Renin activity in dog brain: enzymological similarity to cathepsin D.
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 during this procedure; cathepsin D activity accompanied the brain renin activity throughout the purification and showed a similar increase in specific activity. The renin and cathepsin activity in the partially purified preparation behaved identically during isoelectric focusing. The partially purified renin and cathepsin activity exhibited saturation kinetics with their respective substrates and were without activity above pH 6.0. Both enzyme activities were irreversibly inhibited by the pepsin inhibitor pepstatin, in nanomolar concentrations. These data, in conjunction with the literature concerning brain cathepsin, suggest that the renin activity in brain is due to cathepsin D, and that this renin activity exhibited by cathepsin D may be of limited significance under physiological conditions.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002403:Cathepsins / Q000302:isolation & purification / Q000378:metabolism*; D004285:Dogs; D010450:Endopeptidases / Q000378:metabolism; D007525:Isoelectric Focusing; D012083:Renin / Q000302:isolation & purification / Q000378:metabolism*
D002403:Cathepsins; D010450:Endopeptidases; D012083:Renin