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Giglio, P.

Publications and source records attributed to Giglio, P..

4 recordsLinked to original sources

BNIP3-mTOR Signaling Mediates Resistance to MET Inhibition in Glioblastoma

Glioblastoma (GBM) is an aggressive primary brain malignancy with poor prognosis due to rapid progression, extensive invasiveness, and intrinsic resistance to standard therapies. Aberrant activation of receptor tyrosine kinases (RTKs), particularly MET, drives tumor proliferation, invasion, and therapy resistance. Here, we show that MET inhibition with crizotinib induces senescence and mitochondrial dysfunction in glioma-initiating cells (GICs), in part via downregulation of the mitochondrial protein BNIP3. However, BNIP3 downregulation activates mTOR signaling, enabling adaptive resistance. Targeting mTOR with everolimus in combination with crizotinib synergistically enhances anti-tumor effects, inducing apoptosis, senescence, and necroptosis, and significantly reducing cell viability and sphere-forming capacity. In orthotopic GBM xenograft models, this combination, particularly in a sequential regimen, markedly prolongs survival without overt toxicity. Our findings identify a BNIP3-mTOR signaling axis as a critical mediator of resistance to MET inhibition and provide a mechanistic rationale for combined MET and mTOR targeting as a promising therapeutic strategy in GBM. Statement of Translational RelevanceGlioblastoma (GBM) remains a highly aggressive and treatment-resistant brain tumor with limited therapeutic options. Our study identifies a BNIP3-mTOR signaling axis as a key mediator of resistance to MET inhibition. We show for the first time that combined MET and mTOR inhibition exhibits synergistic effects against GBM in vitro and in vivo. This combination prolongs survival without overt toxicity, providing a strong preclinical rationale for clinical evaluation in GBM patients with high MET expression and offering a promising strategy to overcome adaptive resistance.

cancer biology↗

A Human Neuronal Co-Culture System Reveals Early Tumor-Neuron Communication and Targetable Pathways in Glioblastoma

BackgroundGlioblastoma (GB, IDH wild type) is the most aggressive primary brain tumor in adults, with recurrence driven by residual tumor cells that re-establish interaction with surrounding neurons. While neuronal activity is recognized as a driver of GB progression, the earliest neuronal responses to tumor contact remain poorly understood. Existing models rarely capture these acute events or the heterogeneity of responses generated by tumors of different origins, limiting insight into the earliest neuron-tumor interactions. MethodsWe developed a dual-interface human iPSC-derived neuronal culture system to investigate acute neuronal responses to glioblastoma exposure. Neurons were challenged with either established GB cell lines or patient-derived glioblastoma cells (PDGCs). Using quantitative proteomics, high-resolution imaging, and immunological assays, we characterized compartment-specific neuronal changes and mapped activated signaling pathways. We also screened selective inhibitors for their effects on both tumor proliferation and neuronal integrity. FindingsWithin 24 hours of exposure, neurons displayed synaptic remodeling and activation of GB-related signaling cascades. Proteomic analysis of GB exposed neurons revealed enrichment of pathways associated with GB and abnormalities in neuronal circuits. Notably, the U-87MG cell line, but not PDGCs, induced pronounced synaptic disruption, neurite retraction, and MAPK pathway activation, with distinct molecular signatures across neuronal compartments. ERK1/2 and p38 MAPK signaling were differentially activated depending on the GB cells source, correlating with specific structural and functional synaptic alterations. Targeted inhibition of MAPK components significantly suppressed U-87MG proliferation and preserved neuronal architecture. InterpretationWe present a human neuronal culture model that detects and discriminates the earliest neuron-derived responses to glioblastoma from diverse tumor sources. By linking neuronal remodeling to tumor-specific signaling pathways, the platform uncovers both the heterogeneity of neuron-tumor interactions and early, targetable vulnerabilities. This system offers a translational tool to advance understanding of GB recurrence and to guide development of therapies with dual neuroprotective and anti-tumor efficacy. In BriefEarly interactions between glioblastoma and human neurons drive rapid, source-specific synaptic remodeling mediated by compartmental MAPK pathway activation. This neuronal co-culture model identifies distinct profiles of tumor-neuron communication, highlights synaptic vulnerability as a therapeutic axis, and demonstrates that MAPK pathway inhibition yields both neuroprotective and anti-tumor effects. SummaryGlioblastoma (GB) co-opts neuronal circuits to drive tumor progression, yet the earliest neuronal responses that may shape recurrence remain poorly defined. We developed a human iPSC-derived neuronal co-culture model that captures acute communication between neurons and glioblastoma from diverse sources, including serum-adapted cell lines and patient-derived cells. Within 24 hours, glioma-exposed neurons exhibited synaptic remodeling and activation of tumor-associated signaling pathways. High-resolution imaging and proteomics revealed compartment-specific synaptic alterations, with ERK1/2 and p38 MAPK signaling differentially engaged depending on the tumor source, corresponding to distinct structural and functional outcomes. Pharmacologic inhibition of MAPK components both suppressed tumor cells growth and preserved neuronal integrity. By modeling source-dependent and early neuron-tumor interactions, this platform not only identifies MAPK signaling as a critical mediator of synaptic vulnerability but also provides a clinically relevant tool for investigating the mechanisms of glioblastoma recurrence. It offers a framework for developing therapies that target the dual vulnerabilities of tumor progression and circuit remodeling. Highlights O_LIA dual-interface human iPSC-derived neuronal co-culture system models early neuron-glioblastoma (GB) interaction. C_LIO_LISerum-adapted U-87MG, but not serum-free patient-derived GB cells, induces pronounced synaptic disruption and neurite retraction. C_LIO_LIGlobal proteome of neurons reveals GB-associated signatures and neuronal circuit alterations in response to both U-87MG and patient-derived GB cells. C_LIO_LIERK1/2 and p38 MAPK signaling are differentially activated in neuronal compartments, depending on GB source. C_LIO_LIMAPK pathway inhibition suppresses U-87MG proliferation and preserves neuronal integrity, revealing actionable neuroprotective and anti-tumor targets. C_LI

cancer biology↗

Disulfide-mediated tetramerization of TRAP1 fosters its antioxidant and pro-neoplastic activities.

The mitochondrial chaperone TRAP1 exerts a protective function in cells exposed to diverse stress conditions in both physiological and pathological contexts. In cancer cells, it contributes to neoplastic progression ensuing metabolic rewiring and protection from oxidative insults. TRAP1 works as a homodimer, but recent evidence has indicated that it can form tetramers whose functional effects remain elusive. Here, we find that TRAP1 forms redox-sensitive tetramers via disulfide bonds involving two critical cysteine residues, C261 and C573. TRAP1 tetramerization is elicited by oxidative stress and abrogated upon expression of the double C261S/C573R mutant. In cancer contexts, the expression of the TRAP1 C261S/C573R mutant is unable to inhibit the activity of its client succinate dehydrogenase and to confer protection against oxidative insults, and it hampers invasiveness of aggressive sarcoma cells. Our data indicate that TRAP1 undergoes tetramerization in response to oxidative stress and identify C261 and C573 as critical for TRAP1 structural rearrangement and for functions.

cell biology↗

S-nitrosylation affects TRAP1 structure and ATPase activity and modulates cell response to apoptotic stimuli

The mitochondrial chaperone TRAP1 has been involved in several mitochondrial functions, and modulation of its expression/activity has been suggested to play a role in the metabolic reprogramming distinctive of cancer cells. TRAP1 posttranslational modifications, i.e. phosphorylation, can modify its capability to bind to different client proteins and modulate its oncogenic activity. Recently, it has been also demonstrated that TRAP1 is S-nitrosylated at Cys501, a redox modification associated with its degradation via the proteasome. Here we report molecular dynamics simulations of TRAP1, together with analysis of long-range structural communication, providing a model according to which Cys501 S-nitrosylation induces conformational changes to distal sites in the structure of the protein. The modification is also predicted to alter open and closing motions for the chaperone function. By means of colorimetric assays and site directed mutagenesis aimed at generating C501S variant, we also experimentally confirmed that selective S-nitrosylation of Cys501 decreases ATPase activity of recombinant TRAP1. Coherently, C501S mutant was more active and conferred protection to cell death induced by staurosporine. Overall, our results provide the first in silico, in vitro and cellular evidence of the relevance of Cys501 S-nitrosylation in TRAP1 biology.

biochemistry↗