Purine salvage promotes treatment resistance in H3K27M-mutant diffuse midline glioma.

Diffuse midline glioma H3K27M Purine metabolism Radiation therapy resistance

Journal

Cancer & metabolism
ISSN: 2049-3002
Titre abrégé: Cancer Metab
Pays: England
ID NLM: 101607582

Informations de publication

Date de publication:
09 Apr 2024
Historique:
received: 01 09 2023
accepted: 21 03 2024
medline: 10 4 2024
pubmed: 10 4 2024
entrez: 9 4 2024
Statut: epublish

Résumé

Diffuse midline gliomas (DMG), including diffuse intrinsic pontine gliomas (DIPGs), are a fatal form of brain cancer. These tumors often carry a driver mutation on histone H3 converting lysine 27 to methionine (H3K27M). DMG-H3K27M are characterized by altered metabolism and resistance to standard of care radiation (RT) but how the H3K27M mediates the metabolic response to radiation and consequent treatment resistance is uncertain. We performed metabolomics on irradiated and untreated H3K27M isogenic DMG cell lines and observed an H3K27M-specific enrichment for purine synthesis pathways. We profiled the expression of purine synthesis enzymes in publicly available patient data and our models, quantified purine synthesis using stable isotope tracing, and characterized the in vitro and in vivo response to de novo and salvage purine synthesis inhibition in combination with RT. DMG-H3K27M cells activate purine metabolism in an H3K27M-specific fashion. In the absence of genotoxic treatment, H3K27M-expressing cells have higher relative activity of de novo synthesis and apparent lower activity of purine salvage demonstrated via stable isotope tracing of key metabolites in purine synthesis and by lower expression of hypoxanthine-guanine phosphoribosyltransferase (HGPRT), the rate-limiting enzyme of purine salvage into IMP and GMP. Inhibition of de novo guanylate synthesis radiosensitized DMG-H3K27M cells in vitro and in vivo. Irradiated H3K27M cells upregulated HGPRT expression and hypoxanthine-derived guanylate salvage but maintained high levels of guanine-derived salvage. Exogenous guanine supplementation decreased radiosensitization in cells treated with combination RT and de novo purine synthesis inhibition. Silencing HGPRT combined with RT markedly suppressed DMG-H3K27M tumor growth in vivo. Our results indicate that DMG-H3K27M cells rely on highly active purine synthesis, both from the de novo and salvage synthesis pathways. However, highly active salvage of free purine bases into mature guanylates can bypass inhibition of the de novo synthetic pathway. We conclude that inhibiting purine salvage may be a promising strategy to overcome treatment resistance in DMG-H3K27M tumors.

Sections du résumé

BACKGROUND BACKGROUND
Diffuse midline gliomas (DMG), including diffuse intrinsic pontine gliomas (DIPGs), are a fatal form of brain cancer. These tumors often carry a driver mutation on histone H3 converting lysine 27 to methionine (H3K27M). DMG-H3K27M are characterized by altered metabolism and resistance to standard of care radiation (RT) but how the H3K27M mediates the metabolic response to radiation and consequent treatment resistance is uncertain.
METHODS METHODS
We performed metabolomics on irradiated and untreated H3K27M isogenic DMG cell lines and observed an H3K27M-specific enrichment for purine synthesis pathways. We profiled the expression of purine synthesis enzymes in publicly available patient data and our models, quantified purine synthesis using stable isotope tracing, and characterized the in vitro and in vivo response to de novo and salvage purine synthesis inhibition in combination with RT.
RESULTS RESULTS
DMG-H3K27M cells activate purine metabolism in an H3K27M-specific fashion. In the absence of genotoxic treatment, H3K27M-expressing cells have higher relative activity of de novo synthesis and apparent lower activity of purine salvage demonstrated via stable isotope tracing of key metabolites in purine synthesis and by lower expression of hypoxanthine-guanine phosphoribosyltransferase (HGPRT), the rate-limiting enzyme of purine salvage into IMP and GMP. Inhibition of de novo guanylate synthesis radiosensitized DMG-H3K27M cells in vitro and in vivo. Irradiated H3K27M cells upregulated HGPRT expression and hypoxanthine-derived guanylate salvage but maintained high levels of guanine-derived salvage. Exogenous guanine supplementation decreased radiosensitization in cells treated with combination RT and de novo purine synthesis inhibition. Silencing HGPRT combined with RT markedly suppressed DMG-H3K27M tumor growth in vivo.
CONCLUSIONS CONCLUSIONS
Our results indicate that DMG-H3K27M cells rely on highly active purine synthesis, both from the de novo and salvage synthesis pathways. However, highly active salvage of free purine bases into mature guanylates can bypass inhibition of the de novo synthetic pathway. We conclude that inhibiting purine salvage may be a promising strategy to overcome treatment resistance in DMG-H3K27M tumors.

Identifiants

pubmed: 38594734
doi: 10.1186/s40170-024-00341-7
pii: 10.1186/s40170-024-00341-7
doi:

Types de publication

Journal Article

Langues

eng

Pagination

11

Subventions

Organisme : NCI NIH HHS
ID : 5T32CA140044-13
Pays : United States
Organisme : NCI NIH HHS
ID : F32CA260735
Pays : United States
Organisme : NCI NIH HHS
ID : K08CA234416
Pays : United States
Organisme : NIH HHS
ID : R01CA240515
Pays : United States
Organisme : NINDS NIH HHS
ID : R21NS123879-01
Pays : United States

Informations de copyright

© 2024. The Author(s).

