FAP

Fibroblast activation protein alpha (FAP), also known as FAPA, SIMP, DPPIV or FAPalpha, is a melanoma membrane-bound gelatinase as well as a Type II transmembrane serine protease. It belongs to the S9B prolyl oligopeptidase subfamily. FAP is catalytically active as a 170kD dimer and has both dipeptidyl peptidase and endopeptidase activity.

FAP has a restricted expression pattern. This protein is undetectable in normal tissues or resting fibroblasts, but is highly expressed in reactive stromal fibroblasts of epithelial cancers, granulation tissue of healing wounds, and malignant cells of bone and soft tissue sarcomas. FAP protein is thought to be involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. In association with DPP4, this protein participates in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM, which may contribute to invasiveness in malignant cancers. It is worth mentioning that a monoclonal antibody, Sibrotuzumab, targeting FAP has entered the clinical trial for metastatic colorectal cancer, but unfortunately failed in phase II clinical trial.

Gene ID: 2191
UniProt ID: Q12884

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