Urtica dioica Agglutinin (UDA)

Preliminary

Hevein-domain lectin (chitin-binding plant lectin)

Mechanism of Action

UDA is a small (8.5 kDa), two-domain chitin-binding lectin with selective affinity for N-acetylglucosamine oligomers displayed on sex hormone-binding globulin (SHBG). By binding SHBG, UDA competitively occludes the steroid-binding domain of the protein, reducing its capacity to sequester testosterone and DHT in circulation. Additionally, UDA binds to the epidermal growth factor receptor (EGFR) on prostatic stromal cells, inhibiting EGF-mediated proliferative signaling. Lectin-carbohydrate interactions also modulate lymphocyte proliferation and cytokine release, suggesting immunomodulatory contributions independent of hormonal effects. UDA is heat-labile and degraded by gastric acid, making bioavailability dependent on preparation method and pH.

Research Notes

Nettle RootWestern

In vitro binding studies (Wagner et al., 1994) demonstrated that UDA binds SHBG with a dissociation constant in the nanomolar range, comparable to endogenous steroid ligands. Radioligand receptor assays confirmed displacement of DHT from SHBG at physiologically relevant lectin concentrations. Animal studies showed reduction in prostatic epithelial proliferation with UDA treatment; however, human pharmacokinetic data confirming intact UDA absorption remain limited, and the clinical contribution of UDA relative to phytosterols and polysaccharides in standardized extracts has not been isolated in controlled trials.

Found In 1 Herb

Nettle Root

Western

3D Molecular Structure

Hevein-domain lectin (chitin-binding plant lectin)

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Urtica dioica Agglutinin (UDA)

Hevein-domain lectin (chitin-binding plant lectin)Bioactive phytochemical with therapeutic properties

Representative pattern: C₄H₂NO

Atoms

Carbon

Oxygen

Nitrogen

Hydrogen

Live Research

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