Prolyl endopeptidase FAP is a 170 kDa membrane-bound gelatinase. It was independently identified as a surface glycoprotein recognized by the F19 monoclonal antibody in activated fibroblasts[6] and a Surface Expressed Protease (seprase) in invasive melanoma cells.[7][8]
FAP is a 760 amino acid long type II transmembrane glycoprotein. It contains a very short cytoplasmic N terminal part (6 amino acids), a transmembrane region (amino acids 7–26), and a large extracellular part with an alpha/beta-hydrolase domain and an eight-bladed beta-propeller domain.[9][10]
A soluble form of FAP, which lacks the intracellular and transmembrane part, is present in blood plasma.[11] FAP is a non-classical serine protease, which belongs to the S9B prolyl oligopeptidase subfamily. Other members of the S9B subfamily are DPPIV, DPP8 and DPP9.[12] FAP is most closely related to DPPIV (approximately 50% of their amino acids are identical). The active site of FAP is localized in the extracellular part of the protein and contains a catalytic triad composed of Ser624 Asp702 His734 in humans and mice.[10] FAP is catalytically active as a 170kD homodimer and has a dipeptidase and an endopeptidase activity.
Several bioactive peptides and structural proteins were reported to be cleaved by FAP, such as neuropeptide Y (NPY), Peptide YY, Substance P (SP), and B-type natriuretic peptide (BNP),[13] human fibroblast growth factor 21 (FGF-21), human alpha2 antiplasmin and denatured collagen I and III. NPY, FGF-21 and alpha2 antiplasmin are considered to be physiological FAP substrates.[14][15]
Expression and possible functionEdit
FAP expression under physiological conditions is very low in the majority of adult tissues. FAP is nevertheless expressed during embryonic development,[16] and in adults in pancreatic alpha cells[17] in multipotent bone marrow stromal cells (BM-MSC)[18] and uterine stroma.[19]
FAP expression is high in reactive stromalfibroblasts of epithelial cancers, granulation tissue of healing wounds, and malignant cells of bone and soft tissue sarcomas. FAP is thought to be involved in the control of fibroblast growth or epithelial-mesenchymal interactions during development, tissue repair, and epithelial carcinogenesis.[5]
Clinical significanceEdit
FAP expression is seen on activated stromal fibroblasts of more than 90% of all human carcinomas.[14][15] Stromal fibroblasts play an important role in the development, growth and metastasis of carcinomas. Several approaches of FAP targeting mainly in cancer treatment are currently being tested including the use of low molecular weight inhibitors, prodrugs activated by FAP, various anti-FAP antibodies and their conjugates, FAP-CAR T cells, and FAP vaccines.[15]
By cleaving FGF-21, FAP is also thought to play a possible role in energy metabolism.[20]
Talabostat is an inhibitor of FAP and related enzymes, for which clinical trials have been done, but further research is suspended.
Sibrotuzumab is a monoclonal antibody against FAP.
ReferencesEdit
^ abcGRCh38: Ensembl release 89: ENSG00000078098 - Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000000392 - Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Garin-Chesa P, Old LJ, Rettig WJ (September 1990). "Cell surface glycoprotein of reactive stromal fibroblasts as a potential antibody target in human epithelial cancers". Proceedings of the National Academy of Sciences of the United States of America. 87 (18): 7235–9. Bibcode:1990PNAS...87.7235G. doi:10.1073/pnas.87.18.7235. PMC54718. PMID 2402505.
^Monsky WL, Lin CY, Aoyama A, Kelly T, Akiyama SK, Mueller SC, Chen WT (November 1994). "A potential marker protease of invasiveness, seprase, is localized on invadopodia of human malignant melanoma cells". Cancer Research. 54 (21): 5702–10. PMID 7923219.
^Aoyama A, Chen WT (November 1990). "A 170-kDa membrane-bound protease is associated with the expression of invasiveness by human malignant melanoma cells". Proceedings of the National Academy of Sciences of the United States of America. 87 (21): 8296–300. Bibcode:1990PNAS...87.8296A. doi:10.1073/pnas.87.21.8296. PMC54942. PMID 2172980.
