This record provides bibliographic details and links to the original research. An editorial study breakdown is not available.
What the researchers found
ACE2 efficiently cleaves pyr-apelin 13 and apelin 17 peptides, reducing their vasodilatory and cardioprotective effects. ACE2 knockout or inhibition enhances apelin peptide activity, while ACE2-generated cleavage products lack these beneficial functions. Stable apelin analogues resistant to ACE2 degradation retain biological activity.
Why it matters
Understanding how ACE2 degrades apelin peptides helps explain their short lifespan and guides the design of more stable apelin-based drugs for cardiovascular diseases.
How the study worked
The study combined computer modeling, experiments in ACE2 knockout mice, pharmacological ACE2 inhibition, biochemical assays with recombinant ACE2, and functional tests on endothelial cells and myocardial ischemia-reperfusion models. Synthetic apelin analogues resistant to ACE2 cleavage were also designed and tested.
What this study cannot tell us
The study does not specify clinical trial data or long-term effects of stable apelin analogues in humans, and the exact therapeutic potential remains to be confirmed.
Read the original research
Angiotensin-Converting Enzyme 2 Metabolizes and Partially Inactivates Pyr-Apelin-13 and Apelin-17: Physiological Effects in the Cardiovascular System.
Hypertension (Dallas, Tex. : 1979), 68(2), 365-77
Citation
Wang, Wang; McKinnie, Shaun M K; Farhan, Maikel; Paul, Manish; McDonald, Tyler; McLean, Brent; Llorens-Cortes, Catherine; Hazra, Saugata; Murray, Allan G; Vederas, John C; Oudit, Gavin Y. (2016). Angiotensin-Converting Enzyme 2 Metabolizes and Partially Inactivates Pyr-Apelin-13 and Apelin-17: Physiological Effects in the Cardiovascular System.. Hypertension (Dallas, Tex. : 1979), 68(2), 365-77. https://doi.org/10.1161/HYPERTENSIONAHA.115.06892