Modulation of Lonp1 Activity by Small Compounds
Open accessAbstract
The Lon protease homolog 1 (LONP1) is an ATP-dependent mitochondrial protease essential for maintaining proteostasis, bioenergetics, and cellular homeostasis. LONP1 plays a pivotal role in protein quality control, mitochondrial DNA maintenance, and oxidative phosphorylation system (OXPHOS) regulation, particularly under stress conditions. Dysregulation of LONP1 has been implicated in various pathologies, including cancer, metabolic disorders, and reproductive diseases, positioning it as a promising pharmacological target. This review examines compounds that modulate LONP1 activity, categorizing them into inhibitors and activators. Inhibitors such as CDDO and its derivatives selectively target LONP1, impairing mitochondrial proteolysis, inducing protein aggregation, and promoting apoptosis, particularly in cancer cells. Compounds like Obtusilactone A and proteasome inhibitors (e.g., MG262) demonstrate potent cytotoxicity, further expanding the therapeutic landscape. Conversely, LONP1 activators, including Artemisinin derivatives and 84-B10, restore mitochondrial function and protect against conditions such as polycystic ovary syndrome (PCOS) and acute kidney injury (AKI). Future research should focus on improving the specificity, bioavailability, and pharmacokinetics of these modulators. Advances in structural biology and drug discovery will enable the development of novel LONP1-targeted therapies, addressing diseases driven by mitochondrial dysfunction and proteostasis imbalance.
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Mitochondrial dysfunction contributes to muscle loss and metabolic decline in older adults.
“Additionally, resistance training enhances mitochondrial function by increasing the number and efficiency of mitochondria within muscle cells, which is particularly important in older adults, as mitochondrial dysfunction contributes to muscle loss and metabolic decline [67].”
From A Narrative Review on GLP-1 Receptor Agonists for Obesity in Older Women: Maximizing Weight Loss While Preserving Lean Mass (2026) · cites this paper as [67]
Section 2, “General Features of LONP1” (page unavailable), discusses mitochondrial bioenergetics and protection of muscle-cell models from damage. It does not link mitochondrial dysfunction to muscle loss or metabolic decline in older adults; searches for sarcopenia, muscle atrophy, and aging did not find that claim in our copy. (LLM, conf=0.72)
Experimental — accuracy not yet measuredResistance training enhances mitochondrial function by increasing the number and efficiency of mitochondria within muscle cells.
“Additionally, resistance training enhances mitochondrial function by increasing the number and efficiency of mitochondria within muscle cells, which is particularly important in older adults, as mitochondrial dysfunction contributes to muscle loss and metabolic decline [67].”
From A Narrative Review on GLP-1 Receptor Agonists for Obesity in Older Women: Maximizing Weight Loss While Preserving Lean Mass (2026) · cites this paper as [67]
Section 2, “General Features of LONP1” (page unavailable), discusses how LONP1 maintains mitochondrial function, including in muscle-cell models. It does not address whether resistance training increases the number or efficiency of mitochondria in muscle cells. Searches for resistance training, exercise-related mitochondrial biogenesis, and muscle loss in older adults found no passage establishing the attributed claim. (LLM, conf=0.76)
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Mitochondrial Lon protease is a gatekeeper for proteins newly imported into the matrix
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Powering down the mitochondrial LonP1 protease: a novel strategy for anticancer therapeutics
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Self-citationOrganismal and Cellular Stress Responses upon Disruption of Mitochondrial Lonp1 Protease
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How is sesamin metabolised in the human liver to show its biological effects?
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Structure-Based Design of Selective LONP1 Inhibitors for Probing In Vitro Biology
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Self-citationLeveraging Peptide Substrate Libraries to Design Inhibitors of Bacterial Lon Protease
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A Lon-Like Protease with No ATP-Powered Unfolding Activity
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WITHDRAWN: LonP1 Drives Proneural Mesenchymal Transition in IDH1-R132H Diffuse GliomaPreprint
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- Authors
- Zanini, G., Micheloni, G., Sinigaglia, G., Selleri, V., Mattioli, A. V., Nasi, M., Pierri, C. L., & Pinti, M.
- Affiliations
- University of Modena and Reggio Emilia (IT)
- Istituto Nazionale per le Ricerche Cardiovascolari (IT)
- University of Bari Aldo Moro (IT)
- Corresponding author
- Pinti, Marcello
- ORCID
- Venue
- Biomolecules
- Publisher
- MDPI AG
- Published
- 2025-04-09
- Volume
- 15
- Issue
- 4
- Pages
- 553
- ISSN
- 2218-273X (ISSN-L)
- PMC
- PMC12024584
- OpenAlex
- W4409313643
- Cited by
- 7
- References
- 121
- Citations by year
- 2026: 7
- FWCI
- 0.62
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Biomolecules (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Archivio istituzionale della ricerca (Alma Mater Studiorum Università di Bologna) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- IRIS UNIMORE (University of Modena and Reggio Emilia) (submittedVersion, other-oa)
- CINECA IRIS Institutional Research Information System (University of Bari Aldo Moro) (submittedVersion)
- Funders
- AIRC (IG 2017 ID 19786, IG 2024 ID 30707)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- LONP1, mitochondrial proteolysis, small molecule modulators, CDDO, proteasome inhibitors, artemisinin derivatives, mitochondrial proteostasis, mitochondrial dysfunction, polycystic ovary syndrome, acute kidney injury, cancer therapy, apoptosis, protein aggregation
- MeSH terms
- Proteostasis, Animals, Humans, Mitochondria, Mitochondrial Proteins, ATP-Dependent Proteases, Small Molecule Libraries
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