^PDB: 1Z68; Aertgeerts K, Levin I, Shi L, Snell GP, Jennings A, Prasad GS, Zhang Y, Kraus ML, Salakian S, Sridhar V, Wijnands R, Tennant MG (May 2005). "Structural and kinetic analysis of the substrate specificity of human fibroblast activation protein alpha". The Journal of Biological Chemistry. 280 (20): 19441–4. doi:10.1074/jbc.C500092200. PMID 15809306. S2CID 25810686.
^ abGoldstein LA, Ghersi G, Piñeiro-Sánchez ML, Salamone M, Yeh Y, Flessate D, Chen WT (July 1997). "Molecular cloning of seprase: a serine integral membrane protease from human melanoma". Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1361 (1): 11–9. doi:10.1016/S0925-4439(97)00032-X. PMID 9247085.
^Lee KN, Jackson KW, Christiansen VJ, Lee CS, Chun JG, McKee PA (February 2006). "Antiplasmin-cleaving enzyme is a soluble form of fibroblast activation protein". Blood. 107 (4): 1397–404. doi:10.1182/blood-2005-08-3452. PMID 16223769. S2CID 17654245.
^Keane FM, Nadvi NA, Yao TW, Gorrell MD (April 2011). "Neuropeptide Y, B-type natriuretic peptide, substance P and peptide YY are novel substrates of fibroblast activation protein-α". The FEBS Journal. 278 (8): 1316–32. doi:10.1111/j.1742-4658.2011.08051.x. PMID 21314817. S2CID 33826473.
^ abPuré E, Blomberg R (August 2018). "Pro-tumorigenic roles of fibroblast activation protein in cancer: back to the basics". Oncogene. 37 (32): 4343–4357. doi:10.1038/s41388-018-0275-3. PMC6092565. PMID 29720723.
^ abcBusek P, Mateu R, Zubal M, Kotackova L, Sedo A (June 2018). "Targeting fibroblast activation protein in cancer - Prospects and caveats". Frontiers in Bioscience. 23 (10): 1933–1968. doi:10.2741/4682. PMID 29772538.
^Niedermeyer J, Garin-Chesa P, Kriz M, Hilberg F, Mueller E, Bamberger U, Rettig WJ, Schnapp A (April 2001). "Expression of the fibroblast activation protein during mouse embryo development". The International Journal of Developmental Biology. 45 (2): 445–7. PMID 11330865.
^Busek P, Hrabal P, Fric P, Sedo A (May 2015). "Co-expression of the homologous proteases fibroblast activation protein and dipeptidyl peptidase-IV in the adult human Langerhans islets". Histochemistry and Cell Biology. 143 (5): 497–504. doi:10.1007/s00418-014-1292-0. PMID 25361590. S2CID 788806.
^Bae S, Park CW, Son HK, Ju HK, Paik D, Jeon CJ, Koh GY, Kim J, Kim H (September 2008). "Fibroblast activation protein alpha identifies mesenchymal stromal cells from human bone marrow". British Journal of Haematology. 142 (5): 827–30. doi:10.1111/j.1365-2141.2008.07241.x. PMID 18510677. S2CID 40643695.
^Dolznig H, Schweifer N, Puri C, Kraut N, Rettig WJ, Kerjaschki D, Garin-Chesa P (August 2005). "Characterization of cancer stroma markers: in silico analysis of an mRNA expression database for fibroblast activation protein and endosialin". Cancer Immunity. 5: 10. PMID 16076089.
^Sánchez-Garrido MA, Habegger KM, Clemmensen C, Holleman C, Müller TD, Perez-Tilve D, Li P, Agrawal AS, Finan B, Drucker DJ, Tschöp MH, DiMarchi RD, Kharitonenkov A (October 2016). "Fibroblast activation protein (FAP) as a novel metabolic target". Molecular Metabolism. 5 (10): 1015–1024. doi:10.1016/j.molmet.2016.07.003. PMC5034526. PMID 27689014.
