Alanyl aminopeptidase (CD13) (CD13)

Alanyl aminopeptidase, commonly known as CD13 or Aminopeptidase N (APN), is a membrane-bound zinc-dependent metalloprotease that plays a critical role in various physiological and pathological processes (UniProt P15144). While it is expressed in several tissues including the kidney, intestine, and myeloid cells, its specific upregulation on the surface of angiogenic endothelial cells makes it a significant target in oncology (Pasqualini et al., 2000). In the context of tumor angiogenesis, CD13 facilitates cell migration and tube formation by degrading extracellular matrix components and modulating growth factor signaling (Bhagwat et al., 2001). Therapeutic strategies often exploit the unique expression of CD13 on tumor vasculature using the NGR (Asn-Gly-Arg) peptide motif, which selectively binds to the CD13 isoform present in angiogenic vessels (Curnis et al., 2000). This allows for the targeted delivery of cytotoxic agents or cytokines, such as tumor necrosis factor (TNF), directly to the tumor microenvironment while minimizing systemic toxicity (Luan & Xu, 2007).

Other names

Aminopeptidase NAPNANPEPMicrosomal aminopeptidasegp150PEPN

Inhibition of aminopeptidase enzymatic activity to prevent peptide processing and cell signaling; targeted delivery of therapeutic payloads (cytotoxins or cytokines) via NGR-peptide binding to the CD13 receptor specifically expressed on angiogenic vasculature.