Membrane Alanyl Aminopeptidase (ANPEP), also known as CD13, is an enzyme that belongs to the class of peptidases. It is a transmembrane glycoprotein predominantly found on the cell surface of various tissues and cell types, including endothelial cells, fibroblasts, and certain malignant cells.
The primary function of Membrane Alanyl Aminopeptidase is the cleavage of amino-terminal neutral, hydrophobic amino acids from oligopeptides and proteins. It specifically targets amino acids such as alanine, proline, and leucine, playing a crucial role in protein maturation and degradation processes. This enzyme contributes to various physiological and pathological processes, including antigen processing and presentation, regulation of immune responses, and promotion of cell migration and invasion.
In addition to its peptidase activity, Membrane Alanyl Aminopeptidase is involved in various signaling pathways, including modulation of cell adhesion molecules, growth factors, and matrix metalloproteinases. It also interacts with multiple cell surface receptors and contributes to angiogenesis, tissue remodeling, and inflammation, thus making it an attractive target for therapeutic intervention.
Dysregulation or aberrant expression of Membrane Alanyl Aminopeptidase has been associated with a variety of diseases, including cancer, inflammation, and autoimmune disorders. Inhibition or modulation of this enzyme's activity holds potential in the development of novel therapeutic strategies for these conditions.
