Fhit Interaction with Ferredoxin Reductase Triggers Generation of Reactive Oxygen Species and Apoptosis of Cancer Cells
Open accessAbstract
Fhit protein is lost in most cancers, its restoration suppresses tumorigenicity, and virus-mediated FHIT gene therapy induces apoptosis and suppresses tumors in preclinical models. We have used protein cross-linking and proteomics methods to characterize a Fhit protein complex involved in triggering Fhit-mediated apoptosis. The complex includes Hsp60 and Hsp10 that mediate Fhit stability and may affect import into mitochondria, where it interacts with ferredoxin reductase, responsible for transferring electrons from NADPH to cytochrome P450 via ferredoxin. Viral-mediated Fhit restoration increases production of intracellular reactive oxygen species, followed by increased apoptosis of lung cancer cells under oxidative stress conditions; conversely, Fhit-negative cells escape apoptosis, carrying serious oxidative DNA damage that may contribute to an increased mutation rate. Characterization of Fhit interacting proteins has identified direct effectors of the Fhit-mediated apoptotic pathway that is lost in most cancers through loss of Fhit.
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HIT proteins have been shown to be involved in diverse cellular stress responses, such as DNA damage, oxidative stress and induced apoptosis.
“HIT proteins have been shown to be involved in diverse cellular stress responses, such as DNA damage, oxidative stress and induced apoptosis1718.”
From Determining crystal structures through crowdsourcing and coursework (2016) · cites this paper as [18]
The Abstract reports that Fhit restoration increases reactive oxygen species and apoptosis under oxidative stress, while the Discussion links Fhit to responses to DNA damage. The paper establishes these roles for Fhit specifically, not for HIT proteins as a group. (LLM, conf=0.86)
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Fhit Nuclear Import Following EGF Stimulation Sustains Proliferation of Breast Cancer Cells
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- Authors
- Trapasso, F., Pichiorri, F., Gaspari, M., Palumbo, T., Aqeilan, R. I., Gaudio, E., Okumura, H., Iuliano, R., Di Leva, G., Fabbri, M., Birk, D. E., Raso, C., Green-Church, K., Spagnoli, L. G., Venuta, S., Huebner, K., & Croce, C. M.
- Affiliations
- The Ohio State University Comprehensive Cancer Center – Arthur G. James Cancer Hospital and Richard J. Solove Research Institute (US)
- University of Rome Tor Vergata (IT)
- Magna Graecia University (IT)
- Thomas Jefferson University (US)
- Corresponding author
- Croce, Carlo M.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2008-05
- Volume
- 283
- Issue
- 20
- Pages
- 13736-13744
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2376222
- OpenAlex
- W2118030637
- Cited by
- 71
- References
- 41
- Citations by year
- 2024: 1 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 2 · 2019: 1 · 2018: 2 · 2017: 7 · 2016: 8 · 2015: 8 · 2014: 6 · 2013: 7 · 2012: 5
- FWCI
- 3.70
- Type
- journal article
- Language
- en
- Status
- Retracted
- Update notices
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Cineca Institutional Research Information System (Tor Vergata University) (submittedVersion)
- Funders
- National Cancer Institute (CA78890, CA 77738, P01CA078890, P01CA077738, P30CA016058)
- National Center for Research Resources (S10RR023647)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- FHIT, ferredoxin reductase, reactive oxygen species, apoptosis, cancer cells, HSP60, Hsp10, mitochondrial protein import, protein-protein interaction, oxidative DNA damage, lung cancer, viral gene therapy, tumor suppression, oxidative stress
- MeSH terms
- Bis(5'-adenosyl)triphosphatase, Cytosol, DNA Damage, Humans, Mitochondria, Models, Biological, Mutation, Neoplasm Proteins, Neoplasms, Protein Binding, Apoptosis, Reactive Oxygen Species, Acid Anhydride Hydrolases, Chaperonin 60, Chaperonin 10, Cell Line, Tumor, Ferredoxin-Nitrite Reductase
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