whole-body tumor dosimetry with remedy outcomes. J. Nucl. Med. 60, 517–523 (2019).
Solar, M., Niaz, M. O., Nelson, A., Skafida, M. & Niaz, M. J. Assessment of 177Lu-PSMA-617 in sufferers with metastatic castration-resistant prostate most cancers. Cureus 12, e8921 (2020).
Schuchardt, C. et al. Prostate-specific membrane antigen radioligand remedy utilizing 177Lu-PSMA I&T and 177Lu-PSMA-617 in sufferers with metastatic castration-resistant prostate most cancers: comparability of security, biodistribution, and dosimetry. J. Nucl. Med. 63, 1199–1207 (2022).
Kratochwil, C. et al. 225Ac-PSMA-617 for PSMA-targeted ɑ-radiation remedy of metastatic castration-resistant prostate most cancers. J. Nucl. Med. 57, 1941–1944 (2016).
Hammer, S. et al. Preclinical efficacy of a PSMA-targeted thorium-227 conjugate (PSMA-TTC), a focused ɑ remedy for prostate most cancers. Clin. Most cancers Res. 26, 1985–1996 (2020).
Kiess, A. P. et al. 2S)-2-(3-(1-Carboxy-5-(4-211At-Astatobenzamido)Pentyl)Ureido)-pentanedioic acid for PSMA-targeted ɑ-particle radiopharmaceutical remedy. J. Nucl. Med. 57, 1569–1575 (2016).
Ye, L. F. et al. Radiation-induced lipid peroxidation triggers ferroptosis and synergizes with ferroptosis inducers. ACS Chem. Biol. 15, 469–484 (2020).
Lang, X. et al. Radiotherapy and immunotherapy promote tumoral lipid oxidation and ferroptosis through synergistic repression of SLC7A11. Most cancers Discov. 9, 1673–1685 (2019).
Lowe, S. W., Schmitt, E. M., Smith, S. W., Osborne, B. A. & Jacks, T. p53 is required for radiation-induced apoptosis in mouse thymocytes. Nature 362, 847–849 (1993).
Kastan, M. B., Onyekwere, O., Sidransky, D., Vogelstein, B. & Craig, R. W. Participation of p53 protein within the mobile response to DNA harm. Most cancers Res. 51, 6304–6311 (1991).
Jiang, L. et al. Ferroptosis as a p53-mediated exercise throughout tumour suppression. Nature 520, 57–62 (2015).
Wang, Y. et al. Epigenetic regulation of ferroptosis by H2B monoubiquitination and p53. EMBO Rep. 20, e47563 (2019).
Shen, D. et al. PARPi remedy enhances radiotherapy-induced ferroptosis and antitumor immune responses through the cGAS signaling pathway in colorectal most cancers. Most cancers Lett. 550, 215919 (2022).
Lei, G., Mao, C., Yan, Y., Zhuang, L. & Gan, B. Ferroptosis, radiotherapy, and mixture therapeutic methods. Protein Cell 12, 836–857 (2021).
Beretta, G. L. & Zaffaroni, N. Radiotherapy-induced ferroptosis for most cancers remedy. Entrance. Mol. Biosci. 10, 1216733 (2023).
Upadhyayula, P. S. et al. Dietary restriction of cysteine and methionine sensitizes gliomas to ferroptosis and induces alterations in energetic metabolism. Nat. Commun. 14, 1187 (2023).
Xue, Y. et al. Intermittent dietary methionine deprivation facilitates tumoral ferroptosis and synergizes with checkpoint blockade. Nat. Commun. 14, 4758 (2023).
Dierge, E. et al. Peroxidation of n-3 and n-6 polyunsaturated fatty acids within the acidic tumor setting results in ferroptosis-mediated anticancer results. Cell Metab. 33, 1701–1715 e1705 (2021).
Ferrer, M. et al. Ketogenic eating regimen promotes tumor ferroptosis however induces relative corticosterone deficiency that accelerates cachexia. Cell Metab. 35, 1147–1162 e1147 (2023).
Pissios, P. et al. Methionine and choline regulate the metabolic phenotype of a ketogenic eating regimen. Mol. Metab. 2, 306–313 (2013).
Eaton, J. Okay. et al. Selective covalent focusing on of GPX4 utilizing masked nitrile-oxide electrophiles. Nat. Chem. Biol. 16, 497–506 (2020).
Eaton, J. Okay., Ruberto, R. A., Kramm, A., Viswanathan, V. S. & Schreiber, S. L. Diacylfuroxans are masked nitrile oxides that inhibit GPX4 covalently. J. Am. Chem. Soc. 141, 20407–20415 (2019).
