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nature portfolio privacy policy hrasg12v-inducible nih-3t3 cells cdna libraries amplified editing x-ray films cl-xposure™ bz-h4m/measurement application software advertising author information authors silvia von karstedt nih-3t3 krasg12v cells oncogenic-ras-harboring cancer cells german research foundation nrf2-dependent antioxidant response reprints nature nano-esi-ms/ms middle covalent g12c-specific inhibitor cancer research nonsense-mediated mrna decay loxp-flanked kras gene goat-anti-rabbit-hrp goat-anti-rat-hrp nonsense-mediated rna decay cystine/glutamate antiporter xct human kras-driven cancers goat-anti-mouse-hrp genotype-selective antitumor agents lc-esi-ms/ms lsl-krasg12d-inducible mefs including ether-linked species ros-induced cell death fatma isil yapici wt kras-expressing clones ripk1 inhibitor nec-1s endogenous radical-trapping agents cell-line selectivity improves s-appt induces ferroptosis von karstedt lab original author medical research cancer cell-autonomous trail human glucose‐6‐phosphate dehydrogenase hundred microliters opti-mem stabilizing pd-l1 mrna flag-tagged kras kras-mutant cells decreased author correspondence poor relapse-free survival

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         headline:Elevated FSP1 protects KRAS-mutated cells from ferroptosis during tumor initiation
         description:Oncogenic KRAS is the key driver oncogene for several of the most aggressive human cancers. One key feature of oncogenic KRAS expression is an early increase in cellular reactive oxygen species (ROS) which promotes cellular transformation if cells manage to escape cell death, mechanisms of which remain incompletely understood. Here, we identify that expression of oncogenic as compared to WT KRAS in isogenic cellular systems renders cells more resistant to ferroptosis, a recently described type of regulated necrosis. Mechanistically, we find that cells with mutant KRAS show a specific lack of ferroptosis-induced lipid peroxidation. Interestingly, KRAS-mutant cells upregulate expression of ferroptosis suppressor protein 1 (FSP1). Indeed, elevated levels of FSP1 in KRAS-mutant cells are responsible for mediating ferroptosis resistance and FSP1 is upregulated as a consequence of MAPK and NRF2 pathway activation downstream of KRAS. Strikingly, FSP1 activity promotes cellular transformation in soft agar and its overexpression is sufficient to promote spheroid growth in 3D in KRAS WT cells. Moreover, FSP1 expression and its activity in ferroptosis inhibition accelerates tumor onset of KRAS WT cells in the absence of oncogenic KRAS in vivo. Consequently, we find that pharmacological induction of ferroptosis in pancreatic organoids derived from the LsL-KRASG12D expressing mouse model is only effective in combination with FSP1 inhibition. Lastly, FSP1 is upregulated in non-small cell lung cancer (NSCLC), colorectal cancer (CRC) and pancreatic ductal adenocarcinoma (PDAC) as compared to the respective normal tissue of origin and correlates with NRF2 expression in PDAC patient datasets. Based on these data, we propose that KRAS-mutant cells must navigate a ferroptosis checkpoint by upregulating FSP1 during tumor establishment. Consequently, ferroptosis-inducing therapy should be combined with FSP1 inhibitors for efficient therapy of KRAS-mutant cancers.
         datePublished:2022-11-29T00:00:00Z
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      headline:Elevated FSP1 protects KRAS-mutated cells from ferroptosis during tumor initiation
      description:Oncogenic KRAS is the key driver oncogene for several of the most aggressive human cancers. One key feature of oncogenic KRAS expression is an early increase in cellular reactive oxygen species (ROS) which promotes cellular transformation if cells manage to escape cell death, mechanisms of which remain incompletely understood. Here, we identify that expression of oncogenic as compared to WT KRAS in isogenic cellular systems renders cells more resistant to ferroptosis, a recently described type of regulated necrosis. Mechanistically, we find that cells with mutant KRAS show a specific lack of ferroptosis-induced lipid peroxidation. Interestingly, KRAS-mutant cells upregulate expression of ferroptosis suppressor protein 1 (FSP1). Indeed, elevated levels of FSP1 in KRAS-mutant cells are responsible for mediating ferroptosis resistance and FSP1 is upregulated as a consequence of MAPK and NRF2 pathway activation downstream of KRAS. Strikingly, FSP1 activity promotes cellular transformation in soft agar and its overexpression is sufficient to promote spheroid growth in 3D in KRAS WT cells. Moreover, FSP1 expression and its activity in ferroptosis inhibition accelerates tumor onset of KRAS WT cells in the absence of oncogenic KRAS in vivo. Consequently, we find that pharmacological induction of ferroptosis in pancreatic organoids derived from the LsL-KRASG12D expressing mouse model is only effective in combination with FSP1 inhibition. Lastly, FSP1 is upregulated in non-small cell lung cancer (NSCLC), colorectal cancer (CRC) and pancreatic ductal adenocarcinoma (PDAC) as compared to the respective normal tissue of origin and correlates with NRF2 expression in PDAC patient datasets. Based on these data, we propose that KRAS-mutant cells must navigate a ferroptosis checkpoint by upregulating FSP1 during tumor establishment. Consequently, ferroptosis-inducing therapy should be combined with FSP1 inhibitors for efficient therapy of KRAS-mutant cancers.
      datePublished:2022-11-29T00:00:00Z
      dateModified:2022-11-29T00:00:00Z
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      keywords:
         Cell biology
         Oncogenes
         Life Sciences
         general
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         Cell Biology
         Stem Cells
         Apoptosis
         Cell Cycle Analysis
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            address:
               name:University of Cologne, Faculty of Medicine and University Hospital Cologne, Department of Translational Genomics, Cologne, Germany
               type:PostalAddress
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            address:
               name:CECAD Cluster of Excellence, University of Cologne, Cologne, Germany
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            address:
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      name:CECAD Cluster of Excellence, University of Cologne, Cologne, Germany
      name:University of Cologne, Faculty of Medicine and University Hospital Cologne, Department of Translational Genomics, Cologne, Germany
      name:CECAD Cluster of Excellence, University of Cologne, Cologne, Germany
      name:University of Cologne, Faculty of Medicine and University Hospital Cologne, Department of Translational Genomics, Cologne, Germany
      name:CECAD Cluster of Excellence, University of Cologne, Cologne, Germany
      name:University of Cologne, Faculty of Medicine and University Hospital Cologne, Department of Translational Genomics, Cologne, Germany
      name:CECAD Cluster of Excellence, University of Cologne, Cologne, Germany
      name:University of Cologne, Faculty of Medicine and University Hospital Cologne, Department of Translational Genomics, Cologne, Germany
      name:CECAD Cluster of Excellence, University of Cologne, Cologne, Germany
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      name:CECAD Cluster of Excellence, University of Cologne, Cologne, Germany
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      name:University of Cologne, Faculty of Medicine and University Hospital Cologne, Department of Translational Genomics, Cologne, Germany
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      name:CECAD Cluster of Excellence, University of Cologne, Cologne, Germany
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