FH Variant Pathogenicity Promotes Purine Salvage Pathway Dependence in Kidney Cancer.


Journal

Cancer discovery
ISSN: 2159-8290
Titre abrégé: Cancer Discov
Pays: United States
ID NLM: 101561693

Informations de publication

Date de publication:
06 09 2023
Historique:
received: 05 08 2022
revised: 27 03 2023
accepted: 24 05 2023
pmc-release: 06 03 2024
medline: 7 9 2023
pubmed: 31 5 2023
entrez: 31 5 2023
Statut: ppublish

Résumé

Fumarate accumulation due to loss of fumarate hydratase (FH) drives cellular transformation. Germline FH alterations lead to hereditary leiomyomatosis and renal cell cancer (HLRCC) where patients are predisposed to an aggressive form of kidney cancer. There is an unmet need to classify FH variants by cancer-associated risk. We quantified catalytic efficiencies of 74 variants of uncertain significance. Over half were enzymatically inactive, which is strong evidence of pathogenicity. We next generated a panel of HLRCC cell lines expressing FH variants with a range of catalytic activities, then correlated fumarate levels with metabolic features. We found that fumarate accumulation blocks de novo purine biosynthesis, rendering FH-deficient cells reliant on purine salvage for proliferation. Genetic or pharmacologic inhibition of the purine salvage pathway reduced HLRCC tumor growth in vivo. These findings suggest the pathogenicity of patient-associated FH variants and reveal purine salvage as a targetable vulnerability in FH-deficient tumors. This study functionally characterizes patient-associated FH variants with unknown significance for pathogenicity. This study also reveals nucleotide salvage pathways as a targetable feature of FH-deficient cancers, which are shown to be sensitive to the purine salvage pathway inhibitor 6-mercaptopurine. This presents a new rapidly translatable treatment strategy for FH-deficient cancers. This article is featured in Selected Articles from This Issue, p. 1949.

Identifiants

pubmed: 37255402
pii: 727063
doi: 10.1158/2159-8290.CD-22-0874
pmc: PMC10527600
mid: NIHMS1906929
doi:

Substances chimiques

Fumarate Hydratase EC 4.2.1.2
Purines 0

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

2072-2089

Subventions

Organisme : NIAMS NIH HHS
ID : R01 AR070245
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA215185
Pays : United States

Informations de copyright

©2023 American Association for Cancer Research.

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Auteurs

Blake R Wilde (BR)

Department of Biological Chemistry, University of California Los Angeles, Los Angeles, California.
Jonsson Comprehensive Cancer Center, University of California Los Angeles, Los Angeles, California.

Nishma Chakraborty (N)

Department of Biological Chemistry, University of California Los Angeles, Los Angeles, California.

Nedas Matulionis (N)

Department of Biological Chemistry, University of California Los Angeles, Los Angeles, California.

Stephanie Hernandez (S)

Department of Biological Chemistry, University of California Los Angeles, Los Angeles, California.

Daiki Ueno (D)

Institute of Urologic Oncology, University of California Los Angeles, Los Angeles, California.

Michayla E Gee (ME)

Department of Biological Chemistry, University of California Los Angeles, Los Angeles, California.

Edward D Esplin (ED)

Invitae, San Francisco, California.

Karen Ouyang (K)

Invitae, San Francisco, California.

Keith Nykamp (K)

Invitae, San Francisco, California.

Brian Shuch (B)

Jonsson Comprehensive Cancer Center, University of California Los Angeles, Los Angeles, California.
Institute of Urologic Oncology, University of California Los Angeles, Los Angeles, California.

Heather R Christofk (HR)

Department of Biological Chemistry, University of California Los Angeles, Los Angeles, California.
Invitae, San Francisco, California.
Broad Stem Cell Research Center, University of California Los Angeles, Los Angeles, California.

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