Search bioRxiv⌕ Search

Biology subjects

Berra, E.

Publications and source records attributed to Berra, E..

3 recordsLinked to original sources

Secreted spermidine synthase reveals a paracrine role for PGC1a-induced growth suppression in prostate cancer

Prostate cancer is the fifth cause of death by cancer worldwide, second in incidence in the male population. The definition of the molecular basis of its development and the oncogenic signals driving lethality continue to be important objectives in prostate cancer research. Prior work from others and us has demonstrated that loss of PGC1 expression results in a metabolic, signaling and transcriptional reprogramming that supports the development of metastatic disease. However, we do not fully understand the spectrum of tumor suppressive effects regulated by this co-regulator. Here we show that PGC1 governs non-cell autonomous paracrine tumor suppression in prostate cancer. A systematic analysis of the transcriptional landscapes associated to PGC1 loss of expression revealed that PGC1 alters the expression of genes encoding for secreted proteins. Cell secretome studies corroborated that PGC1-dependent ERR regulation in prostate cancer cells suppresses the growth of tumor cells exposed to their conditioned media. The integration of in vitro and in vivo secretomics data and genetic perturbation assays revealed spermidine synthase as a transcriptional target of PGC1 and mediator of a paracrine metabolic growth suppressive effect. Moreover, the activity of the regulatory axis PGC1-ERR-SRM was reflected in patients and had prognostic value. Altogether, this work provides unprecedented evidence of the non-cell autonomous tumor suppression role of PGC1, which broadens the view of this co-regulator as a multifactorial tumor suppressor in prostate cancer.

cancer biology↗

A rise in double-strand breaks sensitizes tumours to oxidative metabolism inhibitors

ABSTRACTDouble strand brakes (DSB) accumulate in cellular DNA as a result of deficiencies in homologous recombination repair systems, such as mutations in BRCA genes, or upon antitumoral treatments. In the present study we show that the accumulation of DSB, regardless of its origins, leads to a shift towards oxidative metabolism. We have identified that DSB-induced reactive oxygen species (ROS) promote the activation of NRF2 which downregulates the glycolytic transcription factor HIF-1. HIF-1 inhibition is a key step in this metabolic shift, because leads to the reduction of PDHK1 levels and the consequential activation of pyruvate dehydrogenase, a mitochondrial gatekeeper of cellular metabolism, promoting this metabolic shift. Remarkably, after the induction of DSBs, the tumour is more sensitive to the inhibition of oxidative metabolism since both treatments synergize in vivo, resulting in reduced tumour growth. Therefore, we demonstrate a significant feedback between DSBs induction and cancer cell metabolism that ultimately limits the cells potential for metabolic plasticity, hence sensitizing it to the action of counteracting drugs.

cancer biology↗

USP29 is a novel non-canonical Hypoxia Inducible Factor-α activator

Hypoxia Inducible Factor (HIF) is the master transcriptional regulator that orchestrates cellular adaptation to low oxygen. HIF is tightly regulated via the stability of its -subunit, which is subjected to oxygen-dependent proline hydroxylation by Prolyl-Hydroxylase Domain containing proteins (PHDs/EGLNs), and ultimately targeted for proteasomal degradation through poly-ubiquitination by von-Hippel-Lindau protein (pVHL). However, sustained HIF- signalling is found in many tumours independently of oxygen availability pointing towards the relevance of non-canonical HIF- regulators. In this study, we establish the Ubiquitin Specific Protease 29 (USP29) as direct post-translational activator of HIF- in a variety of cancer cell lines. USP29 binds to HIF-, decreases poly-ubiquitination and thus protects HIF- from proteasomal degradation. Deubiquitinating activity of USP29 is essential to stabilise not only HIF-1 but also HIF-2, via their C-termini in an oxygen/PHD/pVHL-independent manner. Furthermore, in prostate cancer samples the expression of USP29 correlates with the HIF-target gene CA9 (carbonic anhydrase 9) as well as disease progression and severity.

cell biology↗