Quantitation of fibroblast activation protein (FAP)-specific protease activity in mouse, baboon and human fluids and organs☆

@article{Keane2013QuantitationOF,
  title={Quantitation of fibroblast activation protein (FAP)-specific protease activity in mouse, baboon and human fluids and organs☆},
  author={Fiona M. Keane and Tsun-Wen Yao and Stefanie Seelk and Margaret G. Gall and Sumaiya Islam Chowdhury and Sarah E. Poplawski and Jack H. Lai and Youhua Li and Wengen Wu and Penny Farrell and Ana J{\'u}lia Vieira de Ribeiro and Brenna Osborne and Denise M. T. Yu and Devanshi Seth and Khairunnessa Rahman and Paul S Haber and Ali Kemal Topaloğlu and Chuanming Wang and Sally E Thomson and Annemarie Hennessy and Johannes B Prins and Stephen Morris Twigg and Susan V. Mclennan and Geoffrey W McCaughan and William W. Bachovchin and Mark D. Gorrell},
  journal={FEBS Open Bio},
  year={2013},
  volume={4},
  pages={43 - 54}
}
View on Wiley
febs.onlinelibrary.wiley.com
74 Citations
Highly Influential Citations
1
Background Citations
29
Methods Citations
8
Results Citations
2

74 Citations

Citation Type

Citation Type

Selective Homogeneous Assay for Circulating Endopeptidase Fibroblast Activation Protein (FAP)
TLDR
A novel homogeneous fluorescence intensity assay for circulating FAP activity based on a recently identified natural substrate, FGF21, which can effectively distinguish endopeptidase activity of FAP from that of other related enzymes such as prolyl endopepticase (PREP) and was validated using Fap-deficient mice.
Understanding fibroblast activation protein (FAP): Substrates, activities, expression and targeting for cancer therapy
TLDR
The need to better define the substrate repertoire and expression patterns of FAP to elucidate its role in biological and pathological processes is highlighted, emphasising the need for methods to exploit and target this protease more rapidly.
Neuropeptide Y is a physiological substrate of fibroblast activation protein: Enzyme kinetics in blood plasma and expression of Y2R and Y5R in human liver cirrhosis and hepatocellular carcinoma
Novel Small Molecule-Derived, Highly Selective Substrates for Fibroblast Activation Protein (FAP).
TLDR
Sub substrate-type FAP probes that are structurally derived from a FAP-inhibitor (UAMC1110) that equal or surpass the most advanced peptide-based FAP substrates reported to date are presented.
Fibroblast activation protein-α in fibrogenic disorders and cancer: more than a prolyl-specific peptidase?
TLDR
FAP-α is selectively expressed at sites of tissue remodeling and repair and enhances tumor progression, suggesting that this protease may be a therapeutic target to treat human disorders associated with fibrotic dysregulation.
Targeting fibroblast activation protein in cancer - Prospects and caveats.
TLDR
A better understanding of its role in individual tumor types, careful selection of patients, and identification of suitable combinations with currently available anticancer treatments will be critical for a successful translation of preclinically tested approaches of FAP targeting into clinical setting.
In Vitro and In Situ Activity-Based Labeling of Fibroblast Activation Protein with UAMC1110-Derived Probes
TLDR
Three different activity-based probes based on the FAP-inhibitor UAMC1110, an in-house developed molecule considered to be the most potent and selective FAP inhibitor available, are described and demonstrated that the three probes have subnanomolar FAP affinity and pronounced selectivity with respect to the related S9 family members.
Fibroblast activation protein (FAP) as a novel metabolic target
Fibroblast activation protein is dispensable for control of glucose homeostasis and body weight in mice
Fibroblast activation protein in liver fibrosis.
TLDR
Its differential pattern of expression in diseases supports the emerging concept for FAP as a potential disease biomarker as well as a useful therapeutic target for drug intervention.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 85 REFERENCES
Targeted Disruption of Mouse Fibroblast Activation Protein
TLDR
Fap −/− mice are fertile, show no overt developmental defects, and have no general change in cancer susceptibility, to explore the role of FAP in vivo.
Expression of the fibroblast activation protein during mouse embryo development.
TLDR
It is reported that Fap-/- lacZ mice express beta-Galactosidase at regions of active tissue remodeling during embryogenesis including somites and perichondrial mesenchyme from cartilage primordia.
Fibroblast activation protein: A cell surface dipeptidyl peptidase and gelatinase expressed by stellate cells at the tissue remodelling interface in human cirrhosis
TLDR
The expression of FAP is delineated in cirrhotic human liver and recombinant FAP was shown to have gelatinase and dipeptidyl peptidase activities and FAP may contribute to the HSC‐induced extracellular matrix (ECM) changes of cirrhosis.
Fibroblast activation protein and chronic liver disease.
TLDR
The FAP homodimer is structurally very similar to DPIV but FAP glycoprotein expression is largely confined to mesenchymal cells in diseased and damaged tissue, notably the tissue remodelling region in chronically injured liver.
Expression and role of the cell surface protease seprase/fibroblast activation protein-α (FAP-α) in astroglial tumors
TLDR
Seprase or fibroblast activation protein-α is highly expressed on the surface of glioma cells and contributes to diffuseglioma invasion through extracellular matrix components.
Targeting inhibition of fibroblast activation protein-α and prolyl oligopeptidase activities on cells common to metastatic tumor microenvironments.
TLDR
Targeting FAP-positive cells, especially mesenchymal stem cells and cancer-associated fibroblasts for inactivation or destruction, and inhibiting POP-producing EC may abrogate stromal invasion and angiogenesis simultaneously and thereby diminish cancer growth.
Targeting the cancer stroma with a fibroblast activation protein-activated promelittin protoxin
TLDR
Intratumoral injection of an FAP-activated protoxin produced significant lysis and growth inhibition of human breast and prostate cancer xenografts with minimal toxicity to the host animal.
Antiplasmin-cleaving enzyme is a soluble form of fibroblast activation protein.
TLDR
Data support APCE as a soluble derivative of FAP and Met-alpha2AP as its physiologic substrate, which may increase plasmin inhibition within fibrin surrounding certain neoplasms and have an impact on growth and therapeutic susceptibility.
Fibroblast Activation Protein, a Dual Specificity Serine Protease Expressed in Reactive Human Tumor Stromal Fibroblasts*
TLDR
It is demonstrated that FAP is present as an active cell surface-bound collagenase in epithelial tumor stroma and opens up investigation into physiological substrates of its novel, tumor-associated dipeptidyl peptidase activity.
Fibroblast activation protein increases apoptosis, cell adhesion, and migration by the LX‐2 human stellate cell line
TLDR
Findings further support a pro‐fibrogenic role for FAP by indicating that FAP has important nonenzymatic functions that in chronic liver injury may facilitate tissue remodeling through FAP‐mediated enhancement of HSC cell adhesion, migration, and apoptosis.
...
1
2
3
4
5
...