Disintegrin and metalloproteinase domain-containing protein 10 (ADAM10) cleaves the membrane-bound precursor of TNF-alpha at '76-Ala-|-Val-77' to its mature soluble form. ADAM10 is responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP). ADAM10 contributes to the normal cleavage of the cellular prion protein. ADAM10 is involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity. ADAM10 also controls the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis.