The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.
Activation of SAT1 engages polyamine metabolism with p53-mediated ferroptotic responses
Open accessAbstract
Significance: Although it is commonly accepted that p53-mediated cell-cycle arrest, apoptosis, and senescence all serve as major mechanisms of tumor suppression, accumulating evidence indicates that other activities of p53, such as ferroptosis, are also critical for tumor suppression. However, the molecular mechanisms by which p53-mediated ferroptosis operates are not completely understood. In this study, we discovered that p53 can execute ferroptotic cell-death responses by directly activating its target gene SAT1 , coded for the spermidine/spermine N 1 -acetyltransferase 1. These data indicate a regulatory role of p53 in polyamine metabolism and reveal that p53-mediated activation of SAT1 contributes significantly to ferroptotic responses. Thus, p53 may engage multiple metabolic pathways with ferroptotic cell-death responses for tumor suppression.
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“Furthermore, the expression of SAT1 is associated with arachidonate 15-lipoxygenase (ALOX15) levels, and PD146176, an ALOX15 inhibitor, suppresses ferroptosis induced by SAT1.127”
From p53: from understanding its structure to advances in therapeutic targeting (2026) · cites this paper as [127]
In the citing paper
“p53 can also activate the expression of SAT1, a rate-limiting enzyme in polyamine catabolism, thereby inducing lipid peroxidation and ferroptosis upon ROS stress.130”
From Targeting p53 pathways: mechanisms, structures, and advances in therapy (2023) · cites this paper as [130]
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Regulation of Ferroptotic Cancer Cell Death by GPX4
Yang, W. S., SriRamaratnam, R., Welsch, M. E., Shimada, K., Skouta, R., Viswanathan, V. S., Cheah, J. H., Clemons, P. A., Shamji, A. F., Clish, C. B., et al. (2014) · Cell · doi:10.1016/j.cell.2013.12.010 · Cited by 7,713
Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607
Lane, D. P. (1992) · Nature · doi:10.1038/358015a0 · Cited by 5,138
In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661
Mice deficient for p53 are developmentally normal but susceptible to spontaneous tumours
Donehower, L. A., Harvey, M., Slagle, B. L., McArthur, M. J., Montgomery, C. A., Butel, J. S., & Bradley, A. (1992) · Nature · doi:10.1038/356215a0 · Cited by 4,649
Ferroptosis as a p53-mediated activity during tumour suppression
Jiang, L., Kon, N., Li, T., Wang, S.-J., Su, T., Hibshoosh, H., Baer, R., & Gu, W. (2015) · Nature · doi:10.1038/nature14344 · Cited by 3,398
Self-citationMetabolic Reprogramming: A Cancer Hallmark Even Warburg Did Not Anticipate
Ward, P. S., & Thompson, C. B. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.02.014 · Cited by 3,233
Blinded by the Light: The Growing Complexity of p53
Vousden, K. H., & Prives, C. (2009) · Cell · doi:10.1016/j.cell.2009.04.037 · Cited by 3,163
Cancer cell metabolism: warburg and beyond
Hsu, P. P., & Sabatini, D. M. (2008) · Cell · doi:10.1016/j.cell.2008.08.021 · Cited by 2,452
The first 30 years of p53: growing ever more complex.
Levine, A. J., & Oren, M. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2723 · Cited by 1,967
Cited by
Ferroptosis: A Regulated Cell Death Nexus Linking Metabolism, Redox Biology, and Disease
Stockwell, B. R., Friedmann Angeli, J. P., Bayir, H., Bush, A. I., Conrad, M., Dixon, S. J., Fulda, S., Gascón, S., Hatzios, S. K., Kagan, V. E., et al. (2017) · Cell · doi:10.1016/j.cell.2017.09.021 · Cited by 7,695
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680
Ferroptosis: past, present and future
Li, J., Cao, F., Yin, H.-L., Huang, Z.-J., Lin, Z.-T., Mao, N., Sun, B., & Wang, G. (2020) · Cell Death & Disease · doi:10.1038/s41419-020-2298-2 · Cited by 4,171
Targeting Ferroptosis as a Vulnerability in Cancer
Lei, G., Zhuang, L., & Gan, B. (2022) · Nature reviews. Cancer · doi:10.1038/s41568-022-00459-0 · Cited by 2,252
Ferroptosis: machinery and regulation
Chen, X., Li, J., Kang, R., Klionsky, D. J., & Tang, D. (2021) · Autophagy · doi:10.1080/15548627.2020.1810918 · Cited by 2,099
Metadata
- Authors
- Ou, Y., Wang, S.-J., Li, D., Chu, B., & Gu, W.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2016-10-03
- Volume
- 113
- Issue
- 44
- Pages
- E6806-E6812
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2527907612
- Cited by
- 765
- References
- 11
- FWCI
- 16.42
- Type
- journal article
- Language
- en
- Open access
- green
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- Ou, Y., Wang, S.-J., Li, D., Chu, B., & Gu, W. (2016). Activation of SAT1 engages polyamine metabolism with p53-mediated ferroptotic responses. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1607152113
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