The ACE2/Ang (1–7)/MasR axis as an emerging target for antihypertensive peptides

Abstract

Food protein-derived bioactive peptides, particularly antihypertensive peptides, are important constituents of functional foods or nutraceuticals. Most antihypertensive are identified as the inhibitors of angiotensin converting enzyme (ACE), a key enzyme responsible for the generation of angiotensin II (Ang II), which is a vasoconstricting peptide. Hence, ACE has long been used as a universal target to identify antihypertensive peptides. Angiotensin converting enzyme 2 (ACE2), is a homolog of ACE but uses Ang II as its key substrate to produce angiotensin (1–7), exerting vasodilatory activity via the mas receptor (MasR). Therefore, ACE2 functions in the opposite way as ACE and is an emerging novel target for cardiovascular therapy. The potential of food protein-derived bioactive peptides in targeting ACE2 has been rarely explored. While, recently we found that IRW, an egg white ovotransferrin-derived antihypertensive peptide, reduced blood pressure in spontaneously hypertensive rats via the ACE2/Ang (1–7)/MasR axis, indicating a new mechanism of food protein-derived bioactive peptides in reducing blood pressure. The objectives of this review are to summarize the functions of the ACE2/Ang (1–7)/MasR axis and to examine its potential roles in the actions of food protein-derived antihypertensive peptides. The interaction between antihypertensive peptides and the ACE2/Ang (1–7)/MasR axis will also be discussed.

Keywords:

• ACE2/Ang (1–7)/MasR axis
• antihypertensive peptides
• food bioactives
• molecular mechanisms

Acknowledgements

The laboratory of Dr. Jianping Wu is supported by Grants from Natural Sciences and Engineering Research Council (NSERC) of Canada and Alberta Agriculture and Forestry.

Disclosure statement

The authors declare there is no conflict of interest.