Amine oxidase copper-containing 3 (Vascular adhesion protein-1) (AOC3)

Amine oxidase copper-containing 3 (AOC3), widely known as Vascular Adhesion Protein-1 (VAP-1), is a homodimeric transmembrane glycoprotein that functions as both a cell adhesion molecule and a copper-dependent enzyme [1, 4]. It is predominantly expressed on the surface of endothelial cells, adipocytes, and smooth muscle cells, where it plays a critical role in regulating leukocyte trafficking from the blood into tissues [2]. The enzymatic domain of AOC3, classified as a semicarbazide-sensitive amine oxidase (SSAO), catalyzes the oxidative deamination of primary amines into aldehydes, hydrogen peroxide, and ammonia [1, 2]. These reaction products are potent mediators of oxidative stress and can activate pro-inflammatory signaling pathways, contributing to tissue damage in chronic diseases [2, 4]. Consequently, AOC3 is a major therapeutic target for conditions characterized by excessive inflammation and fibrosis, such as non-alcoholic steatohepatitis (NASH) and diabetic complications [3]. Pharmacological strategies include small-molecule inhibitors and monoclonal antibodies designed to block its enzymatic activity or its interaction with leukocytes, thereby reducing pathological cell infiltration and oxidative injury [2, 3].

Other names

Vascular adhesion protein-1VAP-1Semicarbazide-sensitive amine oxidaseSSAOCopper amine oxidaseHPAOMembrane primary amine oxidase

Inhibition of the semicarbazide-sensitive amine oxidase (SSAO) enzymatic activity to prevent the production of pro-inflammatory byproducts (aldehydes, H2O2) and reduce leukocyte extravasation into inflamed tissues [2, 3].