Further readingEdit
Rettig WJ, Su SL, Fortunato SR, Scanlan MJ, Raj BK, Garin-Chesa P, Healey JH, Old LJ (August 1994). "Fibroblast activation protein: purification, epitope mapping and induction by growth factors". International Journal of Cancer. 58 (3): 385–92. doi:10.1002/ijc.2910580314. PMID 7519584. S2CID 26488735.
Mathew S, Scanlan MJ, Mohan Raj BK, Murty VV, Garin-Chesa P, Old LJ, Rettig WJ, Chaganti RS (January 1995). "The gene for fibroblast activation protein alpha (FAP), a putative cell surface-bound serine protease expressed in cancer stroma and wound healing, maps to chromosome band 2q23". Genomics. 25 (1): 335–7. doi:10.1016/0888-7543(95)80157-H. PMID 7774951.
Scanlan MJ, Raj BK, Calvo B, Garin-Chesa P, Sanz-Moncasi MP, Healey JH, Old LJ, Rettig WJ (June 1994). "Molecular cloning of fibroblast activation protein alpha, a member of the serine protease family selectively expressed in stromal fibroblasts of epithelial cancers". Proceedings of the National Academy of Sciences of the United States of America. 91 (12): 5657–61. Bibcode:1994PNAS...91.5657S. doi:10.1073/pnas.91.12.5657. PMC44055. PMID 7911242.
Piñeiro-Sánchez ML, Goldstein LA, Dodt J, Howard L, Yeh Y, Tran H, Argraves WS, Chen WT (March 1997). "Identification of the 170-kDa melanoma membrane-bound gelatinase (seprase) as a serine integral membrane protease". The Journal of Biological Chemistry. 272 (12): 7595–601. doi:10.1074/jbc.272.12.7595. PMID 9065413. S2CID 27391619.
Goldstein LA, Ghersi G, Piñeiro-Sánchez ML, Salamone M, Yeh Y, Flessate D, Chen WT (July 1997). "Molecular cloning of seprase: a serine integral membrane protease from human melanoma". Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease. 1361 (1): 11–9. doi:10.1016/s0925-4439(97)00032-x. PMID 9247085.
Goldstein LA, Chen WT (January 2000). "Identification of an alternatively spliced seprase mRNA that encodes a novel intracellular isoform". The Journal of Biological Chemistry. 275 (4): 2554–9. doi:10.1074/jbc.275.4.2554. PMID 10644713. S2CID 45385101.
Ghersi G, Dong H, Goldstein LA, Yeh Y, Hakkinen L, Larjava HS, Chen WT (August 2002). "Regulation of fibroblast migration on collagenous matrix by a cell surface peptidase complex". The Journal of Biological Chemistry. 277 (32): 29231–41. doi:10.1074/jbc.M202770200. PMID 12023964. S2CID 23470018.
Levy MT, McCaughan GW, Marinos G, Gorrell MD (April 2002). "Intrahepatic expression of the hepatic stellate cell marker fibroblast activation protein correlates with the degree of fibrosis in hepatitis C virus infection". Liver. 22 (2): 93–101. doi:10.1034/j.1600-0676.2002.01503.x. PMID 12028401.
Artym VV, Kindzelskii AL, Chen WT, Petty HR (October 2002). "Molecular proximity of seprase and the urokinase-type plasminogen activator receptor on malignant melanoma cell membranes: dependence on beta1 integrins and the cytoskeleton". Carcinogenesis. 23 (10): 1593–601. doi:10.1093/carcin/23.10.1593. PMID 12376466.
