Definitive Evidence for Renin in Rat Brain by Affinity Chromatographic Separation from Protease

1978 ◽  
Vol 55 (s4) ◽  
pp. 121s-123s ◽  
Author(s):  
Tadashi Inagami ◽  
Hideyoshi Yokosawa ◽  
Shigehisa Hirose

1. Angiotensin I-generating activity of rat brain extract was separated into two components by affinity chromatography on a casein—Sepharose gel column. 2. The component without affinity to the gel was identified as true renin on the basis of its sensitivity to anti-renin antibody and the lack of protease activity. 3. The second renin-like component with affinity to the gel was a protease insensitive to the anti-renin antibody. Its renin-like activity examined with sheep substrate was pronounced compared with the rate of angiotensin I generation from the rat substrate. 4. It was concluded that rat brain contains true renin, which can be detected by the use of rat substrate but can be masked when examined with sheep substrate.

1982 ◽  
Vol 242 (5) ◽  
pp. E292-E297 ◽  
Author(s):  
V. J. Dzau ◽  
A. Brenner ◽  
N. L. Emmett

We observed that unfractionated rat brain extract incubated with substrate at pH 6.0 yielded 12 times the quantity of angiotensin I as incubations at pH 7.4, but the enzyme activity measured at pH 6 was not primarily due to renin. To examine the existence of renin in brain, we used three methods of affinity chromatography (pepstatin-, renin-specific antibody-, and alpha-casein-Sepharose) to fractionate the angiotensin I-generating enzymes in the brain. 1) Brain extract applied to renin-specific column eluted a peak of angiotensin-releasing activity (ARA) that had a pH optimum of 6.0. This ARA was inhibited by antirenin antibody. Another peak of ARA with a pH optimum of 4 appeared in the nonbound fraction. This peak was not affected by antirenin antibody and had acid protease activity. 2) Pepstatin affinity column elution with lithium bromide yielded an early ARA peak (pH optimum 6.5), inhibited by antirenin antibody and a later peak (pH optimum 4.0) not inhibited by antirenin antibody. The latter contained acid protease activity. 3) alpha-Casein-Sepharose column also separated neutral proteases and immunoreactive renin from acid protease capable of generating angiotensin. In summary, rat brain contains a host of angiotensin I-generating enzymes that can be detected and separated as neutral and acid proteases and immunoreactive renin depending on the pH of the assay and conditions of purification. These findings indicate the presence of an enzyme with immunoidentity to renin in rat brain but do not imply local biosynthesis.


1980 ◽  
Vol 59 (s6) ◽  
pp. 45s-47s ◽  
Author(s):  
V. J. Dzau ◽  
Amy Brenner ◽  
Neremiah Emmett ◽  
E. Haber

1. The major angiotensin I-generating activity of rat brain extracts has a pH optimum different from that of renal renin and is not inhibited by renin specific antibody. 2. Affinity chromatography utilizing renin specific antibody, pepstatin and α-casein yielded fractions that resembled renal renin more closely with respect to antibody inhibition and pH optimum as well as an absence of the ability to hydrolyse haemoglobin. 3. We conclude that rat brain contains a host of enzymes with angiotensin I-generating activity including acid and neutral proteases and an enzyme with the immunochemical identity of renal renin. The biosynthetic origins of this renin-like protein remain uncertain.


1988 ◽  
Vol 47 (2) ◽  
pp. 125-132 ◽  
Author(s):  
Klaus Hermann ◽  
Mohan K. Raizada ◽  
Colin Sumners ◽  
M. Ian Phillips

1994 ◽  
Vol 91 (10) ◽  
pp. 4574-4578 ◽  
Author(s):  
S. Loukas ◽  
M. Mercouris ◽  
F. Panetsos ◽  
C. Zioudrou

2016 ◽  
Vol 25 (6) ◽  
pp. 1331-1331
Author(s):  
Iman Razeghian Jahromi ◽  
Davood Mehrabani ◽  
Ali Mohammadi ◽  
Mehdi Dianatpour ◽  
Amin Tamadon ◽  
...  

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