Expression levels of seprase/FAPα and DPPIV/CD26 in epithelial ovarian carcinoma.
Zhengzhou, China. In Oncol Lett, 31 Jul 2015
UNASSIGNED: Dipeptidyl peptidase IV (DPPIV; also known as cluster of differentiation 26) and the surface-expressed protease, seprase [also known as fibroblast activation protein alpha (FAPα)], are able to degrade the extracellular matrix; therefore, they are involved in malignant cell invasion and metastasis.
Fibroblast activation protein α–specific, near-infrared peptide probe (KGPGPNQC) linked to Cy5.5 and a quencher dye, QSY21
Bethesda, United States. In Unknown Journal, 2012
The fibroblast activation protein α (FAPα; also known as seprase) is a tumor stromal fibroblast cell-surface dipeptidyl peptidase IV (DPPIV) serine protease that is expressed in various pathologies such as cancers (colon-rectal, pancreas, lung, ovarian, etc.), arthritis, fibrosis, and inflammation, but not in normal tissues (1).
Dipeptidyl peptidase IV activity and/or structure homologues (DASH) and their substrates in cancer.
Praha, Czech Republic. In Int J Biochem Cell Biol, 2004
These comprise for example, seprase, fibroblast activation protein alpha, DPP6, DPP8, DPP9, attractin, N-acetylated-alpha-linked-acidic dipeptidases I, II and L, quiescent cell proline dipeptidase, thymus-specific serine protease and DPP IV-beta.
Seprase complexes in cellular invasiveness.
Stony Brook, United States. In Cancer Metastasis Rev, 2003
A group of type II integral serine proteases, including dipeptidyl peptidase IV (DPP4/CD26), seprase/fibroblast activation protein alpha (FAPalpha) and related type II transmembrane prolyl serine peptidases, exert their mechanisms of action on the cell surface.