Abstract
Renin is an enzyme elaborated in juxta glomerular cells of the kidney and released into the blood stream by various stimuli. Although it is an endopeptidase, its function is strictly limited to the formation of angiotensin I from angiotensinogen by the cleavage of a unique leucyl-leucine peptide bond in this substrate molecule (Fig.l). Angiotensin I is converted into the octapeptide angiotensin II by a carboxydipeptidase, known as converting enzyme, and thenceforth to the heptapeptide angiotensin III by an aminopeptidase. Not only is angiotensin II the most potent pressor substance known, but both angiotensin II and III also stimulate the adrenal cortex to release the mineral corticoid aldosterone. Thus, renin triggers a chain of events aimed at elevating the blood pressure. Because of its strategically important position in the renin-angiosin-aldosterone system, the activity of renin in the circulation is tightly regulated by intricate multiple feedback control mechanisms. Excellent reviews on the control of renin release have been published recently (1–4).
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Inagami, T., Murakami, K., Misono, K., Workman, R.J., Cohen, S., Suketa, Y. (1977). Renin and Precursors: Purification, Characterization, and Studies on Active Site. In: Tang, J. (eds) Acid Proteases: Structure, Function, and Biology. Advances in Experimental Medicine and Biology, vol 95. Springer, New York, NY. https://doi.org/10.1007/978-1-4757-0719-9_14
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DOI: https://doi.org/10.1007/978-1-4757-0719-9_14
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