angiotensinase

Angiotensinase refers to a group of enzymes that catalyze the degradation of angiotensin peptides, specifically angiotensin I and angiotensin II, which are key components of the renin-angiotensin-aldosterone system (RAAS). This system plays a critical role in regulating blood pressure, fluid balance, and electrolyte homeostasis. Angiotensinase activity helps modulate the effects of angiotensin by breaking down these peptides into inactive fragments, thereby counteracting their vasoconstrictive and hypertensive actions.

The primary angiotensinases include neutral endopeptidase (NEP, also known as CD10), aminopeptidase A (APA), and angiotensin-converting enzyme (ACE). Neutral endopeptidase cleaves angiotensin II at the Phe³-His⁴ bond, while aminopeptidase A removes the N-terminal aspartate residue from angiotensin II, rendering it inactive. ACE, traditionally known for converting angiotensin I to angiotensin II, can also degrade angiotensin II under certain conditions.

Elevated angiotensinase activity may contribute to reduced blood pressure, whereas diminished activity has been associated with hypertension and cardiovascular diseases. Research into angiotensinase has explored its potential therapeutic implications, particularly in treating conditions like hypertension, heart failure, and diabetic nephropathy. Some studies suggest that enhancing angiotensinase activity could offer an alternative or complementary approach to existing RAAS-targeting therapies, such as ACE inhibitors or angiotensin receptor blockers (ARBs).

Despite its physiological significance, angiotensinase remains less studied compared to other RAAS components. Further investigation into its regulation, specific isoforms, and potential as a drug target could provide new insights for cardiovascular medicine.