ArticleThe Biochemical journal1997
Novel activity of endothelin-converting enzyme: hydrolysis of bradykinin.
Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- The role of the kallikrein-kinin system genes in the salt sensitivity of blood pressure: the GenSalt Study.American journal of epidemiology · 2012Trial
- Review
- Novel Therapeutic Approaches Targeting the Renin-Angiotensin System and Associated Peptides in Hypertension and Heart Failure.Pharmacological reviews · 2019Review
- Neprilysin Inhibitors and Bradykinin.Frontiers in medicine · 2018Review
- Pharmacological hypothesis: Nitric oxide-induced inhibition of ADAM-17 activity as well as vesicle release can in turn prevent the production of soluble endothelin-converting enzyme.Pharmacology research & perspectives · 2017Review
- Amyloid-clearing proteins and their epigenetic regulation as a therapeutic target in Alzheimer's disease.Frontiers in aging neuroscience · 2014Review
- Endothelin-converting enzymes and related metalloproteases in Alzheimer's disease.Journal of Alzheimer's disease : JAD · 2013Review
- Dynamic changes in the secondary structure of ECE-1 and XCE account for their different substrate specificities.BMC bioinformatics · 2012Article
- Endothelin-converting enzyme-2 is increased in Alzheimer's disease and up-regulated by Abeta.The American journal of pathology · 2009Article
- The kallikrein-kinin system in health and in diseases of the kidney.Kidney international · 2009Review
- Endothelin-converting enzyme 1 promotes re-sensitization of neurokinin 1 receptor-dependent neurogenic inflammation.British journal of pharmacology · 2009Article
- Effects of 4-hydroxy-nonenal and Amyloid-beta on expression and activity of endothelin converting enzyme and insulin degrading enzyme in SH-SY5Y cells.Journal of Alzheimer's disease : JAD · 2009Article
- Molecular bases for the recognition of short peptide substrates and cysteine-directed modifications of human insulin-degrading enzyme.Biochemistry · 2008Article
- The endothelin system as a therapeutic target in cardiovascular disease: great expectations or bleak house?British journal of pharmacology · 2008Review
- Endothelin-converting enzyme-1 regulates endosomal sorting of calcitonin receptor-like receptor and beta-arrestins.The Journal of cell biology · 2007Article
- Endothelin-converting enzyme 1 degrades neuropeptides in endosomes to control receptor recycling.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- New insights into the roles of metalloproteinases in neurodegeneration and neuroprotection.International review of neurobiology · 2007Review
- Functional roles of cell surface peptidases in reproductive organs.Reproductive medicine and biology · 2004Review
- Stromal-epithelial interactions influence prostate cancer cell invasion by altering the balance of metallopeptidase expression.British journal of cancer · 2004Article
- Computer modeling and nanosecond simulation of the enzyme-substrate complex of the common lymphoblastic leukemia antigen (neprilysin) indicates shared residues at the primary specificity pocket (S1') with matrix metalloproteases.Journal of molecular modeling · 2003Article
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Endothelin-converting enzyme (ECE) is the key enzyme in the production of the potent vasoconstrictor endothelin from its inactive precursor big endothelin. To date, no other physiological peptide substrate has been identified for ECE. Here, by using Chinese hamster ovary (CHO) cells transfected with rat ECE-1 cDNA, we have established that ECE can hydrolyse the vasodilator bradykinin. The hydrolysis of bradykinin by ECE is exclusively at the Pro7-Phe8 bond, producing bradykinin-(1-7) and bradykinin-(8-9). Hydrolysis is completely inhibited by 100 microM phosphoramidon and 200 microM EDTA, but only slightly by the specific neprilysin inhibitor thiorphan (100 microM). The ability of ECE to act as a peptidyl dipeptidase rather than an endopeptidase in hydrolysing bradykinin suggests a much broader specificity for the enzyme than previously recognized, which may lead to the design of new and specific inhibitors of ECE and to the identification of other potential physiological substrates.
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