ABSTRACT
INTRODUCTION Renin, an a partyl protease, is primarily ynthe ized, tored, proce ed, and released from the granules of juxtaglomerular (JG) cell of the kidney in re pon e to everal physiological timuli , including lowered blood pre ure in the glomerular arteriole, odium depletion, and
direct stimulation by the renal ympathetic nerve . Once relea ed into the y temic circulation, renin specifically cleave 10 amino acids from angioten inogen, it only known ubstrate, to form the decapeptide, angiotensin I (Ang 1), which i further proce ed to angiotensin ll (Ang ll) by angiotensin-converting enzyme (ACE). Ang ll is the biologically active peptide of the renin-angiotensin y tern (RAS) and mediate its effect through the binding and activation of AT 1 or AT 2 receptor located throughout the cardiova cular y - tern. Ang IT-mediated activation of angioten in receptor re ults in a wide array of phy iological effect , mo t notably, va ocon triction, aldo terone release, enhancement of renal odium tran port, and timulation of thir t. Moreover, Ang ll ha al o been propo ed to
play an important role in growth of variou vascular mooth mu cle cell type and may be a primary regulator of growth and development of cardiovascular and renal ti ue .
