Background
Renin is a member of the aspartyl proteinase family produced largely in part by the juxtaglomerular cells in the kidney. Renin is produced as prorenin with 43 pro residues at the N-terminal of mature Renin. The inactive prorenin becomes activated proteolytically by trypsin, cathepsin B, or other proteinases. Renin also has a very high selectivity for substrates due to a long peptide recognition on either side of the peptide bond undergoing cleavage. An octapeptide substrate was the minimum length to be cleaved by Renin. Renin plays a crucial role in the regulation of blood pressure and salt balance through the cleavage of angiotensinogen,which is the only known physiological substrate of Renin. Renin releases the decapeptide angiotensin I, which in turn is further converted to vasoactive hormone angiotensin II by angiotensin converting enzyme (ACE).
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