arginaase

Angiotensinase, also known as angiotensin-converting enzyme (ACE), is a zinc-dependent metallopeptidase enzyme that plays a crucial role in the renin-angiotensin system, a key component of the body's cardiovascular and renal systems. ACE is primarily found in the lungs, where it is responsible for converting angiotensin I, a decapeptide, into angiotensin II, an octapeptide. Angiotensin II is a potent vasoconstrictor and stimulates the release of aldosterone, which in turn promotes sodium and water retention, thereby increasing blood pressure and volume.

ACE inhibitors are a class of medications commonly used to treat hypertension, heart failure, and diabetic nephropathy. These drugs work by inhibiting the activity of ACE, thereby reducing the production of angiotensin II and its associated effects. By blocking the conversion of angiotensin I to angiotensin II, ACE inhibitors help to lower blood pressure and improve cardiovascular function.

The gene encoding ACE is located on chromosome 17q23.1, and variations in this gene have been associated with an increased risk of hypertension and cardiovascular disease. ACE is also involved in the degradation of bradykinin, a vasodilator peptide, which further underscores its importance in the regulation of blood pressure and vascular tone.

In summary, angiotensinase, or ACE, is a vital enzyme in the renin-angiotensin system that influences blood pressure and cardiovascular health. Its inhibition through ACE inhibitors is a common therapeutic approach for managing hypertension and related conditions.