Exploring the Potential of Calebin-A in Targeting Obesity-Related Genes and Pathways
Mahmoudi A., Saeedi-Boroujeni A., Karav S., Kesharwani P., Sahebkar A.
Laboratory Study on Type 2 Diabetes, published in J Cell Mol Med (2026) — summary generated from the PubMed abstract.
Evidence from laboratory and animal studies provides groundwork for understanding mechanisms and potential before human studies continue.
- Level A · Stronger Clinical Evidence
- Level B · Emerging clinical evidence with positive signals
- Level C · Early human research exploring benefits
- Level D · Scientific groundwork from lab and animal studies
- Emerging · Emerging topic under active research
This page is generated from the PubMed record. The Thai description is an automated summary of bibliographic fields and the abstract, not a full translation, and is not medical advice.
- Study type
- Laboratory Study
- Journal
- J Cell Mol Med (2026)
- Reported sample size
- —
- Source database
- Europe PMC
- PMID
- 42286733
- PMCID
- PMC13263248
- DOI
- 10.1111/jcmm.71244
Abstract (original English)
Obesity is a global health crisis affecting millions, associated with metabolic disorders such as type 2 diabetes and cardiovascular disease. Calebin-A, a bioactive compound derived from Curcuma species, has shown promise in managing obesity and its complications. This study utilized bioinformatics tools to explore the molecular mechanisms of Calebin-A in obesity. Transcriptomic data from obese and normal omental adipose tissue (GSE286454) were analysed, identifying 317 differentially expressed genes (DEGs). Functional enrichment analysis indicated a notable engagement of lysosomal activity, immune response, cell migration, axon guidance and apoptosis pathways. A STRING-based protein-protein interaction network revealed nine hub genes through a composite centrality score. Among these, CTSB, CTSZ, CTSA, GRN and TUBB exhibited upregulation and were prioritized for subsequent analysis. External validation (GSE59034; 16 obese vs. 16 controls) corroborated the consistent upregulation of CTSB, CTSZ, GRN and CTSA. Target prediction analysis identified 443 potential targets for Calebin-A, with pathway-level overlap suggesting a convergence on immune, lysosomal and cytoskeletal processes. Molecular docking studies indicated favourable binding affinities (-5.2 to -7.1 kcal/mol), with CTSZ demonstrating the most robust interaction. A 100 ns molecular dynamics simulation validated structur
What this study does not prove
- • This study does not prove SVF is an approved treatment or a replacement for standard care.
- • This is preclinical work; animal or laboratory results cannot be applied to humans.
Evidence level
Evidence from laboratory and animal studies provides groundwork for understanding mechanisms and potential before human studies continue.
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