Gorrell MD, Wang XM, Levy MT, Kable E, Marinos G, Cox G, McCaughan GW (2004). "Intrahepatic Expression of Collagen and Fibroblast Activation Protein (FAP) in Hepatitis C Virus Infection". Dipeptidyl Aminopeptidases in Health and Disease. Advances in Experimental Medicine and Biology. Vol. 524. pp. 235–43. CiteSeerX10.1.1.535.3436. doi:10.1007/0-306-47920-6_28. ISBN978-0-306-47717-1. PMID 12675244.
Jin X, Iwasa S, Okada K, Mitsumata M, Ooi A (2003). "Expression patterns of seprase, a membrane serine protease, in cervical carcinoma and cervical intraepithelial neoplasm". Anticancer Research. 23 (4): 3195–8. PMID 12926053.
Iwasa S, Jin X, Okada K, Mitsumata M, Ooi A (September 2003). "Increased expression of seprase, a membrane-type serine protease, is associated with lymph node metastasis in human colorectal cancer". Cancer Letters. 199 (1): 91–8. doi:10.1016/S0304-3835(03)00315-X. PMID 12963128.
Goodman JD, Rozypal TL, Kelly T (2003). "Seprase, a membrane-bound protease, alleviates the serum growth requirement of human breast cancer cells". Clinical & Experimental Metastasis. 20 (5): 459–70. doi:10.1023/A:1025493605850. PMID 14524536. S2CID 1511984.
Okada K, Chen WT, Iwasa S, Jin X, Yamane T, Ooi A, Mitsumata M (2004). "Seprase, a membrane-type serine protease, has different expression patterns in intestinal- and diffuse-type gastric cancer". Oncology. 65 (4): 363–70. doi:10.1159/000074650. PMID 14707457. S2CID 41823279.
Cheng JD, Valianou M, Canutescu AA, Jaffe EK, Lee HO, Wang H, Lai JH, Bachovchin WW, Weiner LM (March 2005). "Abrogation of fibroblast activation protein enzymatic activity attenuates tumor growth". Molecular Cancer Therapeutics. 4 (3): 351–60. doi:10.1158/1535-7163.MCT-04-0269. PMID 15767544.
Aertgeerts K, Levin I, Shi L, Snell GP, Jennings A, Prasad GS, Zhang Y, Kraus ML, Salakian S, Sridhar V, Wijnands R, Tennant MG (May 2005). "Structural and kinetic analysis of the substrate specificity of human fibroblast activation protein alpha". The Journal of Biological Chemistry. 280 (20): 19441–4. doi:10.1074/jbc.C500092200. PMID 15809306. S2CID 25810686.
Fassnacht M, Lee J, Milazzo C, Boczkowski D, Su Z, Nair S, Gilboa E (August 2005). "Induction of CD4(+) and CD8(+) T-cell responses to the human stromal antigen, fibroblast activation protein: implication for cancer immunotherapy". Clinical Cancer Research. 11 (15): 5566–71. doi:10.1158/1078-0432.CCR-05-0699. PMID 16061874. S2CID 13455377.
External linksEdit
Overview of all the structural information available in the PDB for UniProt: Q12884 (Human Prolyl endopeptidase FAP) at the PDBe-KB.
