Renin enzyme (Renin)

Renin is an aspartyl protease enzyme secreted predominantly by the juxtaglomerular cells in the kidney in response to decreased renal perfusion, reduced sodium concentration at the macula densa, or increased sympathetic nervous system activity[1][2][3][5]. Renin’s primary physiological function is the cleavage of angiotensinogen (synthesized by the liver) to produce angiotensin I, the first and rate-limiting step of the renin–angiotensin–aldosterone system (RAAS)[2][3][5][7]. Through this pathway, renin indirectly modulates systemic blood pressure, blood volume, renal sodium retention, and vascular tone[1][2][3]. The active site of renin features two aspartate residues essential for acid-base catalysis of peptide bond cleavage on angiotensinogen[2]. Prorenin is the inactive precursor that can be enzymatically or non-enzymatically activated to mature renin[5]. Excess or dysregulation of renin activity plays a central pathogenic role in hypertension, cardiovascular disease, and certain forms of renal disease[1][3][5][7].

Other names

ProreninAspartyl proteaseAngiotensinogenase

Direct competitive inhibition of active site (by small molecule renin inhibitors such as aliskiren) Blockade of angiotensinogen cleavage and downstream angiotensin I/II production