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Edinger, A.

Publications and source records attributed to Edinger, A..

2 recordsLinked to original sources

Mevalonate Biosynthesis is a Metabolic Vulnerability of Gemcitabine-resistant Pancreatic Cancer

Pancreatic ductal adenocarcinoma (PDAC) is a lethal malignancy with a devastating prognosis. Gemcitabine, a pyrimidine anti-metabolite, is a cornerstone in PDAC therapy. However, resistance remains a major hurdle in clinical care. Resistance can arise from microenvironmental metabolites or through direct metabolic reprogramming of pancreatic cancer cells. Here, we generated PDAC models of acquired gemcitabine resistance to determine the relationship between these mechanisms. We observed that physiological levels of exogenous pyrimidines have a diminished ability to impact gemcitabine response in PDAC cells with acquired resistance. This occurs as the metabolic reprogramming of PDAC cells in response to gemcitabine treatment forces a suppression of the pyrimidine salvage pathway. Importantly, this metabolic rewiring renders gemcitabine-resistant PDAC cells highly susceptible to inhibition of the rate limiting enzyme of the mevalonate biosynthesis pathway, 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR), using statins. Notably, statin treatment inhibits the growth of gemcitabine-resistant tumors in immunocompetent mouse models. Through metabolite rescue experiments, we identified geranylgeranyl pyrophosphate as the critical metabolite lost during statin treatment, resulting in reduced protein geranylation in PDAC cells. Finally, as downregulation of the HMGCR is gradually acquired during gemcitabine resistance, we observed that HMGCR expression predicts patient response to gemcitabine. Collectively, these data demonstrate that the mevalonate biosynthesis pathway represents a promising therapeutic target in gemcitabine resistance and may serve as a biomarker to stratify treatment selection in PDAC patients.

cancer biology↗

Rab7a activation promotes degradation of select tight junction proteins at the blood-brain barrier after ischemic stroke

Adherens (AJ) and tight junction (TJ) integrity is critical for blood-brain barrier (BBB) function in the healthy brain. Junction disassembly due to degradation of AJ and TJ proteins leads to acute BBB dysfunction after ischemic stroke, but the mechanisms are not fully understood. Here, we show that endothelial cell deletion of Rab7a, a small GTPase crucial for protein degradation through the endolysosomal system, reduces acute BBB dysfunction and improves neuronal health in mice after ischemic stroke by preventing degradation of select junctional proteins and preserving TJ structural morphology. Two pro-inflammatory cytokines, TNF and IL1{beta}, that trigger barrier disruption in brain endothelial cells (BECs) in vitro and are upregulated in stroke, contribute to Rab7a activation. Silencing Rab7a in vitro partially rescues cytokine-driven barrier disruption in BECs by reducing internalization of some junctional proteins and the formation of F-actin bundles at cell junctions. Rab7a is, therefore, critical for degradation of select junctional proteins during the acute BBB damage after ischemic stroke.

cell biology↗