fibroblast, activation, protein, alpha, fibroblast, activation, protein, alpha, alpha, also, known, prolyl, endopeptidase, enzyme, that, humans, encoded, gene, fapavailable, structurespdbortholog, search, pdbe, rcsblist, codes1z68identifiersaliasesfap, dppiv, . Fibroblast activation protein alpha FAP alpha also known as prolyl endopeptidase FAP is an enzyme that in humans is encoded by the FAP gene 5 FAPAvailable structuresPDBOrtholog search PDBe RCSBList of PDB id codes1Z68IdentifiersAliasesFAP DPPIV FAPA SIMP fibroblast activation protein alpha FAPalphaExternal IDsOMIM 600403 MGI 109608 HomoloGene 48282 GeneCards FAPEC number3 4 14 5Gene location Human Chr Chromosome 2 human 1 Band2q24 2Start162 170 684 bp 1 End162 245 151 bp 1 Gene location Mouse Chr Chromosome 2 mouse 2 Band2 C1 3 2 35 85 cMStart62 331 287 bp 2 End62 404 419 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed instromal cell of endometriumislet of Langerhanssmooth muscle tissuegallbladdermyometriumright coronary arteryascending aortacanal of the cervixleft coronary arteryvisceral pleuraTop expressed inbody of femurretinal pigment epitheliuminternal carotid arteryexternal carotid arterysquamous epitheliummesotheliumanklecalvariaintercostal musclenoseMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionprotein dimerization activity protein homodimerization activity endopeptidase activity protease binding integrin binding peptidase activity protein binding serine type peptidase activity metalloendopeptidase activity serine type endopeptidase activity hydrolase activity dipeptidyl peptidase activityCellular componentcytoplasm integral component of membrane cell projection membrane focal adhesion basal part of cell plasma membrane apical part of cell ruffle membrane extracellular region cell surface cell junction lamellipodium membrane lamellipodium extracellular spaceBiological processpositive regulation of execution phase of apoptosis regulation of collagen catabolic process melanocyte apoptotic process negative regulation of extracellular matrix disassembly negative regulation of extracellular matrix organization proteolysis cell adhesion negative regulation of cell proliferation involved in contact inhibition angiogenesis melanocyte proliferation proteolysis involved in cellular protein catabolic process regulation of fibrinolysis endothelial cell migration apoptotic processSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez219114089EnsemblENSG00000078098ENSMUSG00000000392UniProtQ12884P97321RefSeq mRNA NM 001291807NM 004460NM 007986RefSeq protein NP 001278736NP 004451NP 032012Location UCSC Chr 2 162 17 162 25 MbChr 2 62 33 62 4 MbPubMed search 3 4 WikidataView Edit HumanView Edit MouseProlyl endopeptidase FAP is a 170 kDa membrane bound gelatinase It was independently identified as a surface glycoprotein recognized by the F19 monoclonal antibody in activated fibroblasts 6 and a Surface Expressed Protease seprase in invasive melanoma cells 7 8 Contents 1 Structure and enzymatic activity 2 Expression and possible function 3 Clinical significance 4 References 5 Further reading 6 External linksStructure and enzymatic activity EditFAP is a 760 amino acid long type II transmembrane glycoprotein It contains a very short cytoplasmic N terminal part 6 amino acids a transmembrane region amino acids 7 26 and a large extracellular part with an alpha beta hydrolase domain and an eight bladed beta propeller domain 9 10 A soluble form of FAP which lacks the intracellular and transmembrane part is present in blood plasma 11 FAP is a non classical serine protease which belongs to the S9B prolyl oligopeptidase subfamily Other members of the S9B subfamily are DPPIV DPP8 and DPP9 12 FAP is most closely related to DPPIV approximately 50 of their amino acids are identical The active site