Ma. Cicilini et al., HEART PROLYL ENDOPEPTIDASE ACTIVITY IN ONE-KIDNEY, ONE-CLIP HYPERTENSIVE RATS, Brazilian journal of medical and biological research, 27(12), 1994, pp. 2821-2830
1. Heart mass, prolyl endopeptidase activity and fractionated proteins
from heart tissue were studied in one-kidney, one clip hypertensive r
ats (N = 6) and compared to sham-operated rats (N = 6). 2. Body weight
, arterial pressure and tissue mass were measured 4 weeks after artery
clipping. Z-Gly-Pro-p-nitroaniline hydrolysis was used to measure tis
sue prolyl endopeptidase activity in the homogenate. Protein was fract
ionated into the soluble and myofibrillar fractions. 3. In the normote
nsive rats, prolyl endopeptidase activity expressed in terms of protei
n specific activity (mu M substrate hydrolyzed h(-1) mg supernatant pr
otein(-1)) occurred in atria and was 2.5-fold higher than in the ventr
icles (3.79 +/- 0.20 vs 1.44 +/- 0.02, P<0.05). In the one-kidney, one
clip hypertensive rats, the left ventricle tissue increased 1.7-fold
(2.27 +/- 0.11 vs 3.72 +/- 0.11 mg wet weight tissue/g body weight, P<
0.001), the soluble protein fraction (54.86 +/- 3.60 vs 57.38 +/- 6.64
mg/g wet weight tissue) was unchanged, while the myofibrillar fractio
n increased 1.9-fold (118.9 +/- 9.09 vs 229.8 +/- 8.47 mg/g wet weight
tissue, P<0.001). 4. The specific activity of the atrial and ventricu
lar prolyl endopeptidase decreased in atria and increased in ventricle
s as the result of hypertension (3.79 +/- 0.2 vs 2.84 +/- 0.13 and 1.4
4 +/- 0.02 vs 1.87 +/- 0.13; respectively). These regional differences
in prolyl endopeptidase enzyme content caused by one-kidney, one clip
hypertension in neurosecretory and non-neurosecretory heart areas sug
gest that this enzyme plays a local role in the turnover of specific p
olypeptides.