“…Using purified cathepsin D from procine spleen, they indicated that the two-optima phenomenon is a property of a single enzyme species. 10 The pH optimum curve ( fig. 4) obtained with brain renin-like activity (non-perfused dog brain) showed a broad shoulder or approximately optimum pH in the range of 4-5; moreover a second pH optimum in the range of 6-7 was obtained.…”
SUMMARY A renin-like enzyme and add protease (cathepsin) from whole and saline-perfused dog brains were separated by CM-cellnlose cbromatography with a linear NaCl gradient. Plasma renin and cathepsin were also separated using the same system. During the separation steps (in all the above cases) the specific activity of the brain renin-like enzyme was increased, while the specific activity of the brain cathepsin was decreased. Approximately a 70-fold increase in the specific activity of brain renln-like enzyme and a sixfold decrease in brain cathepsin specific activity was obtained from saline-perfused brain. The separation made it possible to study the pH optimum of the brain renin-like enzyme and acid protease. The brain renin-like enzyme showed optimal activity in the range of pH 6-7. Immunologically, the renin-like enzyme was distinctly different from dog kidney renin.
“…Using purified cathepsin D from procine spleen, they indicated that the two-optima phenomenon is a property of a single enzyme species. 10 The pH optimum curve ( fig. 4) obtained with brain renin-like activity (non-perfused dog brain) showed a broad shoulder or approximately optimum pH in the range of 4-5; moreover a second pH optimum in the range of 6-7 was obtained.…”
SUMMARY A renin-like enzyme and add protease (cathepsin) from whole and saline-perfused dog brains were separated by CM-cellnlose cbromatography with a linear NaCl gradient. Plasma renin and cathepsin were also separated using the same system. During the separation steps (in all the above cases) the specific activity of the brain renin-like enzyme was increased, while the specific activity of the brain cathepsin was decreased. Approximately a 70-fold increase in the specific activity of brain renln-like enzyme and a sixfold decrease in brain cathepsin specific activity was obtained from saline-perfused brain. The separation made it possible to study the pH optimum of the brain renin-like enzyme and acid protease. The brain renin-like enzyme showed optimal activity in the range of pH 6-7. Immunologically, the renin-like enzyme was distinctly different from dog kidney renin.
“…The central effects of angiotensin require normal cerebrospinal fluid (CSF) [Na+] and its activity is enhanced by high CSF [Na+] (2 -4 ). A negative correlation exists between brain water and electrolytes and brain renin activity (16). Water deprivation decreases renin activity in the pituitary of desert rats but increases plasma renin activity (14).…”
Angiotensin, present in the central nervous system and kidneys, affects salt/water balance when administered to either site but the relationship between central and peripheral actions is unclear. One reported difference between central and peripheral administration of the peptide is that the former causes natriuresis whereas the latter conserves sodium. We injected angiotensin II into the lateral cerebroventricles of conscious rats maintained on low, normal and high sodium intakes. Prior to injection, plasma [Na+] and hematocrits were similar in the 3 groups. Angiotensin increased plasma vasopressin content in all groups at 1 and 5 min; the 1-min peak was greater in the high Na+ rats. In control and low Na+ rats plasma renin activity (PRA) was suppressed 5 and 20 min after angiotensin. Basal PRA of high Na+ rats was low and tended to be further suppressed by angiotensin. Angiotensin-induced water intake was similar in all groups. Thus, the response pattern to intraventricular angiotensin (vasopressin release, PRA suppression and drinking behavior) occurred over a range of sodium intakes sufficient to suppress or elevate basal PRA. These responses, and the natriuretic effect of intraventricular angiotensin, would be beneficial under conditions of Na+ excess. Conversely, these effects would be detrimental in Na+-defícient conditions since they reduce the ability to maintain extracellular [Na+]. Angiotensin effects in brain may be increased by sodium excess whereas the renal angiotensin system is utilized in response to Na+ deficiency.
“…9, D-7900 Ulm (Donau), West Germany. Ferraro, Nahmod, Goldstein & Finkielman, 1971 ;Ganten, Kusumoto, Constantopoulos, Ganten, Boucher & Genest, 1973). In previous experiments, the presence of renin in arterial walls has been demonstrated (Rosenthal, Boucher, Rojo-Ortega & Genest, 1969;Genest, Shard, Rosenthal & Boucher, 1969;Hayduk, Boucher & Genest, 1970;Basso & Taquini, 1971) and in later reports the importance of angiotensin II generated at the peripheral vascular level has been stressed (Brunner, Chang, Wallach, Sealey & Laragh, 1972;Swales & Thurston, 1973;Thurston & Swales, 1974).…”
1.The metabolic role of arterial angiotensin I-forming enzyme (i.e. renin activity) was studied in total homogenates and in subcellular fractions of the aorta of normotensive and hypertensive rats.2. Angiotensin I-forming enzyme was measured in (a) uninephrectomized rats rendered hypertensive with D-aldosterone and sodium chloride (10 g/l) drinking solution, (b) rats treated in the same manner but with the addition of spironolactone, and (c) control rats.3. Hypertension developed in aldosterone-treated rats within 3-6 weeks and was associated with decreased plasma and renal renin values. Total aortic renin activity was up to sixfold higher in the hypertensive animals than in control animals and there was an increased ratio of supernatant to microsomal renin activity in the aorta.4. In spironolactone-treated rats blood pressure and total aortic renin concentrations were comparable with those in the control rats.5. The results support the hypothesis that renin generated at local vascular sites, which is independent of circulating renin levels, contributes to regulation of blood pressure.
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