of FAP is localized in the extracellular part of the protein and contains a catalytic triad composed of Ser624 Asp702 His734 in humans and mice 10 FAP is catalytically active as a 170kD homodimer and has a dipeptidase and an endopeptidase activity Several bioactive peptides and structural proteins were reported to be cleaved by FAP such as neuropeptide Y NPY Peptide YY Substance P SP and B type natriuretic peptide BNP 13 human fibroblast growth factor 21 FGF 21 human alpha2 antiplasmin and denatured collagen I and III NPY FGF 21 and alpha2 antiplasmin are considered to be physiological FAP substrates 14 15 Expression and possible function EditFAP expression under physiological conditions is very low in the majority of adult tissues FAP is nevertheless expressed during embryonic development 16 and in adults in pancreatic alpha cells 17 in multipotent bone marrow stromal cells BM MSC 18 and uterine stroma 19 FAP expression is high in reactive stromal fibroblasts of epithelial cancers granulation tissue of healing wounds and malignant cells of bone and soft tissue sarcomas FAP is thought to be involved in the control of fibroblast growth or epithelial mesenchymal interactions during development tissue repair and epithelial carcinogenesis 5 Clinical significance EditFAP expression is seen on activated stromal fibroblasts of more than 90 of all human carcinomas 14 15 Stromal fibroblasts play an important role in the development growth and metastasis of carcinomas Several approaches of FAP targeting mainly in cancer treatment are currently being tested including the use of low molecular weight inhibitors prodrugs activated by FAP various anti FAP antibodies and their conjugates FAP CAR T cells and FAP vaccines 15 By cleaving FGF 21 FAP is also thought to play a possible role in energy metabolism 20 Talabostat is an inhibitor of FAP and related enzymes for which clinical trials have been done but further research is suspended Sibrotuzumab is a monoclonal antibody against FAP References Edit a b c GRCh38 Ensembl release 89 ENSG00000078098 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000000392 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine a b Entrez Gene fibroblast activation protein alpha Garin Chesa P Old LJ Rettig WJ September 1990 Cell surface glycoprotein of reactive stromal fibroblasts as a potential antibody target in human epithelial cancers Proceedings of the National Academy of Sciences of the United States of America 87 18 7235 9 Bibcode 1990PNAS 87 7235G doi 10 1073 pnas 87 18 7235 PMC 54718 PMID 2402505 Monsky WL Lin CY Aoyama A Kelly T Akiyama SK Mueller SC Chen WT November 1994 A potential marker protease of invasiveness seprase is localized on invadopodia of human malignant melanoma cells Cancer Research 54 21 5702 10 PMID 7923219 Aoyama A Chen WT November 1990 A 170 kDa membrane bound protease is associated with the expression of invasiveness by human malignant melanoma cells Proceedings of the National Academy of Sciences of the United States of America 87 21 8296 300 Bibcode 1990PNAS 87 8296A doi 10 1073 pnas 87 21 8296 PMC 54942 PMID 2172980 PDB 1Z68 Aertgeerts K Levin I Shi L Snell GP Jennings A Prasad GS Zhang Y Kraus ML Salakian S Sridhar V Wijnands R Tennant MG May 2005 Structural and kinetic analysis of the substrate specificity of human fibroblast activation protein alpha The Journal of Biological Chemistry 280 20 19441 4 doi 10 1074 jbc C500092200 PMID 15809306 S2CID 25810686 a b Goldstein LA Ghersi G Pineiro Sanchez ML Salamone M Yeh Y Flessate D Chen WT July 1997 Molecular cloning of seprase a serine integral membrane protease from human melanoma Biochimica et Biophysica Acta BBA Molecular Basis of Disease 1361 1 11 9 doi 10 1016 S0925 4439 97 00032 X PMID 9247085 Lee KN Jackson KW Christiansen VJ Lee CS Chun JG