Skip to main content

Ferroptosis induction as a strategy to treat pancreatic cancer

Resisting cell death, an original hallmark of cancer, is necessary for cancer growth. As a result, many therapeutic approaches have been made to induce cancer specific induction of cell death. This is especially important in pancreatic cancer, in which new targets are critically needed for this highly lethal cancer. There a multiple types of cancer cell death, for example, the caspase-dependent apoptosis, necroptosis, and pyroptosis and the lysosomal dependent autophagy. But today we are going to focus on the iron-dependent pathway ferroptosis.  

Ferroptosis is characterized by iron dependency and lipid reactive oxygen species (ROS) accumulation. This pathway was first discovered in 2012 by the Stockwell group in which they observed that the small molecule erastin induced a non-apoptotic form of cell death in the N-ras mutated fibrosarcoma cell line HT-1080 and that they could recover cell death via inhibition using the novel ferroptosis inhibitor ferrostatin-1. Ferrostatin-1 was also discovered to be neuroprotective, preventing glutamate-induced neurotoxicity. This led the researchers to question if either calcium influx or decreased cystine, oxidized cysteine, uptake were involved as these processes have been known to be initiators for glutamate-induced cell death. They discovered that inhibition of cystine uptake by multiple methods (erastin, SAS, or glutamate), but not calcium influx, could trigger ferroptosis and that promotion of cystine uptake could rescue iron-dependent cell death in cancer cells. Additionally, it has been shown that deletion of the cystine xc- gene Slc7a11 has no major toxicity in unstressed mice, further suggesting this could be a good target.

Most pancreatic ductal adenocarcinoma (PDAC) cases, more than 90%, have mutated KRAS, which has been shown in many studies to induce increased production of reactive oxygen species through increased cellular proliferation and reprogramming of cellular metabolism. Normal cells would die under high ROS levels, but cancer cells can counteract high levels of ROS via upregulating detoxifying metabolites like glutathione. Glutathione, a tripeptide of L-glutamate, cysteine, and glycine, has been shown to increase cancer cell resistance to oxidative stress. Additionally, the oxidized cystine has been shown to regulate intracellular GSH metabolism, further strengthening its role in ROS detoxification. 

Recently, Badgley et al. discovered that genetic and pharmacological depletion of cystine levels can induce ferroptosis in pancreatic cancer models to inhibit tumor growth. They hypothesized that import of cystine is important for PDAC cells to survive under high oxidative stress and could be a good therapeutic target. In this study, they used a chemically enhanced erastin analog imidazole ketone erastin (IKE) that has been modified to increase water solubility, metabolic stability, potency, and selectivity. In vitro, IKE treatment reduced cell viability in four out of five PDAC cell lines tested mimicking cystine starvation, with neither method inducing caspase 3 cleavage. 

They also examined the effect of reduced cystine transport in vivo by modifying the commonly used KPC mouse to delete the cystine transport gene Slc7a11 upon tamoxifen induction (KPFSR). Median survival time was doubled in tamoxifen treated mice compared to the control and this survival extension was reversed upon addition of the cysteine analog NAC further suggesting the increase in survival is linked to cysteine metabolism. Prior to this paper, there was no in vivo characterization of ferroptosis, but the authors observed distinct histopathological markers in the KPSFR mouse model. Additionally, they performed RNA sequencing on malignant cells and observed enrichment in the ferroptotic gene signature from the previously mentioned erastin treated HT-10800 cells. 

Drug delivery has always been a problem in PDAC due to extensive fibrosis and decreased tissue perfusion. To deplete cystine levels pharmacologically, the authors used the engineered enzyme cyst(e)inase, which has a favorable half-life and stability in vivo and has been shown to degrade both cystine and cysteine. Cyst(e)inase treatment in the KPC mouse model revealed similar histopathology to the KPFSR mouse and all four tumors treated with 100 mg/kg cyst(e)inase exhibited stabilized tumors. 