Yang, W. S. et al. Regulation of ferroptotic most cancers cell loss of life by GPX4. Cell 156, 317–331 (2014).
Koppula, P. et al. A targetable CoQ-FSP1 axis drives ferroptosis- and radiation-resistance in KEAP1 inactive lung cancers. Nat. Commun. 13, 2206 (2022).
Doll, S. et al. FSP1 is a glutathione-independent ferroptosis suppressor. Nature 575, 693–698 (2019).
Xavier da Silva, T. N., Schulte, C., Alves, A. N., Maric, H. M. & Friedmann Angeli, J. P. Molecular characterization of AIFM2/FSP1 inhibition by iFSP1-like molecules. Cell Dying Dis. 14, 281 (2023).
Hendricks, J. M. et al. Identification of structurally various FSP1 inhibitors that sensitize most cancers cells to ferroptosis. Cell Chem. Biol. 30, 1090–1103 e1097 (2023).
Yoshioka, H. et al. Identification of a small molecule that enhances ferroptosis through inhibition of ferroptosis suppressor protein 1 (FSP1). ACS Chem. Biol. 17, 483–491 (2022).
Antoszczak, M. & Huczynski, A. Salinomycin and its derivatives — a brand new class of multiple-targeted “magic bullets”. Eur. J. Med. Chem. 176, 208–227 (2019).
Miyazaki, Y., Shibuya, M., Sugawara, H., Kawaguchi, O. & Hirsoe, C. Salinomycin, a brand new polyether antibiotic. J. Antibiot. 27, 814–821 (1974).
Zhou, S. et al. Salinomycin: a novel anti-cancer agent with identified anti-coccidial actions. Curr. Med. Chem. 20, 4095–4101 (2013).
Mai, T. T. et al. Salinomycin kills most cancers stem cells by sequestering iron in lysosomes. Nat. Chem. 9, 1025–1033 (2017).
Mohammad, A. et al. Summary 3107: HSB-1216, a novel agent for the remedy of chemotherapy-resistant ES-SCLC. Most cancers Res. 81, 3107–3107 (2021).
Kharbanda, S. et al. Novel iron-mediated cell loss of life (Ferroptosis) inducer, HSB-1216, suppress acute myeloid leukemia development. Eur. J. Most cancers https://doi.org/10.1016/s0959-8049(22)00936-4 (2022).
Li, J. et al. Ferroptosis: previous, current and future. Cell Dying Dis. 11, 88 (2020).
Kloditz, Okay. & Fadeel, B. Three cell deaths and a funeral: macrophage clearance of cells present process distinct modes of cell loss of life. Cell Dying Discov. 5, 65 (2019).
Zou, Y. & Schreiber, S. L. Progress in understanding ferroptosis and challenges in its focusing on for therapeutic profit. Cell Chem. Biol. 27, 463–471 (2020).
Li, Z. et al. In vivo monitoring cystine/glutamate antiporter-mediated cysteine/cystine pool underneath ferroptosis. Anal. Chim. Acta 1125, 66–75 (2020).
Li, Z. Imaging of hydrogen peroxide (H(2)O(2)) throughout the ferroptosis course of in residing most cancers cells with a sensible fluorescence probe. Talanta 212, 120804 (2020).
Conrad, M. & Pratt, D. A. The chemical foundation of ferroptosis. Nat. Chem. Biol. 15, 1137–1147 (2019).
Zeng, F. et al. Ferroptosis detection: from approaches to functions. Angew. Chem. Int. Ed. 62, e202300379 (2023).
Li, J., Kang, R. & Tang, D. Monitoring autophagy-dependent ferroptosis. Strategies Cell Biol. 165, 163–176 (2021).
Wang, F. et al. PALP: a fast imaging method for stratifying ferroptosis sensitivity in regular and tumor tissues in situ. Cell Chem. Biol. 29, 157–170 e156 (2022).
Wang, F., Naowarojna, N. & Zou, Y. Stratifying ferroptosis sensitivity in cells and mouse tissues by photochemical activation of lipid peroxidation and fluorescent imaging. Star. Protoc. 3, 101189 (2022).
Drummen, G. P., van Liebergen, L. C., Op den Kamp, J. A. & Put up, J. A. C11-BODIPY(581/591), an oxidation-sensitive fluorescent lipid peroxidation probe: (micro)spectroscopic characterization and validation of methodology. Free. Radic. Biol. Med. 33, 473–490 (2002).
Hirayama, T., Okuda, Okay. & Nagasawa, H. A extremely selective turn-on fluorescent probe for iron(II) to visualise labile iron in residing cells. Chem. Sci. 4, 1250–1256, (2013).
