ArticleThe FEBS journal2009
Characterization of a monoclonal antibody as the first specific inhibitor of human NTP diphosphohydrolase-3 : partial characterization of the inhibitory epitope and potential applications.
Article in The FEBS journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 52 citations in OpenAlex.
- Histamine induces ATP release from human subcutaneous fibroblasts, via pannexin-1 hemichannels, leading to Ca2+ mobilization and cell proliferation.The Journal of biological chemistry · 2013Trial
- HIF-1α Stabilization Hampers the Chondrogenic Differentiation of Aged Bone Marrow Mesenchymal Stem Cells by Adenosine AACS pharmacology & translational science · 2025Article
- Endometrial epithelial cell organoids as tools for studying the CD39 family of enzymes and for validating enzyme inhibitors.Histology and histopathology · 2025Article
- CD39 delineates chimeric antigen receptor regulatory T cell subsets with distinct cytotoxic & regulatory functions against human islets.Frontiers in immunology · 2024Article
- Article
- Silencing NTPDase3 activity rehabilitates the osteogenic commitment of post-menopausal stem cell bone progenitors.Stem cell research & therapy · 2023Article
- Human Beta Cell Regenerative Drug Therapy for Diabetes: Past Achievements and Future Challenges.Frontiers in endocrinology · 2021Review
- E-NTPDases: Possible Roles on Host-Parasite Interactions and Therapeutic Opportunities.Frontiers in cellular and infection microbiology · 2021Review
- Lactate activation of α-cell KMolecular metabolism · 2020Article
- A Simple and Efficient Genetic Immunization Protocol for the Production of Highly Specific Polyclonal and Monoclonal Antibodies against the Native Form of Mammalian Proteins.International journal of molecular sciences · 2020Article
- Imatinib mesylate affects extracellular ATP catabolism and expression of NTPDases in a chronic myeloid leukemia cell line.Purinergic signalling · 2020Article
- Development of Anthraquinone Derivatives as Ectonucleoside Triphosphate Diphosphohydrolase (NTPDase) Inhibitors With Selectivity for NTPDase2 and NTPDase3.Frontiers in pharmacology · 2020Article
- Ectonucleoside Triphosphate Diphosphohydrolase-3 Antibody Targets Adult Human Pancreatic β Cells for In Vitro and In Vivo Analysis.Cell metabolism · 2019Article
- Characterization of ecto-nucleotidases in human oviducts with an improved approach simultaneously identifying protein expression and in situ enzyme activity.Histochemistry and cell biology · 2018Article
- Generation and characterization of polyclonal and monoclonal antibodies to human NTPDase2 including a blocking antibody.Purinergic signalling · 2017Article
- Generation and Characterization of Specific Antibodies to the Murine and Human Ectonucleotidase NTPDase8.Frontiers in pharmacology · 2017Article
- Purinergic signalling in endocrine organs.Purinergic signalling · 2014Review
- Purine-metabolizing ectoenzymes control IL-8 production in human colon HT-29 cells.Mediators of inflammation · 2014Article
- 8-BuS-ATP derivatives as specific NTPDase1 inhibitors.British journal of pharmacology · 2013Article
- Epitope mapping in cell surface proteins by site-directed masking: defining the structural elements of NTPDase3 inhibition by a monoclonal antibody.Protein engineering, design & selection : PEDS · 2010Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
The study and therapeutic modulation of purinergic signaling is hindered by a lack of specific inhibitors for NTP diphosphohydrolases (NTPDases),which are the terminating enzymes for these processes. In addition, little is known of the NTPDase protein structural elements that affect enzymatic activity and which could be used as targets for inhibitor design. In the present study, we report the first inhibitory monoclonal antibodies specific for an NTPDase, namely human NTPDase3 (EC 3.6.1.5), as assessed by ELISA, western blotting, flow cytometry, immunohistochemistry and inhibition assays. Antibody recognition of NTPDase3 is greatly attenuated by denaturation with SDS, and abolished by reducing agents, indicating the significance of the native conformation and the disulfide bonds for epitope recognition. Using site-directed chemical cleavage, the SDS-resistant parts of the epitope were located in two fragments of the C-terminal lobe ofNTPDase3 (i.e. Leu220-Cys347 and Cys347-Pro485), which are both required for antibody binding. Additional site-directed mutagenesis revealed the importance of Ser297 and the fifth disulfide bond (Cys399-Cys422) for antibody binding, indicating that the discontinuous inhibitory epitope is located on the extracellular C-terminal lobe of NTPDase3. These antibodies inhibit recombinant NTPDase3 by 60-90%, depending on the conditions. More importantly, they also efficiently inhibit the NTPDase3expressed in insulin secreting human pancreatic islet cells in situ. Because insulin secretion is modulated by extracellular ATP and purinergic receptors, this finding suggests the potential application of these inhibitory antibodies for the study and control of insulin secretion.
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Registered trials
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.