EC Number |
General Information |
Reference |
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3.4.21.B28 | malfunction |
siRNA knockdown of FAP-alpha in a glioma cell line shows decreased invasion through brain extracellular matrix proteoglycan brevican and denatured collagen |
707629 |
3.4.21.B28 | evolution |
the enzyme belongs to the post-prolyl peptidase family |
731043 |
3.4.21.B28 | physiological function |
the enzyme promotes ovarian cancer cell proliferation, drug resistance, invasiveness, and migration in vitro and it significantly facilitates tumor growth in xenograft tumor tissues. The enzyme might directly promote tumor growth and invasiveness in ovarian cancer cells |
731043 |
3.4.21.B28 | metabolism |
FAP-alpha is significantly increased in breast cancer patients with poor outcome and survival |
731551 |
3.4.21.B28 | more |
overexpression of FAP-alpha results in a reduction of phosphorylated focal adhesion kinase level in both MCF-7 cells and MDA-MB-231 cells cultured in normal media and serum-free media, while the growth of MDA-MB-231 cells and the adhesion and invasion ability of both MCF-7 cells and MDA-MB-231 cells are not dramatically influenced by FAP-alpha expression |
731551 |
3.4.21.B28 | physiological function |
in vitro, FAP-alpha promotes proliferation and inhibits migration of breast cancer cells, potentially by regulating the FAK pathway |
731551 |
3.4.21.B28 | physiological function |
fibroblast activation protein-alpha promotes ovarian cancer cell proliferation and invasion via extracellular and intracellular signaling mechanisms, role of the non-enzymatic activities of the enzyme, overview. The enzyme, together with integrin alpha3beta1 and the uPAR signaling complex, mediates cancer cell migration in the HO-8910PM cell line via the small GTPase Rac1. FAP?-mediated upregulation of p-ERK occurs in a time-dependent manner |
731767 |
3.4.21.B28 | evolution |
the enzyme exhibits similar substrate specificity and properties compared to prolyl oligopeptidase, EC 3.4.21.26, the latter is specifically inhibited by Z-Pro-prolinal, while the fibroblast activation protein alpha is not. In contrast to prolyl oligopeptidase, fibroblast activation protein alpha is not expressed in normal adult tissues. Substrate specificity preferences among these sequences include Pro-Phe-Thr, which is strongly cleaved by prolyl oligopeptidase, and Pro-Tyr-Asp, which is strongly cleaved by fibroblast activation protein alpha. Pro-Phe/Tyr-Asp/Glu sequences are extensively cleaved by both prolyl oligopeptidase and fibroblast activation protein alpha, but neither enzyme exhibit substantial cleavage of Pro-Asp/Glu-Phe-Tyr |
731808 |
3.4.21.B28 | physiological function |
the enzyme may contributes to the focal matrix-degrading capability of stromal invadopodia |
752802 |
3.4.21.B28 | physiological function |
the enzyme promotes the ability of proliferation, migration, invasion, apoptosis-inhibition of SGC7901 cells and induces apoptosis of GES1 cells in vitro |
753092 |