McKee PA February 2006 Antiplasmin cleaving enzyme is a soluble form of fibroblast activation protein Blood 107 4 1397 404 doi 10 1182 blood 2005 08 3452 PMID 16223769 S2CID 17654245 Merops the peptidase database Keane FM Nadvi NA Yao TW Gorrell MD April 2011 Neuropeptide Y B type natriuretic peptide substance P and peptide YY are novel substrates of fibroblast activation protein a The FEBS Journal 278 8 1316 32 doi 10 1111 j 1742 4658 2011 08051 x PMID 21314817 S2CID 33826473 a b Pure E Blomberg R August 2018 Pro tumorigenic roles of fibroblast activation protein in cancer back to the basics Oncogene 37 32 4343 4357 doi 10 1038 s41388 018 0275 3 PMC 6092565 PMID 29720723 a b c Busek P Mateu R Zubal M Kotackova L Sedo A June 2018 Targeting fibroblast activation protein in cancer Prospects and caveats Frontiers in Bioscience 23 10 1933 1968 doi 10 2741 4682 PMID 29772538 Niedermeyer J Garin Chesa P Kriz M Hilberg F Mueller E Bamberger U Rettig WJ Schnapp A April 2001 Expression of the fibroblast activation protein during mouse embryo development The International Journal of Developmental Biology 45 2 445 7 PMID 11330865 Busek P Hrabal P Fric P Sedo A May 2015 Co expression of the homologous proteases fibroblast activation protein and dipeptidyl peptidase IV in the adult human Langerhans islets Histochemistry and Cell Biology 143 5 497 504 doi 10 1007 s00418 014 1292 0 PMID 25361590 S2CID 788806 Bae S Park CW Son HK Ju HK Paik D Jeon CJ Koh GY Kim J Kim H September 2008 Fibroblast activation protein alpha identifies mesenchymal stromal cells from human bone marrow British Journal of Haematology 142 5 827 30 doi 10 1111 j 1365 2141 2008 07241 x PMID 18510677 S2CID 40643695 Dolznig H Schweifer N Puri C Kraut N Rettig WJ Kerjaschki D Garin Chesa P August 2005 Characterization of cancer stroma markers in silico analysis of an mRNA expression database for fibroblast activation protein and endosialin Cancer Immunity 5 10 PMID 16076089 Sanchez Garrido MA Habegger KM Clemmensen C Holleman C Muller TD Perez Tilve D Li P Agrawal AS Finan B Drucker DJ Tschop MH DiMarchi RD Kharitonenkov A October 2016 Fibroblast activation protein FAP as a novel metabolic target Molecular Metabolism 5 10 1015 1024 doi 10 1016 j molmet 2016 07 003 PMC 5034526 PMID 27689014 Further reading EditRettig WJ Su SL Fortunato SR Scanlan MJ Raj BK Garin Chesa P Healey JH Old LJ August 1994 Fibroblast activation protein purification epitope mapping and induction by growth factors International Journal of Cancer 58 3 385 92 doi 10 1002 ijc 2910580314 PMID 7519584 S2CID 26488735 Mathew S Scanlan MJ Mohan Raj BK Murty VV Garin Chesa P Old LJ Rettig WJ Chaganti RS January 1995 The gene for fibroblast activation protein alpha FAP a putative cell surface bound serine protease expressed in cancer stroma and wound healing maps to chromosome band 2q23 Genomics 25 1 335 7 doi 10 1016 0888 7543 95 80157 H PMID 7774951 Scanlan MJ Raj BK Calvo B Garin Chesa P Sanz Moncasi MP Healey JH Old LJ Rettig WJ June 1994 Molecular cloning of fibroblast activation protein alpha a member of the serine protease family selectively expressed in stromal fibroblasts of epithelial cancers Proceedings of the National Academy of Sciences of the United States of America 91 12 5657 61 Bibcode 1994PNAS 91 5657S doi 10 1073 pnas 91 12 5657 PMC 44055 PMID 7911242 Pineiro Sanchez ML Goldstein LA Dodt J Howard L Yeh Y Tran H Argraves WS Chen WT March 1997 Identification of the 170 kDa melanoma membrane bound gelatinase seprase as a serine integral membrane protease The Journal of Biological Chemistry 272 12 7595 601 doi 10 1074 jbc 272 12 7595 PMID 9065413 S2CID 27391619 Goldstein LA Ghersi G Pineiro Sanchez ML Salamone M Yeh Y Flessate D Chen WT July 1997 Molecular cloning of seprase a serine integral membrane protease from human