Renin

Literature References: Highly specific aspartyl proteinase of mol wt about 40000 Da, produced and secreted by the kidney. Found also in amniotic fluid. Conc. of renin in the human kidney is about 20 times less than in hog kidney. Purification from hog kidneys: Haas et al., Arch. Biochem. Biophys. 42, 368 (1953); from kidneys of various species: Haas et al., ibid. 48, 256 (1954). Prepn of human renin: Haas et al., ibid. 110, 534 (1965). Exists in a, b and g configurations: Haas et al., ibid. 44, 79 (1953). Purification on DEAE cellulose columns: Passananti, Biochim. Biophys. Acta 34, 246 (1959); Maier, Morgan, ibid. 128, 193 (1966). Has been observed to exist in high molecular weight inactive forms which upon acid treatment decrease in molecular size and increase in enzymic activity. See review of purification studies: E. Haber, E. E. Slater, Circ. Res. 40, Suppl. I, I36 (1977). Renin is secreted by juxtaglomerular cells and acts on the plasma substrate, angiotensinogen, to split off the inactive decapeptide angiotensin I which is converted to the active pressor agent angiotensin II, q.v. Renin itself has no activity. Secretion of renin is stimulated by constriction of a renal artery, blood loss, low sodium levels, adrenal insufficiency. Increased levels of renin shown also in pregnancy. Cloning and sequence analysis of human renin cDNA: T. Imai et al., Proc. Natl. Acad. Sci. USA 80, 7405 (1983). Crystal structure of human recombinant renin: A. R. Sielecki et al., Science 243, 1346 (1989). Review: W. S. Peart, "The Renin-Angiotensin System" in Pharmacol. Rev. 17, 143 (1965); idem, Proc. Roy. Soc. Ser. B 173, 317 (1969); Smeby, Bumpus, "Renin" in Renal Hypertension, I. Page, J. McCubbin, Eds. (Year Book Medical Publishers, Chicago, 1968) pp 14-61. Books: M. R. Lee, Renin and Hypertension (Williams & Wilkins, Baltimore, 1969); Renin vol. 5, S. Oparil et al., Eds. (Eden Press, Quebec, 1980) 368 pp. Review of the renin-angiotensin system: J. C. Romero, F. G. Knox, Hypertension 11, 724-738 (1988).