Kapralov, A. A. et al. Redox lipid reprogramming instructions susceptibility of macrophages and microglia to ferroptotic loss of life. Nat. Chem. Biol. 16, 278–290 (2020).
Weigand, I. et al. Energetic steroid hormone synthesis renders adrenocortical cells extremely vulnerable to kind II ferroptosis induction. Cell Dying Dis. 11, 192 (2020).
Zhao, N. et al. Ferronostics: measuring tumoral ferrous iron with PET to foretell sensitivity to iron-targeted most cancers therapies. J. Nucl. Med. 62, 949–955 (2021).
Phyo, A. P. et al. Antimalarial exercise of artefenomel (OZ439), a novel artificial antimalarial endoperoxide, in sufferers with Plasmodium falciparum and Plasmodium vivax malaria: an open-label section 2 trial. Lancet Infect. Dis. 16, 61–69 (2016).
Feng, H. et al. Transferrin receptor is a selected ferroptosis marker. Cell Rep. 30, 3411–3423 e3417 (2020).
Shibata, Y., Yasui, H., Higashikawa, Okay. & Kuge, Y. Transferrin-based radiolabeled probe predicts the sensitivity of human renal most cancers cell strains to ferroptosis inducer erastin. Biochem. Biophys. Rep. 26, 100957 (2021).
McCormick, P. N. et al. Evaluation of tumor redox standing by way of (S)-4-(3-[18F]fluoropropyl)-L-glutamic acid PET imaging of system xc− exercise. Most cancers Res. 79, 853–863 (2019).
Hoehne, A. et al. [18F]FSPG-PET reveals elevated cystine/glutamate antiporter (xc-) exercise in a mouse mannequin of a number of sclerosis. J. Neuroinflammation 15, 55 (2018).
Park, S. Y. et al. Scientific analysis of (4S)-4-(3-[18F]fluoropropyl)-L-glutamate (18F-FSPG) for PET/CT imaging in sufferers with newly identified and recurrent prostate most cancers. Clin. Most cancers Res. 26, 5380–5387 (2020).
Park, S. Y. et al. Preliminary analysis of (4S)-4-(3-[18F]fluoropropyl)-L-glutamate (FSPG) PET/CT imaging in sufferers with head and neck most cancers, colorectal most cancers, or non-Hodgkin lymphoma. EJNMMI Res. 10, 100 (2020).
Zeng, F. et al. Ferroptosis MRI for early detection of anticancer drug-induced acute cardiac/kidney accidents. Sci. Adv. 9, eadd8539 (2023).
Zhang, C. et al. Fe-based theranostic brokers reply to the tumor microenvironment for MRI-guided ferroptosis-/apoptosis-inducing anticancer remedy. ACS Biomater. Sci. Eng. 8, 2610–2623 (2022).
Zhu, L. et al. Environment friendly magnetic nanocatalyst-induced chemo- and ferroptosis synergistic most cancers remedy together with T1-T2 dual-mode magnetic resonance imaging by way of doxorubicin supply. ACS Appl. Mater. Interfaces 14, 3621–3632 (2022).
Chen, Q. et al. Iron-based nanoparticles for MR imaging-guided ferroptosis together with photodynamic remedy to reinforce most cancers remedy. Nanoscale 13, 4855–4870 (2021).
Zheng, J. & Conrad, M. The metabolic underpinnings of ferroptosis. Cell Metab. 32, 920–937 (2020).
Bayir, H. et al. Attaining life by way of loss of life: redox biology of lipid peroxidation in ferroptosis. Cell Chem. Biol. 27, 387–408 (2020).
Friedmann Angeli, J. P., Krysko, D. V. & Conrad, M. Ferroptosis on the crossroads of cancer-acquired drug resistance and immune evasion. Nat. Rev. Most cancers 19, 405–414 (2019).
Gu, Y. et al. Focusing on ferroptosis: paving new roads for drug design and discovery. Eur. J. Med. Chem. 247, 115015 (2023).
Wang, D. et al. Regulatory pathways and medicines related to ferroptosis in tumors. Cell Dying Dis. 13, 544 (2022).
Jin, J. et al. Machine studying classifies ferroptosis and apoptosis cell loss of life modalities with TfR1 immunostaining. ACS Chem. Biol. 17, 654–660 (2022).
Shibata, Y., Yasui, H., Higashikawa, Okay., Miyamoto, N. & Kuge, Y. Erastin, a ferroptosis-inducing agent, sensitized most cancers cells to X-ray irradiation through glutathione hunger in vitro and in vivo. PLoS ONE 14, e0225931 (2019).
