Metabolic Rewiring by Loss of Sirt5 Promotes Kras-Induced Pancreatic Cancer Progression.


Journal

Gastroenterology
ISSN: 1528-0012
Titre abrégé: Gastroenterology
Pays: United States
ID NLM: 0374630

Informations de publication

Date de publication:
11 2021
Historique:
received: 21 01 2021
revised: 09 06 2021
accepted: 13 06 2021
pubmed: 11 7 2021
medline: 18 1 2022
entrez: 10 7 2021
Statut: ppublish

Résumé

SIRT5 plays pleiotropic roles via post-translational modifications, serving as a tumor suppressor, or an oncogene, in different tumors. However, the role SIRT5 plays in the initiation and progression of pancreatic ductal adenocarcinoma (PDAC) remains unknown. Published datasets and tissue arrays with SIRT5 staining were used to investigate the clinical relevance of SIRT5 in PDAC. Furthermore, to define the role of SIRT5 in the carcinogenesis of PDAC, we generated autochthonous mouse models with conditional Sirt5 knockout. Moreover, to examine the mechanistic role of SIRT5 in PDAC carcinogenesis, SIRT5 was knocked down in PDAC cell lines and organoids, followed by metabolomics and proteomics studies. A novel SIRT5 activator was used for therapeutic studies in organoids and patient-derived xenografts. SIRT5 expression negatively regulated tumor cell proliferation and correlated with a favorable prognosis in patients with PDAC. Genetic ablation of Sirt5 in PDAC mouse models promoted acinar-to-ductal metaplasia, precursor lesions, and pancreatic tumorigenesis, resulting in poor survival. Mechanistically, SIRT5 loss enhanced glutamine and glutathione metabolism via acetylation-mediated activation of GOT1. A selective SIRT5 activator, MC3138, phenocopied the effects of SIRT5 overexpression and exhibited antitumor effects on human PDAC cells. MC3138 also diminished nucleotide pools, sensitizing human PDAC cell lines, organoids, and patient-derived xenografts to gemcitabine. Collectively, we identify SIRT5 as a key tumor suppressor in PDAC, whose loss promotes tumorigenesis through increased noncanonic use of glutamine via GOT1, and that SIRT5 activation is a novel therapeutic strategy to target PDAC.

Sections du résumé

BACKGROUND & AIMS
SIRT5 plays pleiotropic roles via post-translational modifications, serving as a tumor suppressor, or an oncogene, in different tumors. However, the role SIRT5 plays in the initiation and progression of pancreatic ductal adenocarcinoma (PDAC) remains unknown.
METHODS
Published datasets and tissue arrays with SIRT5 staining were used to investigate the clinical relevance of SIRT5 in PDAC. Furthermore, to define the role of SIRT5 in the carcinogenesis of PDAC, we generated autochthonous mouse models with conditional Sirt5 knockout. Moreover, to examine the mechanistic role of SIRT5 in PDAC carcinogenesis, SIRT5 was knocked down in PDAC cell lines and organoids, followed by metabolomics and proteomics studies. A novel SIRT5 activator was used for therapeutic studies in organoids and patient-derived xenografts.
RESULTS
SIRT5 expression negatively regulated tumor cell proliferation and correlated with a favorable prognosis in patients with PDAC. Genetic ablation of Sirt5 in PDAC mouse models promoted acinar-to-ductal metaplasia, precursor lesions, and pancreatic tumorigenesis, resulting in poor survival. Mechanistically, SIRT5 loss enhanced glutamine and glutathione metabolism via acetylation-mediated activation of GOT1. A selective SIRT5 activator, MC3138, phenocopied the effects of SIRT5 overexpression and exhibited antitumor effects on human PDAC cells. MC3138 also diminished nucleotide pools, sensitizing human PDAC cell lines, organoids, and patient-derived xenografts to gemcitabine.
CONCLUSIONS
Collectively, we identify SIRT5 as a key tumor suppressor in PDAC, whose loss promotes tumorigenesis through increased noncanonic use of glutamine via GOT1, and that SIRT5 activation is a novel therapeutic strategy to target PDAC.

