ANPEP / CD13

alanyl (membrane) aminopeptidase

ANPEP (CD13) is a broad specificity aminopeptidase involved in the metabolism of biologically active peptides, phagocytosis, and myeloid cell differentiation. It is known to have bactericidal and tumoricidal activity. ANPEP plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. It is thought to be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. ANPEP cleaves antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrade neurotransmitters at synaptic junctions. It is also implicated as a regulator of IL-8 bioavailability in the endometrium, and therefore may contribute to the regulation of angiogenesis. In normal tissue, ANPEP is present on a majority of cells of myeloid origin, including granulocytes, monocytes, mast cells, and GM-progenitor cells. It is also found on fibroblasts, endothelial cells, epithelial cells from renal proximal tubules and intestinal brush border, bone marrow stromal cells, osteoclasts, and cells lining bile duct canaliculi. In cancer and disease, it is used as a marker for acute myeloid leukemia and plays a role in tumor invasion. It is expressed by the majority of AML, CML in myeloid blast crisis, and in a smaller fraction of lymphoid leukemia. It is absent in normal lymphocytes, platelets and erythrocytes. In the case of human coronavirus 229E (HCoV-229E) infection, it serves as receptor for HCoV-229E spike glycoprotein. It also mediates human cytomegalovirus (HCMV) infection. Additionally, it may play a critical role in the pathogenesis of cholesterol gallstone disease.

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