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February 1, 1999Journal of Biological ChemistryOpen Access

Hydrolysis of Peptide Hormones by Endothelin-converting Enzyme-1

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Population

Recombinant endothelin-converting enzyme-1 (ECE-1) and a collection of biologically active peptides

Comparison

In vitro enzymatic hydrolysis vs Neprilysin (comparison of substrate specificity)

Design

Preclinical

Authors

GJGary D. JohnsonSouthern Methodist UniversityTSTracy I. StevensonScripps Research InstituteKAKyunghye AhnPfizer (United States)

Discussion

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Implication

May extend ECE-1's role to neprilysin substrates in peptide metabolism; leaves open relevance to inhibitor effects in cardiovascular models.

Structured PICO

P
Population
Recombinant endothelin-converting enzyme-1 (ECE-1) and a collection of biologically active peptides
I
Intervention
In vitro enzymatic hydrolysis
C
Comparator
Neprilysin (comparison of substrate specificity)
O
Outcome
Enzymatic activity and substrate specificity (hydrolysis of peptides)surrogate

ECE-1 possesses a broad substrate specificity similar to neprilysin and may be involved in the metabolism of biologically active peptides beyond endothelins.

Cite This Study

Johnson et al. (1999) studied this question.

synapsesocial.com/papers/6a7757c8a0847c3df1ec70c2https://doi.org/10.1074/jbc.274.7.4053
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Novel activity of endothelin-converting enzyme: hydrolysis of bradykinin1997 · 108 citations
  2. 2Human endothelin-converting enzyme (ECE-1): three isoforms with distinct subcellular localizations1997 · 206 citations
  3. 3Localization of rat endothelin-converting enzyme to vascular endothelial cells and some secretory cells1995 · 115 citations
  4. 4The metabolism of neuropeptides. The hydrolysis of peptides, including enkephalins, tachykinins and their analogues, by endopeptidase-24.111984 · 375 citations
  5. 5The endothelin-converting enzyme from human umbilical vein is a membrane-bound metalloprotease similar to that from bovine aortic endothelial cells.1992 · 50 citations