Identifiants

pubmed: 34245764
pii: S0016-5085(21)03159-0
doi: 10.1053/j.gastro.2021.06.045
pmc: PMC8546779
mid: NIHMS1722572
pii:
doi:

Substances chimiques

Enzyme Activators 0
KRAS protein, human 0
SIRT5 protein, mouse 0
Deoxycytidine 0W860991D6
Aspartate Aminotransferase, Cytoplasmic EC 2.6.1.-
GOT1 protein, human EC 2.6.1.-
Got1 protein, mouse EC 2.6.1.-
SIRT5 protein, human EC 3.5.1.-
Sirtuins EC 3.5.1.-
Hras protein, mouse EC 3.6.5.2
Proto-Oncogene Proteins p21(ras) EC 3.6.5.2
Gemcitabine 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

1584-1600

Subventions

Organisme : NCI NIH HHS
ID : R01 CA216853
Pays : United States
Organisme : NCI NIH HHS
ID : P50 CA127297
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA163649
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA210439
Pays : United States
Organisme : NCI NIH HHS
ID : T32 CA009476
Pays : United States
Organisme : NCI NIH HHS
ID : P01 CA217798
Pays : United States

Commentaires et corrections

Type : CommentIn

Informations de copyright

Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.

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Auteurs

Tuo Hu (T)

The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska; Department of Colorectal Surgery, Guangdong Provincial Key Laboratory of Colorectal and Pelvic Floor Diseases, The Sixth Affiliated Hospital, Sun Yat-sen University, Guangzhou, Guangdong, China.

Surendra K Shukla (SK)

The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska.

Enza Vernucci (E)

The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska.

Chunbo He (C)

The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska.

Dezhen Wang (D)

The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska.

Ryan J King (RJ)

The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska.

Kanupriya Jha (K)

Department of Biotechnology, School of Engineering and Applied Sciences, Bennett University, Greater Noida, Uttar Pradesh, India.

Kasturi Siddhanta (K)

The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska; Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska.

Nicholas J Mullen (NJ)

The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska.

Kuldeep S Attri (KS)

The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska.

Divya Murthy (D)

The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska.

Nina V Chaika (NV)

The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska.

Ravi Thakur (R)

The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska.

Scott E Mulder (SE)

The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska; Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska.

Camila G Pacheco (CG)

The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska.

Xiao Fu (X)

The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska.

Robin R High (RR)

Department of Biostatistics, University of Nebraska Medical Center, Omaha, Nebraska.

Fang Yu (F)

Department of Biostatistics, University of Nebraska Medical Center, Omaha, Nebraska.

Audrey Lazenby (A)

Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, Nebraska.

Clemens Steegborn (C)

University of Bayreuth, Department of Biochemistry, Bayreuth, Germany.

Ping Lan (P)

Department of Colorectal Surgery, Guangdong Provincial Key Laboratory of Colorectal and Pelvic Floor Diseases, The Sixth Affiliated Hospital, Sun Yat-sen University, Guangzhou, Guangdong, China.

Kamiya Mehla (K)

The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska.

Dante Rotili (D)

Department of Drug Chemistry and Technologies, Sapienza University of Rome, Rome, Italy.

Sarika Chaudhary (S)

Department of Biotechnology, School of Engineering and Applied Sciences, Bennett University, Greater Noida, Uttar Pradesh, India.

Sergio Valente (S)

Department of Drug Chemistry and Technologies, Sapienza University of Rome, Rome, Italy.

Marco Tafani (M)

Department of Experimental Medicine, Sapienza University of Rome, Rome, Italy.

Antonello Mai (A)

Department of Drug Chemistry and Technologies, Sapienza University of Rome, Rome, Italy.

Johan Auwerx (J)

Laboratory for Integrative Systems Physiology, Ecole Polytechnique Fédérale de Lausanne, Lausanne, Switzerland.

Eric Verdin (E)

Buck Institute for Research on Aging, Novato, California.

David Tuveson (D)

Cancer Center at Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.

Pankaj K Singh (PK)

The Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha, Nebraska; Department of Biochemistry and Molecular Biology, University of Nebraska Medical Center, Omaha, Nebraska; Department of Pathology and Microbiology, University of Nebraska Medical Center, Omaha, Nebraska; Fred & Pamela Buffett Cancer Center, University of Nebraska Medical Center, Omaha, Nebraska. Electronic address: Pankaj.singh@unmc.edu.

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Classifications MeSH