Angiotensin converting enzyme (ACE) is a peptidyl dipeptidase enzyme that plays a crucial role in the renin-angiotensin-aldosterone system (RAAS) and is a significant component of cardiovascular and kidney physiology. It is primarily located on the surface of endothelial cells of blood vessels, particularly in the lung.
The main function of ACE is to convert angiotensin I into the potent vasoconstrictor angiotensin II. This conversion occurs through the enzymatic cleavage of two amino acids from angiotensin I, resulting in the formation of angiotensin II. Angiotensin II is a potent vasoconstrictor that causes the constriction of blood vessels, leading to elevated blood pressure and increased sodium and water reabsorption in the kidney.
Additionally, ACE is responsible for the degradation of bradykinin, a vasodilator peptide. By degrading bradykinin, ACE indirectly promotes vasoconstriction and contributes to the overall regulation of blood pressure.
Inhibition of ACE is a commonly used therapeutic approach in the management of hypertension and heart failure. ACE inhibitors, a class of drugs, block the activity of ACE, leading to reduced production of angiotensin II and increased levels of bradykinin. This ultimately results in vasodilation, reduced blood pressure, and improved cardiac function.
Furthermore, ACE inhibitors have been found to offer additional cardiovascular benefits, including reducing the risk of heart attack, stroke, and heart failure progression.
