Umbilical plasma kininase I activity in fetal hypoxia.
To shed light on the role of bradykinin in preeclampsia in addition to acute hypoxia, we measured the activity of kininase I, the enzyme responsible for its degradation, in umbilical plasma. Kininase I activity in umbilical arteries was compared with that in the umbilical veins. The relationship between kininase I and pH values was also evaluated in women with and without preeclampsia. Also, enzyme activity in supernatants of fetal hepatic cells (NFL/T) cultured under hypoxic or normoxic conditions were determined. Kininase I activity levels in fetal umbilical arteries and veins (n = 33) were similar (r = 0.77). Hypoxia caused suppression of kininase I activity in the supernatant cultures of NFL/T after one hour. However, after 8 and 24 hours, kininase I activity was significantly greater than under normoxic conditions (p < 0.05). Kininase I activity of fetal umbilical vein significantly decreased in the presence of acidemia in the uncomplicated group (n = 75, r = 0.42), whereas the activity negatively correlated with umbilical arterial pH in the preeclamptic group (n = 10, r = - 0.65). Kininase I activity levels in cases complicated with preeclampsia were significantly higher than without preeclampsia (49.2 +/- 9.1 vs. 66.2 +/- 11.3 nmol/ml/min). The present study indicates that kininase I acts as a regulatory factor in bradykinin degradation.
Tsukahara
Y
Y
Department of Obstetrics and Gynecology, Nagoya University Graduate School of Medicine, Japan.
Itakura
A
A
Ohno
Y
Y
Ando
H
H
Mizutani
S
S
D001920:Bradykinin / Q000378:metabolism; D005260:Female; D005312:Fetal Blood / Q000201:enzymology*; D005311:Fetal Hypoxia / Q000201:enzymology*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D001121:Lysine Carboxypeptidase / Q000097:blood*; D011247:Pregnancy; D014469:Umbilical Arteries; D014471:Umbilical Veins
D001121:Lysine Carboxypeptidase; D001920:Bradykinin