Liu, W. et al. Ferroptosis inducer improves the efficacy of oncolytic virus-mediated most cancers immunotherapy. Biomedicines 10, 1425 (2022).
Lu, Z. et al. Mixed anti-cancer results of platycodin D and sorafenib on androgen-independent and PTEN-deficient prostate most cancers. Entrance. Oncol. 11, 648985 (2021).
Oh, S. J., Erb, H. H., Hobisch, A., Santer, F. R. & Culig, Z. Sorafenib decreases proliferation and induces apoptosis of prostate most cancers cells by inhibition of the androgen receptor and Akt signaling pathways. Endocr. Relat. Most cancers 19, 305–319 (2012).
Roh, J. L., Kim, E. H., Jang, H. & Shin, D. Aspirin plus sorafenib potentiates cisplatin cytotoxicity in resistant head and neck most cancers cells by way of xCT inhibition. Free. Radic. Biol. Med. 104, 1–9 (2017).
Cobler, L., Zhang, H., Suri, P., Park, C. & Timmerman, L. A. xCT inhibition sensitizes tumors to gamma-radiation through glutathione discount. Oncotarget 9, 32280–32297 (2018).
Nagane, M. et al. Sulfasalazine, an inhibitor of the cystine-glutamate antiporter, reduces DNA harm restore and enhances radiosensitivity in murine B16F10 melanoma. PLoS ONE 13, e0195151 (2018).
Shamaa, M. M. Sulfasalazine synergistically enhances the inhibitory results of imatinib towards hepatocellular carcinoma (HCC) cells by focusing on NFκB, BCR/ABL, and PI3K/AKT signaling pathway-related proteins. FEBS Open. Bio 11, 588–597 (2021).
Chen, C. et al. Flubendazole performs an essential anti-tumor position in several types of cancers. Int. J. Mol. Sci. 23, 519 (2022).
Zhou, X. et al. Flubendazole, FDA-approved anthelmintic, elicits legitimate antitumor results by focusing on P53 and selling ferroptosis in castration-resistant prostate most cancers. Pharmacol. Res. 164, 105305 (2021).
Li, M. et al. RSL3 enhances the antitumor impact of cisplatin on prostate most cancers cells through inflicting glycolysis dysfunction. Biochem. Pharmacol. 192, 114741 (2021).
Wang, J. et al. Inhibition of phosphoglycerate dehydrogenase induces ferroptosis and overcomes enzalutamide resistance in castration-resistant prostate most cancers cells. Drug Resist. Updat. 70, 100985 (2023).
Zhao, R. et al. ATF6ɑ promotes prostate most cancers development by enhancing PLA2G4A-mediated arachidonic acid metabolism and defending tumor cells towards ferroptosis. Prostate 82, 617–629 (2022).
Wang, H. et al. Discovery of ML210-Primarily based glutathione peroxidase 4 (GPX4) degrader inducing ferroptosis of human most cancers cells. Eur. J. Med. Chem. 254, 115343 (2023).
Eling, N., Reuter, L., Hazin, J., Hamacher-Brady, A. & Brady, N. R. Identification of artesunate as a selected activator of ferroptosis in pancreatic most cancers cells. Oncoscience 2, 517–532 (2015).
Luo, J. et al. Artemisinin spinoff artesunate induces radiosensitivity in cervical most cancers cells in vitro and in vivo. Radiat. Oncol. 9, 84 (2014).
Yin, X. et al. Artesunate suppresses the proliferation and improvement of estrogen receptor-alpha-positive endometrial most cancers in HAND2-dependent pathway. Entrance. Cell Dev. Biol. 8, 606969 (2020).
Zhang, Z. Y. et al. [Artesunate combined with vinorelbine plus cisplatin in treatment of advanced non-small cell lung cancer: a randomized controlled trial]. Zhong Xi Yi Jie He Xue Bao 6, 134–138 (2008).
Solar, Y. et al. Fin56-induced ferroptosis is supported by autophagy-mediated GPX4 degradation and capabilities synergistically with mTOR inhibition to kill bladder most cancers cells. Cell Dying Dis. 12, 1028 (2021).
Khalil, R. et al. Withaferin A will increase the effectiveness of immune checkpoint blocker for the remedy of non-small cell lung most cancers. Cancers 15, 3089 (2023).
Kim, S. H. et al. RNA-seq reveals novel mechanistic targets of withaferin A in prostate most cancers cells. Carcinogenesis 41, 778–789 (2020).
Kyakulaga, A. H., Aqil, F., Munagala, R. & Gupta, R. C. Synergistic combos of paclitaxel and withaferin A towards human non-small cell lung most cancers cells. Oncotarget 11, 1399–1416 (2020).
