1976
DOI: 10.1210/endo-99-1-93
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Renin Activity in Dog Brain: Enzymological Similarity to Cathepsin D

Abstract: The distribution and biochemical properties of the renin activity present in the dog brain were compared with those of the lysosomal enzyme cathepsin D. Renin and cathepsin activity were present in all brain regions studied, in association with high angiotensinase activity. Brain renin activity was partially purified by ammonium sulfate fractionation and Sephadex gel filtration, resulting in the removal of angiotensinase activity. The specific brain renin activity increased approximately one hundred times duri… Show more

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Cited by 101 publications
(33 citation statements)
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“…One possibility is that the generation of angiotensin I may be catalyzed by some enzyme other than renin. In fact, both cathepsin D and kallikrein have been shown to be able to generate angiotensin II from angiotensinogen (28,29). However, the pH optimum for angiotensin formation by both the lysosomal cathepsins and by kallikrein is in the acid range, around pH 4-5, which is far lower than the neutral pH found to be optimal for the interaction of renin with species-specific angiotensinogen (30).…”
Section: Discussionmentioning
confidence: 99%
“…One possibility is that the generation of angiotensin I may be catalyzed by some enzyme other than renin. In fact, both cathepsin D and kallikrein have been shown to be able to generate angiotensin II from angiotensinogen (28,29). However, the pH optimum for angiotensin formation by both the lysosomal cathepsins and by kallikrein is in the acid range, around pH 4-5, which is far lower than the neutral pH found to be optimal for the interaction of renin with species-specific angiotensinogen (30).…”
Section: Discussionmentioning
confidence: 99%
“…Considerable debate exists in the literature concerning the identity of renin-like enzymes (based upon the ability to generate angiotensin I) in extra- (Day and Reid, 1976;Dorer et al, 1978;Ganten et al, 1976;Hackenthal et al, 1978;Skeggs et al, 1969). Pseudorenin and isorenin (Skeggs et al, 1969), an angiotensin-forming enzyme with an acidic pH optimum, are widely distributed in mammalian tissues.…”
Section: Discussionmentioning
confidence: 99%
“…However, the existence of a central angiotensin-forming pathway in vivo is controversial (5). Receivedfor publication 26 March 1985. because brain tissue contains an acid protease similar to cathepsin D, a lysosomal enzyme that cleaves angiotensinogen to produce angiotensin I at acidic pH (6). Recently, independent investigators have shown the existence in brain and in neuroendocrine glands of a protease resembling kidney renin that acts on renin substrate at neutral pH (7,8).…”
Section: Introductionmentioning
confidence: 99%