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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Fibroblast activation protein, alpha

The protein encoded by this gene is a homodimeric integral membrane gelatinase belonging to the serine protease family. It is selectively expressed in reactive stromal fibroblasts of epithelial cancers, granulation tissue of healing wounds, and malignant cells of bone and soft tissue sarcomas. This protein is thought to be involved in the control of fibroblast growth or epithelial-mesenchymal interactions during development, tissue repair, and epithelial carcinogenesis. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: MMP-9, CD26, DSP, lysyl oxidase, HAD
Papers on seprase
Evaluation of a 5-Marker Blood Test for Colorectal Cancer Early Detection in a Colorectal Cancer Screening Setting.
Brenner et al., La Roche-sur-Yon, France. In Clin Cancer Res, Dec 2015
For osteopontin, seprase and ferritin the diagnostic performance in the screening setting was reduced compared to previous studies in diagnostic settings while CEA and anti-p53 showed similar diagnostic performance in both settings.
Expression levels of seprase/FAPα and DPPIV/CD26 in epithelial ovarian carcinoma.
Ding et al., Zhengzhou, China. In Oncol Lett, 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.
Treatment monitoring of patients with epithelial ovarian cancer using invasive circulating tumor cells (iCTCs).
Chen et al., Stony Brook, United States. In Gynecol Oncol, May 2015
METHODS: Molecular and microscopic analyses were used to identify seprase and CD44 as tumor progenitor (TP) markers.
Co-expression of the homologous proteases fibroblast activation protein and dipeptidyl peptidase-IV in the adult human Langerhans islets.
Sedo et al., Praha, Czech Republic. In Histochem Cell Biol, May 2015
Fibroblast activation protein (FAP, seprase, EC 3.4.21.B28) and dipeptidyl peptidase-IV (DPP-IV, CD26, EC are homologous serine proteases implicated in the modulation of the bioavailability and thus the function of a number of biologically active peptides.
Transcriptional regulation of seprase in invasive melanoma cells by transforming growth factor-β signaling.
Chen et al., Stony Brook, United States. In J Biol Chem, 2014
Seprase (also named fibroblast activation protein-α, antiplasmin-cleaving enzyme, and dipeptidyl prolyl peptidase 5) is expressed at high levels by stromal fibroblast, endothelial, and tumor cells in a variety of invasive tumors but is undetectable in the majority of normal adult tissues.
Impact of fibroblast activation protein on osteosarcoma cell lines in vitro.
Jiang et al., Cardiff, United Kingdom. In Oncol Lett, 2014
Fibroblast activation protein (FAP) or seprase, which belongs to the group type II integral serine proteases, is an integral membrane serine peptidase.
FAP-α (Fibroblast activation protein-α) is involved in the control of human breast cancer cell line growth and motility via the FAK pathway.
Jiang et al., Cardiff, United Kingdom. In Bmc Cell Biol, 2013
BACKGROUND: Fibroblast Activation Protein alpha (FAP-α) or seprase is an integral membrane serine peptidase.
Fibroblast activation protein α–specific, near-infrared peptide probe (KGPGPNQC) linked to Cy5.5 and a quencher dye, QSY21
Chopra, 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).
Targeting carcinoma-associated fibroblasts within the tumor stroma with a fibroblast activation protein-activated prodrug.
Denmeade et al., Baltimore, United States. In J Natl Cancer Inst, 2012
Study validates the proteolytic activity of FAP as a target for the activation of a systemically delivered cytotoxic prodrug.
Fibroblast activation protein regulates tumor-associated fibroblasts and epithelial ovarian cancer cells.
Wang et al., Shanghai, China. In Int J Oncol, 2012
FAP is an important regulator of the microenvironment in tumor formation
Comparative analysis of the substrate preferences of two post-proline cleaving endopeptidases, prolyl oligopeptidase and fibroblast activation protein α.
Galande et al., Harrisonburg, United States. In Febs Lett, 2012
analysis of the substrate preferences of two post-proline cleaving endopeptidases, prolyl oligopeptidase and fibroblast activation protein alpha
Expression of fibroblast activation protein in human pancreatic adenocarcinoma and its clinicopathological significance.
Zhu et al., Shanghai, China. In World J Gastroenterol, 2012
Data show that fibroblast activation protein is highly expressed in carcinoma cells and fibroblasts in PDAC tissues, and its expression is associated with desmoplasia and worse prognosis.
Plasma seprase and DPP4 levels as markers of disease and prognosis in cancer.
Chen et al., Stony Brook, United States. In Dis Markers, 2011
Higher plasma seprase was associated with better survival in all non-metastatic cancers combined.
[Expression of fibroblast activation protein in HBV related hepatocellular carcinoma].
Li et al., Guangzhou, China. In Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi, 2011
FAP may play an important role in the occurrence and development of HBV related hepatocellular carcinoma.
Transmigration of melanoma cells through the blood-brain barrier: role of endothelial tight junctions and melanoma-released serine proteases.
Krizbai et al., Szeged, Hungary. In Plos One, 2010
During this process melanoma cells produced and released large amounts of proteolytic enzymes, mainly gelatinolytic serine proteases, including seprase.
The prolyl-aminodipeptidases and their inhibitors as therapeutic targets for fibrogenic disorders.
Gerber-Lemaire et al., Lausanne, Switzerland. In Mini Rev Med Chem, 2009
Prolyl-specific aminodipeptidases include dipeptidyl-aminodipeptidase IV (DPP IV)/CD26, DPP8, DPP9 and fibroblast activation protease-alpha (FAP-alpha)/seprase, able to release X-Pro dipeptides from the N-terminus of peptides.
Alpha2-antiplasmin: potential therapeutic roles in fibrin survival and removal.
McKee et al., Oklahoma City, United States. In Curr Med Chem Cardiovasc Hematol Agents, 2004
The antiplasmin-cleaving enzyme has similarity in primary structure and catalytic properties to fibroblast activation protein/seprase.
Dipeptidyl peptidase IV activity and/or structure homologues (DASH) and their substrates in cancer.
Sedo et al., 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.
Prolyl peptidases: a serine protease subfamily with high potential for drug discovery.
Kozarich et al., Los Angeles, United States. In Curr Opin Chem Biol, 2003
This class includes dipeptidyl peptidase IV (DPP IV; also termed CD26), fibroblast activation protein alpha (FAP; seprase), DPP7 (DPP II; quiescent cell proline dipeptidase), DPP8, DPP9, and prolyl carboxypeptidase (PCP; angiotensinase C).
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