Nishikawa, Y. et al. Withaferin A induces cell loss of life selectively in androgen-independent prostate most cancers cells however not in regular fibroblast cells. PLoS ONE 10, e0134137 (2015).
Yang, E. S., Choi, M. J., Kim, J. H., Choi, Okay. S. & Kwon, T. Okay. Mixture of withaferin A and X-ray irradiation enhances apoptosis in U937 cells. Toxicol. Vitr. 25, 1803–1810 (2011).
Kristensen, G. B., Baekelandt, M., Vergote, I. B. & Trope, C. A section II examine of carboplatin and hexamethylmelamine as induction chemotherapy in superior epithelial ovarian carcinoma. Eur. J. Most cancers 31A, 1778–1780 (1995).
Malik, I. A. Altretamine is an efficient palliative remedy of sufferers with recurrent epithelial ovarian most cancers. Jpn. J. Clin. Oncol. 31, 69–73 (2001).
Woo, J. H. et al. Elucidating compound mechanism of motion by community perturbation evaluation. Cell 162, 441–451 (2015).
Wang, L., Chen, X. & Yan, C. Ferroptosis: an rising therapeutic alternative for most cancers. Genes. Dis. 9, 334–346 (2022).
Qin, Z. et al. Design and synthesis of isothiocyanate-containing hybrid androgen receptor (AR) antagonist to downregulate AR and induce ferroptosis in GSH-deficient prostate most cancers cells. Chem. Biol. Drug. Des. 97, 1059–1078 (2021).
Li, Q. et al. The consequences of buthionine sulfoximine on the proliferation and apoptosis of biliary tract most cancers cells induced by cisplatin and gemcitabine. Oncol. Lett. 11, 474–480 (2016).
Bump, E. A. & Brown, J. M. Function of glutathione within the radiation response of mammalian cells in vitro and in vivo. Pharmacol. Ther. 47, 117–136 (1990).
Guo, J. et al. Ferroptosis: a novel anti-tumor motion for cisplatin. Most cancers Res. Deal with. 50, 445–460 (2018).
Efferth, T. Most cancers mixture therapies with artemisinin-type medication. Biochem. Pharmacol. 139, 56–70 (2017).
Sundar, S. N., Marconett, C. N., Doan, V. B., Willoughby, J. A. Sr & Firestone, G. L. Artemisinin selectively decreases useful ranges of estrogen receptor-ɑ and ablates estrogen-induced proliferation in human breast most cancers cells. Carcinogenesis 29, 2252–2258 (2008).
Wang, T. et al. Mixture remedy with artemisinin and oxaliplatin inhibits tumorigenesis in esophageal most cancers EC109 cell by way of Wnt/β-catenin signaling pathway. Thorac. Most cancers 11, 2316–2324 (2020).
Willoughby, J. A. Sr. et al. Artemisinin blocks prostate most cancers development and cell cycle development by disrupting Sp1 interactions with the cyclin-dependent kinase-4 (CDK4) promoter and inhibiting CDK4 gene expression. J. Biol. Chem. 284, 2203–2213 (2009).
Dai, X. et al. Dihydroartemisinin: a possible pure anticancer drug. Int. J. Biol. Sci. 17, 603–622 (2021).
Han, W. et al. Co-delivery of dihydroartemisinin and pyropheophorbide-iron elicits ferroptosis to potentiate most cancers immunotherapy. Biomaterials 280, 121315 (2022).
Li, Q. et al. Dihydroartemisinin as a sensitizing agent in most cancers therapies. Onco Targets Ther. 14, 2563–2573 (2021).
Lin, R. et al. Dihydroartemisinin (DHA) induces ferroptosis and causes cell cycle arrest in head and neck carcinoma cells. Most cancers Lett. 381, 165–175 (2016).
Abrams, R. P., Carroll, W. L. & Woerpel, Okay. A. 5-membered ring peroxide selectively initiates ferroptosis in most cancers cells. ACS Chem. Biol. 11, 1305–1312 (2016).
Gaschler, M. M. et al. FINO2 initiates ferroptosis by way of GPX4 inactivation and iron oxidation. Nat. Chem. Biol. 14, 507–515 (2018).
Saha, A. et al. Cysteine depletion sensitizes prostate most cancers cells to brokers that improve DNA harm and to immune checkpoint inhibition. J. Exp. Clin. Most cancers Res. 42, 119 (2023).
Badgley, M. A. et al. Cysteine depletion induces pancreatic tumor ferroptosis in mice. Science 368, 85–89 (2020).

