ACE Recombinant Monoclonal Antibody

Function

Angiotensin-converting enzyme (EC 3.4.15.1), or ACE, is a central component of the renin–angiotensin system (RAS), which controls blood pressure by regulating the volume of fluids in the body. It converts the hormone angiotensin I to the active vasoconstrictor angiotensin II. Therefore, ACE indirectly increases blood pressure by causing blood vessels to constrict. ACE inhibitors are widely used as pharmaceutical drugs for treatment of cardiovascular diseases. Other lesser known functions of ACE are degradation of bradykinin, substance P and amyloid beta-protein. ACE hydrolyzes peptides by the removal of a dipeptide from the C-terminus. Likewise it converts the inactive decapeptide angiotensin I to the octapeptide angiotensin II by removing the dipeptide His-Leu. Angiotensin II is a potent vasoconstrictor in a substrate concentration-dependent manner. Angiotensin II binds to the type 1 angiotensin II receptor (AT1), which sets off a number of actions that result in vasoconstriction and therefore increased blood pressure. ACE is also part of the kinin-kallikrein system where it degrades bradykinin, a potent vasodilator, and other vasoactive peptides. Kininase II is the same as angiotensin-converting enzyme. Thus, the same enzyme (ACE) that generates a vasoconstrictor (ANG II) also disposes of vasodilators (bradykinin).

Background References

1. Yang J et al. Pathological Ace2-to-Ace enzyme switch in the stressed heart is transcriptionally controlled by the endothelial Brg1-FoxM1 complex. Proc Natl Acad Sci U S A 113:E5628-35 (2016).

2. Zhou L et al. Multiple Genes of the Renin-Angiotensin System Are Novel Targets of Wnt/ -Catenin Signaling. J Am Soc Nephrol 26(1):107-20 (2015).

Subcellular Location

Secreted. Cell membrane. Cytoplasm.

UNIPROT

SwissProt: P09470 Mouse

Synonyms