Angiotensinases

Angiotensinases are a group of enzymes that cleave peptide bonds in angiotensin peptides. Angiotensin peptides are hormones that play a crucial role in regulating blood pressure and fluid balance within the body. These enzymes are primarily responsible for breaking down these vasoactive peptides, thereby controlling their duration of action and preventing excessive vasoconstriction or fluid retention.

There are several known types of angiotensinases, with angiotensinase A and angiotensinase B being among the earliest identified. Angiotensinase A, also known as carboxypeptidase A, is found in the liver and kidney and primarily cleaves the C-terminal amino acid from angiotensin II, rendering it inactive. Angiotensinase B, also known as aminopeptidase B, acts on the N-terminus of angiotensin peptides. Other angiotensinases, such as angiotensinase C and angiotensinase D, have also been described, each with specific cleavage sites and substrate preferences.

The activity of angiotensinases is vital for maintaining cardiovascular homeostasis. By degrading active angiotensin peptides, they act as a counterbalance to the renin-angiotensin-aldosterone system (RAAS), which is responsible for generating angiotensin II. Dysregulation of angiotensinase activity has been implicated in various cardiovascular diseases, including hypertension and heart failure, as it can lead to an accumulation of active angiotensin peptides and subsequent detrimental effects on the cardiovascular system. Research continues to explore the specific roles and therapeutic potential of modulating angiotensinase activity.