Further work is necessary to achieve a small molecule with ideal cystine depletion and ideal drug delivery in PDAC, but this work suggests that induction of ferroptosis in pancreatic cancer has selective anticancer activity both in vivo and in vitro. Additionally, this work provides a histopathological characterization of ferroptosis in vivo. 

REFERENECES:

Badgley MA, Kremer DM, Maurer HC, et al. Cysteine depletion induces pancreatic tumor ferroptosis in mice. Science. 2020;368(6486):85-89. doi:10.1126/science.aaw9872

Dixon SJ, Lemberg KM, Lamprecht MR, et al. Ferroptosis: an iron-dependent form of nonapoptotic cell death. Cell. 2012;149(5):1060–1072. doi:10.1016/j.cell.2012.03.042


Ye Z, Liu W, Zhuo Q, et al. Ferroptosis: Final destination for cancer?. Cell Prolif. 2020;53(3):e12761. doi:10.1111/cpr.12761

Comments

Popular posts from this blog

Photoswitchable azopyrazoles Flipping the Switches of Ion Channels

Abnormally activated Ca 2+ channels are related to many human diseases, including Stormorken Syndrome, which makes Ca 2+ release-activated Ca 2+ (CRAC) channel a very promising therapeutic target. Several small molecule therapeutics targeting CRAC channels have been developed, including the GSKs series and Synta 66 . Those compounds have relatively high specificity. Meanwhile, a controllable system that can be activated with a switch can probably serve as a convenient tool for further related research.    Photoswitchable chemistry has been applied to a lot of bioactive targets such as ion channels, receptors enzymes and nucleic acids. Recently, the Li group developed CRAC channel inhibitors that can be turned ‘on’ and ‘off’ by UV-light exposure. Scheme 1 . C onverting CRAC channel inhibitors, GSKs , into photoswitchable derivatives, piCRACs . Starting from the well-established GSK-based CRAC inhibitor ( Scheme 1 ), the authors developed a series of nitrosaniline

Proteosome Inhibition Taps Into RNA Splicing

Multiple myeloma (MM) is a malignancy of white blood cells called plasma cells that reside mainly in the bone marrow and is the second most common blood cancer. With increased understanding of biology, the current use of immunomodulatory (IM) drugs and proteasome inhibitors (PI) have taken over the therapeutic landscape for MM. The combination of bortezomib (PI) with lenalidomiede (IM) and dexamethasone is commonly the initial treatment of choice. Early intervention seems to provide a good outcome, but unfortunately, many patients eventually relapse. A major goal in MM treatment is to increase the efficacy of proteasome inhibitors and prevent relapse. To investigate this, Huang et al. used unbiased mass spectrometry-based phosphoproteomics to identify potential vulnerabilities after treatment with the PI carfilzomib and discovered that splicing related proteins had significant changes in phosphorylation that is undetectable upon examination of RNA and protein abundance. Treatment w

One Fluorine Atom Fixes Poor KRAS Inhibitors

KRAS  is the most frequently mutated oncogene in human cancer. In the past few decades, the KRAS oncoprotein had always been deemed as an “undruggable target” due to lack of binding surface and tightly binding to its substrate GTP. In 2013, the Shokat group identified that the mutant cysteine KRAS G12C creates a new allosteric pocket “switch-II pocket” which can be exploited to design covalent inhibitors. KRAS G12C accounts for more than 50% of the incidences of KRAS mutations, involving in many cancers, such as non-small cell lung cancer (NSCLC), colorectal adenocarcinomas and pancreatic cancer. KARS G12C has been an attractive target for drug discovery and development in both academia and industry. MRTX849 is a potent, orally available covalent inhibitor of KRAS G12C developed by Mirati Therapeutics and currently undergoing Phase I/II clinical trials. Recently, a paper published in Journal of Medicinal Chemistry reported the design and optimization of MRTX849 . The medi