ArticleAnalytical chemistry2019
The Plethora of Angiotensin-Converting Enzyme-Processed Peptides in Mouse Plasma.
Article in Analytical chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Alzheimer's disease-linked ACE variants increase ACE1 catalytic activity and production of angiotensin II.The Journal of biological chemistry · 2026Article
- Dimerization and dynamics of human angiotensin-I converting enzyme revealed by cryo-EM and MD simulations.eLife · 2025Article
- Neuronal ACE1 knockout disrupts the hippocampal renin angiotensin system leading to memory impairment and vascular loss in normal aging.Neurobiology of disease · 2024Article
- Proteomic Analysis of Human Macrophages Overexpressing Angiotensin-Converting Enzyme.International journal of molecular sciences · 2024Article
- ACE inhibitors fromIn silico pharmacology · 2024Article
- Structural basis for the inhibition of human angiotensin-1 converting enzyme by fosinoprilat.The FEBS journal · 2022Article
- Captopril alleviates epilepsy and cognitive impairment by attenuation of C3-mediated inflammation and synaptic phagocytosis.Journal of neuroinflammation · 2022Article
- The non-cardiovascular actions of ACE.Peptides · 2022Article
- Exploring the Impact of ACE Inhibition in Immunity and Disease.Journal of the renin-angiotensin-aldosterone system : JRAAS · 2022Review
- Epitope mapping of novel monoclonal antibodies to human angiotensin I-converting enzyme.Protein science : a publication of the Protein Society · 2021Article
- Status of mannose-binding lectin (MBL) and complement system in COVID-19 patients and therapeutic applications of antiviral plant MBLs.Molecular and cellular biochemistry · 2021Review
- Angiotensin-converting enzyme open for business: structural insights into the subdomain dynamics.The FEBS journal · 2021Article
- ACE2 and ACE: structure-based insights into mechanism, regulation and receptor recognition by SARS-CoV.Clinical science (London, England : 1979) · 2020Review
- Investigation of angiotensin-I-converting enzyme (ACE) inhibitory tri-peptides: a combination of 3D-QSAR and molecular docking simulations.RSC advances · 2020Article
- Rationale for targeting complement in COVID-19.EMBO molecular medicine · 2020Review
- Renin-angiotensin aldosterone profile before and after angiotensin-converting enzyme-inhibitor administration in dogs with angiotensin-converting enzyme gene polymorphism.Journal of veterinary internal medicine · 2020Article
- ACE overexpression in myeloid cells increases oxidative metabolism and cellular ATP.The Journal of biological chemistry · 2020Article
- Overexpression of ACE in Myeloid Cells Increases Immune Effectiveness and Leads to a New Way of Considering Inflammation in Acute and Chronic Diseases.Current hypertension reports · 2020Review
- Peripherally derived angiotensin converting enzyme-enhanced macrophages alleviate Alzheimer-related disease.Brain : a journal of neurology · 2020Article
- Overexpression of myeloid angiotensin-converting enzyme (ACE) reduces atherosclerosis.Biochemical and biophysical research communications · 2019Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Angiotensin-converting enzyme (ACE) converts angiotensin I into the potent vasoconstrictor angiotensin II, which regulates blood pressure. However, ACE activity is also essential for other physiological functions, presumably through processing of peptides unrelated to angiotensin. The goal of this study was to identify novel natural substrates and products of ACE through a series of mass-spectrometric experiments. This included comparing the ACE-treated and untreated plasma peptidomes of ACE-knockout (KO) mice, validation with select synthetic peptides, and a quantitative in vivo study of ACE substrates in mice with distinct genetic ACE backgrounds. In total, 244 natural peptides were identified ex vivo as possible substrates or products of ACE, demonstrating high promiscuity of the enzyme. ACE prefers to cleave substrates with Phe or Leu at the C-terminal P2' position and Gly in the P6 position. Pro in P1' and Iso in P1 are typical residues in peptides that ACE does not cleave. Several of the novel ACE substrates are known to have biological activities, including a fragment of complement C3, the spasmogenic C3f, which was processed by ACE ex vivo and in vitro. Analyses with N-domain-inactive (NKO) ACE allowed clarification of domain selectivity toward substrates. The in vivo ACE-substrate concentrations in WT, transgenic ACE-KO, NKO, and CKO mice correspond well with the in vitro observations in that higher levels of the ACE substrates were observed when the processing domain was knocked out. This study highlights the vast extent of ACE promiscuity and provides a valuable platform for further investigations of ACE functionality.
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