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Fibroblast activation protein a (FAPa) also known as seprase belongs to type II integral membrane proteins. FAPa/seprase bounded to cell membrane is serine proteinase with gelatinase activity. Serine proteases family included among others S9B post-prolyl dipeptidyl aminopeptidase subfamily. Besides FAPa/seprase, to S9B subfamily belongs dipeptidyl peptidase IV (DPPIV). Catalytically active FAPa is a 170 kDa homodimer, consisting of two 97 kDa subunits. FAPa besides homodimers also forms heteromeric, catalytically active complexes with DPPIV. Both protease complexes play a role in the degradation of extracellular matrix components (ECM). FAPa besides degradation of selected ECM components controls fibroblasts growth and epidermis mesenchyme interaction during embriogenesis, as well as tissue repair and carcinogenesis. This protein is an inducible antigen that is selectively expressed in activated fibroblasts during wound healing, in carcinoma-associated fibroblasts (CAFs) during metastasis of epithelial cancers and in cells of some malignant tumors. Wound healing and cancerogenesis exhibit similarities at some points. Many growth factors, cytokines and proteases produced by cancer cells during cancerogenesis and tumor metastasis also play essential role in wound healing and tissue fibrosis. FAPa is a myofibroblast marker. Myofibroblasts are present during wound healing, tissues fibrosis as well as cancerogenesis. FAPa overexpression is also characteristic in keloids that are nonmalignant fibrotic tumors forming in a consequence of improper wound healing.
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Andrzej Łukaszyk - przewodniczący, Zofia Bielańska-Osuchowska, Szczepan Biliński, Mieczysław Chorąży, Aleksander Koj, Włodzimierz Korochoda, Leszek Kuźnicki, Aleksandra Stojałowska, Lech Wojtczak

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