Multiple intracellular protein targets of resveratrol (N/A)

Resveratrol (3,5,4'-trihydroxy-trans-stilbene) is a natural polyphenolic compound that interacts with a diverse array of intracellular protein targets, leading to pleiotropic biological effects (Baur & Sinclair, 2006, Nat. Rev. Drug Discov.). Its most prominent target is Sirtuin 1 (SIRT1), an NAD+-dependent deacetylase that resveratrol activates allosterically to promote metabolic health and longevity (Howitz et al., 2003, Nature; Hubbard et al., 2013, Science). Resveratrol also activates AMP-activated protein kinase (AMPK) indirectly by inhibiting cAMP-specific phosphodiesterases (PDEs), which increases intracellular NAD+ levels and enhances mitochondrial function (Park et al., 2012, Cell). Additionally, it modulates inflammatory responses by inhibiting cyclooxygenase-1 (COX-1) and COX-2 enzymes, thereby reducing the production of pro-inflammatory prostaglandins (Subbaramaiah et al., 1998, J. Biol. Chem.). Other significant targets include quinone reductase 2 (NQO2), which it inhibits, and estrogen receptors (ER-alpha and ER-beta), where it acts as a selective modulator (Buryanovskyy et al., 2004, Biochemistry; Gehm et al., 1997, PNAS). Due to its multi-target nature, resveratrol is investigated for its potential in treating type 2 diabetes, cardiovascular diseases, and various cancers, although its clinical utility is often limited by low systemic bioavailability and rapid metabolism (Pirola & Fröjdö, 2008, IUBMB Life).

Other names

Resveratrol-binding proteinsMolecular targets of resveratrolResveratrol effectors

Resveratrol acts as a pleiotropic modulator; it allosterically activates SIRT1 to promote deacetylation of targets like PGC-1alpha and p53, indirectly activates AMPK by inhibiting cAMP-specific phosphodiesterases (PDEs), and competitively inhibits cyclooxygenase enzymes to reduce pro-inflammatory eicosanoids.