ArticleClinical & experimental metastasis2011
Fibroblast activation protein-α promotes tumor growth and invasion of breast cancer cells through non-enzymatic functions.
Article in Clinical & experimental metastasis, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 110 citations in OpenAlex.
- From bench to bedside, blade, and back: FAP expression in juvenile angiofibroma. Potential implications for FAPI-PET/CT imaging and targeted therapy?European journal of nuclear medicine and molecular imaging · 2026Article
- Protein-based Radiopharmaceuticals that target fibroblast activation protein alpha: a review of current progress.EJNMMI radiopharmacy and chemistry · 2025Review
- Transcriptomic, mutational and structural bioinformatics approaches to explore the therapeutic role of FAP in predominant cancer types.Discover oncology · 2024Article
- DropBlot: single-cell western blotting of chemically fixed cancer cells.Nature communications · 2024Article
- From basic research to clinical application: targeting fibroblast activation protein for cancer diagnosis and treatment.Cellular oncology (Dordrecht, Netherlands) · 2024Review
- DPP Inhibition Enhances the Efficacy of PD-1 Blockade by Remodeling the Tumor Microenvironment in Lewis Lung Carcinoma Model.Biomolecules · 2024Article
- Therapeutic potential of [European journal of nuclear medicine and molecular imaging · 2024Article
- The Application of Nanoparticles Targeting Cancer-Associated Fibroblasts.International journal of nanomedicine · 2024Review
- Fibroblast activation protein (FAP) as a prognostic biomarker in multiple tumors and its therapeutic potential in head and neck squamous cell carcinoma.Oncology research · 2024Article
- Fibroblast activation protein: Pivoting cancer/chemotherapeutic insight towards heart failure.Biochemical pharmacology · 2024Review
- Fibroblast Activation Protein Alpha (FAPα) in Fibrosis: Beyond a Perspective Marker for Activated Stromal Cells?Biomolecules · 2023Review
- Fibroblast activation protein drives tumor metastasis via a protease-independent role in invadopodia stabilization.Cell reports · 2023Article
- Translational assessment of a DATA-functionalized FAP inhibitor with facileEuropean journal of nuclear medicine and molecular imaging · 2023Article
- Head-to-Head Comparison of FDG and Radiolabeled FAPI PET: A Systematic Review of the Literature.Life (Basel, Switzerland) · 2023Review
- Spheroids of FAP-Positive Cell Lines as a Model for Screening Drugs That Affect FAP Expression.Biomedicines · 2023Article
- FAP is critical for ovarian cancer cell survival by sustaining NF-κB activation through recruitment of PRKDC in lipid rafts.Cancer gene therapy · 2023Article
- Head-to-Head Comparison between [Pharmaceuticals (Basel, Switzerland) · 2023Article
- Novel Generation of FAP Inhibitor-Based Homodimers for Improved Application in Radiotheranostics.Cancers · 2023Article
- Review
- Functional roles of FAP-α in metabolism, migration and invasion of human cancer cells.Frontiers in oncology · 2023Article
1 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Fibroblast activation protein-α (FAP) is a cell surface, serine protease of the post-prolyl peptidase family that is expressed in human breast cancer but not in normal tissues. Previously, we showed that FAP expression increased tumor growth rates in a mouse model of human breast cancer. Here the role of the proteolytic activities of FAP in promoting tumor growth, matrix degradation and invasion was investigated. Mammary fat pads of female SCID mice were inoculated with breast cancer cells that express FAP and the mice treated with normal saline or Val-boroPro (talabostat); Glu-boroPro (PT-630); or 1-[[(3-hydroxy-1-adamantyl)amino]acetyl]-2-cyano-(S)-pyrrolidine (LAF-237) that inhibit prolyl peptidases. Other mice were injected with breast cancer cells expressing a catalytically inactive mutant of FAP and did not receive inhibitor treatment. PT-630 and LAF-237 did not slow growth of tumors produced by any of the three cell lines expressing FAP. Talabostat slightly decreased the growth rates of the FAP-expressing tumors but because PT-630 and LAF-237 did not, the growth retardation was likely not related to the inhibition of FAP or the related post-prolyl peptidase dipeptidyl peptidase IV. Breast cancer cells expressing a catalytically inactive mutant of FAP (FAP(S624A)) also produced tumors that grew rapidly. In vitro studies revealed that cells expressing wild type FAP or FAP(S624A) degrade extracellular matrix (ECM) more extensively, accumulate higher levels of matrix metalloproteinase-9 (MMP-9) in conditioned medium, are more invasive in type I collagen gels, and have altered signaling compared to control transfectants that do not express FAP and form slow growing tumors. We conclude that the proteolytic activity of FAP participates in matrix degradation, but other functions of the protein stimulate increased tumor growth.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.