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proteins. Page last changed on 14 Mar 2013.
Fibroblast activation protein, alpha
seprase
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)
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Papers on
seprase
Fibroblast activation protein α–specific, near-infrared peptide probe (KGPGPNQC) linked to Cy5.5 and a quencher dye, QSY21
New
Bethesda, United States. In Unknown Journal, Dec 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).
Expression of fibroblast activation protein in human pancreatic adenocarcinoma and its clinicopathological significance.
New
Shanghai, China. In World J Gastroenterol, Mar 2012
OBJECTIVE: To examine fibroblast activation protein (FAP) expression in pancreatic ductal adenocarcinoma (PDAC) and to analyze its relationship with the clinicopathology of PDAC.
Plasma seprase and DPP4 levels as markers of disease and prognosis in cancer.
Stony Brook, United States. In Dis Markers, 2011
Seprase (fibroblast activation protein α) has been examined as an invasion biomarker for various types of solid tumors.
Coupled expression of dipeptidyl peptidase-IV and fibroblast activation protein-α in transformed astrocytic cells.
GeneRIF
Praha, Czech Republic. In Mol Cell Biochem, 2011
the associated dynamics of DPP-IV and FAP gene expression in glioblastoma cells further argues in favor of their putative joint involvement in biological processes
Fibroblast activation protein-α promotes tumor growth and invasion of breast cancer cells through non-enzymatic functions.
GeneRIF
Little Rock, United States. In Clin Exp Metastasis, 2011
Authors conclude that the proteolytic activity of FAP participates in matrix degradation, but other functions of the protein stimulate increased tumor growth.
Ultraviolet exposure of melanoma cells induces fibroblast activation protein-α in fibroblasts: Implications for melanoma invasion.
GeneRIF
Linköping, Sweden. In Int J Oncol, 2011
These experiments suggest a functional association between UVR and FAP-alpha expression that UVR of malignant melanoma converts fibroblasts into FAP-alpha expressing and ECM degrading fibroblasts thus facilitating invasion and migration.
Expression and role of the cell surface protease seprase/fibroblast activation protein-α (FAP-α) in astroglial tumors.
Kiel, Germany. In Biol Chem, 2011
Seprase or fibroblast activation protein-α (FAP-α) is a cell-surface serine protease that was previously described nearly exclusively on reactive and tumor stromal fibroblasts and thought to be involved in tissue remodeling.
A combination of serum markers for the early detection of colorectal cancer.
Penzberg, Germany. In Clin Cancer Res, 2011
Six markers were selected for a marker combination, including the known tumor markers CEA (carcinoembryonic antigen) and CYFRA 21-1 as well as novel markers or markers that are less routinely used for the detection of CRC: ferritin, osteopontin (OPN), anti-p53, and seprase.
FAP-overexpressing fibroblasts produce an extracellular matrix that enhances invasive velocity and directionality of pancreatic cancer cells.
GeneRIF
Philadelphia, United States. In Bmc Cancer, 2010
In NIH 3T3 cells overexpressing recombinant mouse FAP, FAP enzymatic activity during matrix production is important for the topographical organization of the ECM fibers.
Expression and role of fibroblast activation protein-alpha in microinvasive breast carcinoma.
GeneRIF
Guangzhou, China. In Diagn Pathol, 2010
immunostaining with FAP-alpha and Calponin can serve as a novel marker for pathologically diagnosing whether ductal carcinoma in situ has microinvasion.
Transmigration of melanoma cells through the blood-brain barrier: role of endothelial tight junctions and melanoma-released serine proteases.
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.
Histogenesis-specific expression of fibroblast activation protein and dipeptidylpeptidase-IV in human bone and soft tissue tumours.
GeneRIF
Sendai, Japan. In Histopathology, 2009
data suggest that FAP and DPP-IV are consistently expressed in bone and soft tissue tumour cells that are histogenetically related to activated fibroblasts and/or myofibroblasts, irrespective of their malignancy.
Peritumoral activated hepatic stellate cells predict poor clinical outcome in hepatocellular carcinoma after curative resection.
Shanghai, China. In Am J Clin Pathol, 2009
The messenger RNA (mRNA) levels of the functional genes in HSCs (ie, seprase, osteonectin, and tenascin-C), quantitated by real-time quantitative polymerase chain reaction, and the density of peritumoral Foxp3+ T-regulatory cells (Tregs) and CD68+ macrophages (MPhi), assessed immunohistochemically in tissue microarray sections, were positively correlated with the density of peritumoral activated HSCs.
The prolyl-aminodipeptidases and their inhibitors as therapeutic targets for fibrogenic disorders.
Review
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.
Elevation of seprase expression and promotion of an invasive phenotype by collagenous matrices in ovarian tumor cells.
GeneRIF
Stony Brook, United States. In Int J Cancer, 2009
seprase may have a role in promotion of an invasive phenotype by collagenous matrices in ovarian tumor cells
Seprase, dipeptidyl peptidase IV and urokinase-type plasminogen activator expression in dysplasia and invasive squamous cell carcinoma of the esophagus. A study of 229 cases from Anyang Tumor Hospital, Henan Province, China.
Oslo, Norway. In Oncology, 2007
OBJECTIVE: Seprase, dipeptidyl peptidase IV (DPPIV) and urokinase-type plasminogen activator (uPA) play a crucial role in the degradation of the extracellular matrix and in the progression of various human tumors.
Alpha2-antiplasmin: potential therapeutic roles in fibrin survival and removal.
Review
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.
Review
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.
Review
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).
Seprase complexes in cellular invasiveness.
Review
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.
