ArticlePeptides2016
Identification of dipeptidyl peptidase 3 as the Angiotensin-(1-7) degrading peptidase in human HK-2 renal epithelial cells.
Article in Peptides, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 40 citations in OpenAlex.
- Bidirectional crosstalk between the catalytic and moonlighting functions of human dipeptidyl peptidase 3: potential physiological implications.RSC advances · 2026Article
- ACE2-like Catalytic Activity in Anti-SARS-CoV-2 Spike Protein Monoclonal Antibodies.Pathogens (Basel, Switzerland) · 2026Article
- Profiling of Both Dipeptidyl Peptidase III and Renin Reveals Higher Mortality in Septic Shock.Research square · 2026Article
- Novel aspects of the renin-angiotensin-aldosterone system in septic shock.Current opinion in physiology · 2026Article
- One Enzyme, Many Faces: The Expanding Role of DPP3 in Cardiovascular and Critical Care.Journal of clinical medicine · 2025Review
- Targeting high circulating dipeptidyl peptidase 3 in circulatory failure.Critical care (London, England) · 2025Review
- Shock prediction with dipeptidyl peptidase-3 and renin (SPiDeR) in hypoxemic patients with COVID-19.Journal of critical care · 2025Article
- Renin in critically ill patients.Annals of intensive care · 2024Review
- The alternative renin-angiotensin system in critically ill patients: pathophysiology and therapeutic implications.Critical care (London, England) · 2023Review
- Identification of an Additional Metal-Binding Site in Human Dipeptidyl Peptidase III.International journal of molecular sciences · 2023Article
- Influence of Mutations of Conserved Arginines on Neuropeptide Binding in the DPP III Active Site.Molecules (Basel, Switzerland) · 2023Article
- Survey of Dipeptidyl Peptidase III Inhibitors: From Small Molecules of Microbial or Synthetic Origin to Aprotinin.Molecules (Basel, Switzerland) · 2022Review
- Demystifying DPP III Catalyzed Peptide Hydrolysis-Computational Study of the Complete Catalytic Cycle of Human DPP III Catalyzed Tynorphin Hydrolysis.International journal of molecular sciences · 2022Article
- DPP3: From biomarker to therapeutic target of cardiovascular diseases.Frontiers in cardiovascular medicine · 2022Review
- Dipeptidyl peptidase 3, a marker of the antagonist pathway of the renin-angiotensin-aldosterone system in patients with heart failure.European journal of heart failure · 2021Article
- Promotion of vascular integrity in sepsis through modulation of bioactive adrenomedullin and dipeptidyl peptidase 3.Journal of internal medicine · 2021Review
- Dipeptidyl peptidase 3 modulates the renin-angiotensin system in mice.The Journal of biological chemistry · 2020Article
- Involvement of ACE2/Ang-(1-7)/MAS1 Axis in the Regulation of Ovarian Function in Mammals.International journal of molecular sciences · 2020Review
- Absence of Dipeptidyl Peptidase 3 Increases Oxidative Stress and Causes Bone Loss.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2019Article
- Central ANG-(1-7) infusion improves blood pressure regulation in antenatal betamethasone-exposed sheep and reveals sex-dependent effects on oxidative stress.American journal of physiology. Heart and circulatory physiology · 2019Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Angiotensin-(1-7) (Ang-(1-7)) is expressed within the kidney and exhibits renoprotective actions that antagonize the inflammatory, fibrotic and pro-oxidant effects of the Ang II-AT1 receptor axis. We previously identified a peptidase activity from sheep brain, proximal tubules and human HK-2 proximal tubule cells that metabolized Ang-(1-7); thus, the present study isolated and identified the Ang-(1-7) peptidase. Utilizing ion exchange and hydrophobic interaction chromatography, a single 80kDa protein band on SDS-PAGE was purified from HK-2 cells. The 80kDa band was excised, the tryptic digest peptides analyzed by LC-MS and a protein was identified as the enzyme dipeptidyl peptidase 3 (DPP 3, EC: 3.4.14.4). A human DPP 3 antibody identified a single 80kDa band in the purified enzyme preparation identical to recombinant human DPP 3. Both the purified Ang-(1-7) peptidase and DPP 3 exhibited an identical hydrolysis profile of Ang-(1-7) and both activities were abolished by the metallopeptidase inhibitor JMV-390. DPP 3 sequentially hydrolyzed Ang-(1-7) to Ang-(3-7) and rapidly converted Ang-(3-7) to Ang-(5-7). Kinetic analysis revealed that Ang-(3-7) was hydrolyzed at a greater rate than Ang-(1-7) [17.9 vs. 5.5 nmol/min/μg protein], and the Km for Ang-(3-7) was lower than Ang-(1-7) [3 vs. 12μM]. Finally, chronic treatment of the HK-2 cells with 20nM JMV-390 reduced intracellular DPP 3 activity and tended to augment the cellular levels of Ang-(1-7). We conclude that DPP 3 may influence the cellular expression of Ang-(1-7) and potentially reflect a therapeutic target to augment the actions of the peptide.
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Registered trials
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