VAP-1, Human, mAb 174-5

The monoclonal antibody 174-5 recognises human Vascular Adhesion Protein-1 (VAP-1), which- is a glycosylated homodimeric membrane protein consisting of two 90 kDa subunits connected by disulfide bonds. It contains- a short N-terminal cytoplasmic tail, a single membrane-spanning domain and a large extracellular part.- A soluble form of VAP-1 (sVAP-1) has been described, which presumably results from the proteolytic cleavage of membrane-bound VAP-1. Structurally VAP-1 belongs to enzymes called semicarbamizide-sensitive amine oxidases, which contain copper as a cofactor. These enzymes deaminate primary amines in a reaction producing hydrogen peroxide, aldehyde, and ammonia.
VAP-1 is present in endothelial cells, smooth muscle cells, adipocytes, and in follicular dendritic cells. In endothelial cells the majority of VAP-1 is stored within intracellular granules and translocated to the surface upon inflammation where it regulates leukocyte tissue infiltration. Furthermore, the end-products formed by VAP-1 can also regulate leukocyte migration by signaling effects, have insulin-like effects in energy metabolism, and can cause vascular damage by direct cytotoxicity. Elevated sVAP-1serum- levels have been described in several inflammatory- diseases as well as colorectal cancer. Moreover, diminished insulin secretion appears to increase the concentration of soluble VAP-1 in plasma. Therefore, VAP-1 might be an interesting diagnostic marker as well therapeutic- target for modulating inflammation.The monoclonal antibody 174-5 has been shown to cross-react with rat VAP-1 and to inhibit lymphocyte infiltration in rat liver allograft rejection.