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Beschreibung

Fibroblast activation protein (UniProt: , also known as Propyl endopeptidase FAP, Dipeptidyl peptidase FAP, Serine integral membrane protease, SIMP) is encoded by the Fap gene (Gene ID: 14089) in murine species. FAP is a homodimeric type II transmembrane protein that physically attaches to cells and bulk of the protein is exposed to extracellular space. It is a gelatinase of the serine protease family that is selectively expressed by tumor associated fibroblasts and pericytes in a majority of human epithelial cancers, granulation tissue of healing wounds, and malignant cells of bone and soft tissue sarcomas. It is not expressed in most normal tissues, but is expressed during embryonic development. It is present as a homodimer and homodimerization is required for activity of both plasma membrane and soluble forms. It can also form heterodimer with DPP4. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences. Its gelatinase activity is inhibited by several serine-protease inhibitors, such as PMSF, AEBSF, and diisopropyl fluorophosphate (DFP). FAP is involved in the control of fibroblast growth or epithelial-mesenchymal interactions during development, tissue repair, and epithelial carcinogenesis. It is also involved in the cell invasiveness towards the ECM in malignant melanoma cancers. (Ref.: Kelly, T et al. (2012). Int. Rev. Cell Mol. Biol. 297:83-116, Santos, AM et al. (2009). J. Clin. Invest. 119(12):3613-3625).