melanoma Biochimica et Biophysica Acta BBA Molecular Basis of Disease 1361 1 11 9 doi 10 1016 s0925 4439 97 00032 x PMID 9247085 Goldstein LA Chen WT January 2000 Identification of an alternatively spliced seprase mRNA that encodes a novel intracellular isoform The Journal of Biological Chemistry 275 4 2554 9 doi 10 1074 jbc 275 4 2554 PMID 10644713 S2CID 45385101 Ghersi G Dong H Goldstein LA Yeh Y Hakkinen L Larjava HS Chen WT August 2002 Regulation of fibroblast migration on collagenous matrix by a cell surface peptidase complex The Journal of Biological Chemistry 277 32 29231 41 doi 10 1074 jbc M202770200 PMID 12023964 S2CID 23470018 Levy MT McCaughan GW Marinos G Gorrell MD April 2002 Intrahepatic expression of the hepatic stellate cell marker fibroblast activation protein correlates with the degree of fibrosis in hepatitis C virus infection Liver 22 2 93 101 doi 10 1034 j 1600 0676 2002 01503 x PMID 12028401 Artym VV Kindzelskii AL Chen WT Petty HR October 2002 Molecular proximity of seprase and the urokinase type plasminogen activator receptor on malignant melanoma cell membranes dependence on beta1 integrins and the cytoskeleton Carcinogenesis 23 10 1593 601 doi 10 1093 carcin 23 10 1593 PMID 12376466 Gorrell MD Wang XM Levy MT Kable E Marinos G Cox G McCaughan GW 2004 Intrahepatic Expression of Collagen and Fibroblast Activation Protein FAP in Hepatitis C Virus Infection Dipeptidyl Aminopeptidases in Health and Disease Advances in Experimental Medicine and Biology Vol 524 pp 235 43 CiteSeerX 10 1 1 535 3436 doi 10 1007 0 306 47920 6 28 ISBN 978 0 306 47717 1 PMID 12675244 Jin X Iwasa S Okada K Mitsumata M Ooi A 2003 Expression patterns of seprase a membrane serine protease in cervical carcinoma and cervical intraepithelial neoplasm Anticancer Research 23 4 3195 8 PMID 12926053 Iwasa S Jin X Okada K Mitsumata M Ooi A September 2003 Increased expression of seprase a membrane type serine protease is associated with lymph node metastasis in human colorectal cancer Cancer Letters 199 1 91 8 doi 10 1016 S0304 3835 03 00315 X PMID 12963128 Goodman JD Rozypal TL Kelly T 2003 Seprase a membrane bound protease alleviates the serum growth requirement of human breast cancer cells Clinical amp Experimental Metastasis 20 5 459 70 doi 10 1023 A 1025493605850 PMID 14524536 S2CID 1511984 Okada K Chen WT Iwasa S Jin X Yamane T Ooi A Mitsumata M 2004 Seprase a membrane type serine protease has different expression patterns in intestinal and diffuse type gastric cancer Oncology 65 4 363 70 doi 10 1159 000074650 PMID 14707457 S2CID 41823279 Cheng JD Valianou M Canutescu AA Jaffe EK Lee HO Wang H Lai JH Bachovchin WW Weiner LM March 2005 Abrogation of fibroblast activation protein enzymatic activity attenuates tumor growth Molecular Cancer Therapeutics 4 3 351 60 doi 10 1158 1535 7163 MCT 04 0269 PMID 15767544 Aertgeerts K Levin I Shi L Snell GP Jennings A Prasad GS Zhang Y Kraus ML Salakian S Sridhar V Wijnands R Tennant MG May 2005 Structural and kinetic analysis of the substrate specificity of human fibroblast activation protein alpha The Journal of Biological Chemistry 280 20 19441 4 doi 10 1074 jbc C500092200 PMID 15809306 S2CID 25810686 Fassnacht M Lee J Milazzo C Boczkowski D Su Z Nair S Gilboa E August 2005 Induction of CD4 and CD8 T cell responses to the human stromal antigen fibroblast activation protein implication for cancer immunotherapy Clinical Cancer Research 11 15 5566 71 doi 10 1158 1078 0432 CCR 05 0699 PMID 16061874 S2CID 13455377 External links EditOverview of all the structural information available in the PDB for UniProt Q12884 Human Prolyl endopeptidase FAP at the PDBe KB Portal Biology Retrieved from https en wikipedia org w index php title Fibroblast activation protein alpha amp oldid 1172322510, wikipedia, wiki, book, books, library,