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Auteurs

Erik R Peterson (ER)

Doctoral Program in Cancer Biology, University of Michigan, Ann Arbor, MI, USA.
Department of Radiation Oncology, University of Michigan, Ann Arbor, MI, USA.
Rogel Cancer Center, University of Michigan, Ann Arbor, MI, USA.

Peter Sajjakulnukit (P)

Doctoral Program in Cancer Biology, University of Michigan, Ann Arbor, MI, USA.
Rogel Cancer Center, University of Michigan, Ann Arbor, MI, USA.

Andrew J Scott (AJ)

Department of Radiation Oncology, University of Michigan, Ann Arbor, MI, USA.
Rogel Cancer Center, University of Michigan, Ann Arbor, MI, USA.

Caleb Heaslip (C)

Massachusetts College of Pharmacy and Health Sciences, Boston, MA, USA.

Anthony Andren (A)

Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, MI, USA.

Kari Wilder-Romans (K)

Department of Radiation Oncology, University of Michigan, Ann Arbor, MI, USA.
Rogel Cancer Center, University of Michigan, Ann Arbor, MI, USA.

Weihua Zhou (W)

Department of Radiation Oncology, University of Michigan, Ann Arbor, MI, USA.
Rogel Cancer Center, University of Michigan, Ann Arbor, MI, USA.

Sravya Palavalasa (S)

Department of Radiation Oncology, University of Michigan, Ann Arbor, MI, USA.
Rogel Cancer Center, University of Michigan, Ann Arbor, MI, USA.

Navyateja Korimerla (N)

Department of Radiation Oncology, University of Michigan, Ann Arbor, MI, USA.
Rogel Cancer Center, University of Michigan, Ann Arbor, MI, USA.

Angelica Lin (A)

Department of Radiation Oncology, University of Michigan, Ann Arbor, MI, USA.
Rogel Cancer Center, University of Michigan, Ann Arbor, MI, USA.

Alexandra O'Brien (A)

Department of Radiation Oncology, University of Michigan, Ann Arbor, MI, USA.
Rogel Cancer Center, University of Michigan, Ann Arbor, MI, USA.

Ayesha Kothari (A)

Department of Radiation Oncology, University of Michigan, Ann Arbor, MI, USA.
Rogel Cancer Center, University of Michigan, Ann Arbor, MI, USA.

Zitong Zhao (Z)

Department of Radiation Oncology, University of Michigan, Ann Arbor, MI, USA.
Rogel Cancer Center, University of Michigan, Ann Arbor, MI, USA.

Li Zhang (L)

Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, MI, USA.

Meredith A Morgan (MA)

Doctoral Program in Cancer Biology, University of Michigan, Ann Arbor, MI, USA.
Department of Radiation Oncology, University of Michigan, Ann Arbor, MI, USA.
Rogel Cancer Center, University of Michigan, Ann Arbor, MI, USA.

Sriram Venneti (S)

Rogel Cancer Center, University of Michigan, Ann Arbor, MI, USA.
Department of Cellular and Molecular Biology, University of Michigan, Ann Arbor, MI, USA.
Department of Pathology, University of Michigan, Ann Arbor, MI, USA.

Carl Koschmann (C)

Doctoral Program in Cancer Biology, University of Michigan, Ann Arbor, MI, USA.
Rogel Cancer Center, University of Michigan, Ann Arbor, MI, USA.
Department of Pediatrics, University of Michigan, Ann Arbor, MI, USA.

Nada Jabado (N)

Department of Pediatrics, McGill University, Montreal, Quebec, Canada.
Department of Human Genetics, McGill University, Montreal, Quebec, Canada.

Costas A Lyssiotis (CA)

Doctoral Program in Cancer Biology, University of Michigan, Ann Arbor, MI, USA.
Rogel Cancer Center, University of Michigan, Ann Arbor, MI, USA.
Department of Molecular and Integrative Physiology, University of Michigan, Ann Arbor, MI, USA.

Maria G Castro (MG)

Doctoral Program in Cancer Biology, University of Michigan, Ann Arbor, MI, USA.
Rogel Cancer Center, University of Michigan, Ann Arbor, MI, USA.
Department of Cellular and Molecular Biology, University of Michigan, Ann Arbor, MI, USA.
Department of Neurosurgery, University of Michigan, Ann Arbor, MI, USA.

Daniel R Wahl (DR)

Doctoral Program in Cancer Biology, University of Michigan, Ann Arbor, MI, USA. dwahl@med.umich.edu.
Department of Radiation Oncology, University of Michigan, Ann Arbor, MI, USA. dwahl@med.umich.edu.
Rogel Cancer Center, University of Michigan, Ann Arbor, MI, USA. dwahl@med.umich.edu.
Medical Science Unit I, 1301 Catherine Street, Rm 4433, Ann Arbor, MI, 48109, USA. dwahl@med.umich.edu.

Classifications MeSH