Cathepsin B Is a Prorenin Processing Enzyme

Hypertension ◽  
1996 ◽  
Vol 27 (3) ◽  
pp. 514-517 ◽  
Author(s):  
Francisco A.R. Neves ◽  
Keith G. Duncan ◽  
John D. Baxter
Keyword(s):  
Cathepsin B ◽  
Processing Enzyme

scholarly journals Identification of renal cathepsin B as a human prorenin-processing enzyme

1991 ◽  
Vol 266 (19) ◽  
pp. 12633-12638
Author(s):  
P.H. Wang ◽  
Y.S. Do ◽  
L. Macaulay ◽  
T. Shinagawa ◽  
P.W. Anderson ◽  
...  
Keyword(s):  
Cathepsin B ◽  
Processing Enzyme

Cathepsin B is not the processing enzyme for mouse prorenin

2010 ◽  
Vol 298 (5) ◽  
pp. R1212-R1216 ◽  
Author(s):  
Chantal Mercure ◽  
Marie-Josée Lacombe ◽  
Khashayarsha Khazaie ◽  
Timothy L. Reudelhuber
Keyword(s):  
Cathepsin B ◽  
Renin Angiotensin System ◽  
Apparent Molecular Weight ◽  
Culture Cell ◽  
Tissue Culture Cell ◽  
Active Renin ◽  
Processing Enzyme ◽  
Chloroquine Treatment

Renin, an aspartyl protease that catalyzes the rate-limiting step in the renin-angiotensin system (RAS), is proteolytically activated by a second protease [referred to as the prorenin processing enzyme (PPE)] before its secretion from the juxtaglomerular cells of the kidney. Although several enzymes are capable of activating renin in vitro, the leading candidate for the PPE in the kidney is cathepsin B (CTSB) due to is colocalization with the renin precursor (prorenin) in juxtaglomerular cell granules and because of its site-selective activation of human prorenin both in vitro and in transfected tissue culture cell models. To verify the role of CTSB in prorenin processing in vivo, we tested the ability of CTSB-deficient (CTSB−/−) mice to generate active renin. CTSB−/− mice do not exhibit any overt symptoms (renal malformation, preweaning mortality) typical of an RAS deficiency and have normal levels of circulating active renin, which, like those in control animals, rise more than 15-fold in response to pharmacologic inhibition of the RAS. The mature renin enzyme detected in kidney lysates of CTSB−/− mice migrates at the same apparent molecular weight as that in control mice, and the processing to active renin is not affected by chloroquine treatment of the animals. Finally, the distribution and morphology of renin-producing cells in the kidney is normal in CTSB−/− mice. In conclusion, CTSB-deficient mice exhibit no differences compared with controls in their ability to generate active renin, and our results do not support CTSB as the PPE in mice.

scholarly journals Role of Cathepsin B as Prorenin Processing Enzyme in Human Kidney.

1995 ◽  
Vol 18 (2) ◽  
pp. 131-136 ◽  
Author(s):  
Tatsuo Shinagawa ◽  
Kazuhisa Nakayama ◽  
Yasuo Uchiyama ◽  
Eiki Kominami ◽  
Yutaka Doi ◽  
...  
Keyword(s):  
Cathepsin B ◽  
Human Kidney ◽  
Processing Enzyme

Visualisierung und Quantifizierung der Cathepsin B-, K- und L-Aktivität in vitalen Knorpelzellen

2003 ◽  
Vol 141 (S 1) ◽  
Author(s):  
A Köcher ◽  
J Mollenhauer ◽  
B Wiederanders
Keyword(s):  
Cathepsin B

Cathepsin B Gen-Polymorphismus Val26: Keine Assoziation mit idiopathisch chronischer Pankreatitis bei deutschen Patienten

2007 ◽  
Vol 45 (08) ◽  
Author(s):  
F Weiss ◽  
CO Behn ◽  
P Simon ◽  
W Halangk ◽  
MM Lerch
Keyword(s):  
Cathepsin B
Sign in / Sign up

Export Citation Format

Share Document