Cited by 255Amino Acid Enzymes and MetabolismCancer, Hypoxia, and MetabolismPolyamine Metabolism and Applications

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The metabolism of proline, a stress substrate, modulates carcinogenic pathways

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Phang, James M., Donald, Steven P., Pandhare, Jui, Liu, Yongmin·2008·Amino Acids

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Abstract

The resurgence of interest in tumor metabolism has led investigators to emphasize the metabolism of proline as a "stress substrate" and to suggest this pathway as a potential anti-tumor target. Proline oxidase, a.k.a. proline dehydrogenase (POX/PRODH), catalyzes the first step in proline degradation and uses proline to generate ATP for survival or reactive oxygen species for programmed cell death. POX/PRODH is induced by p53 under genotoxic stress and initiates apoptosis by both mitochondrial and death receptor pathways. Furthermore, POX/PRODH is induced by PPARgamma and its pharmacologic ligands, the thiazolidinediones. The anti-tumor effects of PPARgamma may be critically dependent on POX/PRODH. In addition, it is upregulated by nutrient stress through the mTOR pathway to maintain ATP levels. We propose that proline is made available as a stress substrate by the degradation of collagen in the microenvironmental extracellular matrix by matrix metalloproteinases. In a manner analogous to autophagy, this proline-dependent process for bioenergetics from collagen in extracellular matrix can be designated "ecophagy".

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Authors: Phang, J. M., Donald, S. P., Pandhare, J., & Liu, Y.
Affiliations: Frederick National Laboratory for Cancer Research (US)
National Cancer Institute (US)
Science Applications International Corporation (United States) (US)
Corresponding author: Phang, James M.
ORCID: Phang, James M.
Pandhare, Jui
Liu, Yongmin
Venue: Amino Acids
Publisher: Springer Science and Business Media LLC
Published: 2008-04-10
Volume: 35
Issue: 4
Pages: 681-690
ISSN: 0939-4451 (ISSN-L)
1438-2199
DOI: 10.1007/s00726-008-0063-4
OpenAlex: W1986586503
Cited by: 252
References: 60
Citations by year: 2026: 3 · 2025: 14 · 2024: 8 · 2023: 13 · 2022: 15 · 2021: 20 · 2020: 12 · 2019: 15 · 2018: 15 · 2017: 18 · 2016: 10 · 2015: 15 · 2014: 15 · 2013: 13 · 2012: 11
FWCI: 1.35
Type: journal article
Language: en
Open access: green
zenodo.org
Licence: public-domain
www.springer.com/tdm (tdm)
Locations: Amino Acids (publishedVersion)
PubMed (publishedVersion)
Zenodo (CERN European Organization for Nuclear Research) (submittedVersion, public-domain)
Funders: National Institutes of Health (n01co12400-79-0-22)
National Cancer Institute (N01CO12400)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Polyamine Metabolism and Applications
Keywords: proline metabolism, proline oxidase, proline dehydrogenase, cancer metabolism, p53, apoptosis, PPARγ, thiazolidinediones, mTOR, nutritional stress, collagen degradation, matrix metalloproteinases, extracellular matrix, reactive oxygen species, carcinogenesis
MeSH terms: Adenosine Triphosphate, Autophagy, Catalysis, Ligands, Models, Biological, Neoplasms, Proline, Proline Oxidase, Protein Kinases, Gene Expression Regulation, Enzymologic, Tumor Suppressor Protein p53, Apoptosis, Thiazolidinediones, PPAR delta, TOR Serine-Threonine Kinases

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The metabolism of proline, a stress substrate, modulates carcinogenic pathways

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