Understanding fibroblast activation protein (FAP): Substrates, activities, expression and targeting for cancer therapy
Fibroblast activation protein (FAP) is best known for its heightened expression in tumour stroma. This atypical serine protease has both dipeptidyl peptidase and endopeptidase activities, cleaving substrates at a post‐proline bond. FAP expression is difficult to detect in non‐diseased adult organs,...
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| Published in | Proteomics. Clinical applications Vol. 8; no. 5-6; pp. 454 - 463 |
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| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Germany
Blackwell Publishing Ltd
01.06.2014
Wiley Subscription Services, Inc |
| Subjects | |
| Online Access | Get full text |
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| Abstract | Fibroblast activation protein (FAP) is best known for its heightened expression in tumour stroma. This atypical serine protease has both dipeptidyl peptidase and endopeptidase activities, cleaving substrates at a post‐proline bond. FAP expression is difficult to detect in non‐diseased adult organs, but is greatly upregulated in sites of tissue remodelling, which include liver fibrosis, lung fibrosis, atherosclerosis, arthritis, tumours and embryonic tissues. Due to its restricted expression pattern and dual enzymatic activities, FAP is emerging as a unique therapeutic target. However, methods to exploit and target this protease are advancing more rapidly than knowledge of the fundamental biology of FAP. This review highlights this imbalance, emphasising the need to better define the substrate repertoire and expression patterns of FAP to elucidate its role in biological and pathological processes. |
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| AbstractList | Fibroblast activation protein (FAP) is best known for its heightened expression in tumour stroma. This atypical serine protease has both dipeptidyl peptidase and endopeptidase activities, cleaving substrates at a post‐proline bond. FAP expression is difficult to detect in non‐diseased adult organs, but is greatly upregulated in sites of tissue remodelling, which include liver fibrosis, lung fibrosis, atherosclerosis, arthritis, tumours and embryonic tissues. Due to its restricted expression pattern and dual enzymatic activities, FAP is emerging as a unique therapeutic target. However, methods to exploit and target this protease are advancing more rapidly than knowledge of the fundamental biology of FAP. This review highlights this imbalance, emphasising the need to better define the substrate repertoire and expression patterns of FAP to elucidate its role in biological and pathological processes. Fibroblast activation protein (FAP) is best known for its heightened expression in tumour stroma. This atypical serine protease has both dipeptidyl peptidase and endopeptidase activities, cleaving substrates at a post-proline bond. FAP expression is difficult to detect in non-diseased adult organs, but is greatly upregulated in sites of tissue remodelling, which include liver fibrosis, lung fibrosis, atherosclerosis, arthritis, tumours and embryonic tissues. Due to its restricted expression pattern and dual enzymatic activities, FAP is emerging as a unique therapeutic target. However, methods to exploit and target this protease are advancing more rapidly than knowledge of the fundamental biology of FAP. This review highlights this imbalance, emphasising the need to better define the substrate repertoire and expression patterns of FAP to elucidate its role in biological and pathological processes. [PUBLICATION ABSTRACT] Fibroblast activation protein (FAP) is best known for its heightened expression in tumour stroma. This atypical serine protease has both dipeptidyl peptidase and endopeptidase activities, cleaving substrates at a post-proline bond. FAP expression is difficult to detect in non-diseased adult organs, but is greatly upregulated in sites of tissue remodelling, which include liver fibrosis, lung fibrosis, atherosclerosis, arthritis, tumours and embryonic tissues. Due to its restricted expression pattern and dual enzymatic activities, FAP is emerging as a unique therapeutic target. However, methods to exploit and target this protease are advancing more rapidly than knowledge of the fundamental biology of FAP. This review highlights this imbalance, emphasising the need to better define the substrate repertoire and expression patterns of FAP to elucidate its role in biological and pathological processes.Fibroblast activation protein (FAP) is best known for its heightened expression in tumour stroma. This atypical serine protease has both dipeptidyl peptidase and endopeptidase activities, cleaving substrates at a post-proline bond. FAP expression is difficult to detect in non-diseased adult organs, but is greatly upregulated in sites of tissue remodelling, which include liver fibrosis, lung fibrosis, atherosclerosis, arthritis, tumours and embryonic tissues. Due to its restricted expression pattern and dual enzymatic activities, FAP is emerging as a unique therapeutic target. However, methods to exploit and target this protease are advancing more rapidly than knowledge of the fundamental biology of FAP. This review highlights this imbalance, emphasising the need to better define the substrate repertoire and expression patterns of FAP to elucidate its role in biological and pathological processes. |
| Author | Hamson, Elizabeth J. Gorrell, Mark D. Keane, Fiona M. Schilling, Oliver Tholen, Stefan |
| Author_xml | – sequence: 1 givenname: Elizabeth J. surname: Hamson fullname: Hamson, Elizabeth J. organization: Molecular Hepatology, Centenary Institute and Sydney Medical School, University of Sydney, Sydney, Australia – sequence: 2 givenname: Fiona M. surname: Keane fullname: Keane, Fiona M. organization: Molecular Hepatology, Centenary Institute and Sydney Medical School, University of Sydney, Sydney, Australia – sequence: 3 givenname: Stefan surname: Tholen fullname: Tholen, Stefan organization: Institute of Molecular Medicine and Cell Research, University of Freiburg, Freiburg, Germany – sequence: 4 givenname: Oliver surname: Schilling fullname: Schilling, Oliver organization: Faculty of Biology, University of Freiburg, Freiburg, Germany – sequence: 5 givenname: Mark D. surname: Gorrell fullname: Gorrell, Mark D. email: m.gorrell@centenary.usyd.edu.au organization: Molecular Hepatology, Centenary Institute and Sydney Medical School, University of Sydney, Sydney, Australia |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/24470260$$D View this record in MEDLINE/PubMed |
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| Snippet | Fibroblast activation protein (FAP) is best known for its heightened expression in tumour stroma. This atypical serine protease has both dipeptidyl peptidase... |
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| SubjectTerms | Animals Biomarkers, Tumor - metabolism Collagen Degradomics Dipeptidyl peptidase Endopeptidase Exosite Gelatinases - metabolism Gene Expression Regulation, Neoplastic Humans Membrane Proteins - metabolism Molecular Targeted Therapy - methods Neoplasms - drug therapy Neoplasms - genetics Neoplasms - metabolism Protease Proteomics Serine Endopeptidases - metabolism |
| Title | Understanding fibroblast activation protein (FAP): Substrates, activities, expression and targeting for cancer therapy |
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