Jf. Telfer et al., EXPRESSION OF SUPEROXIDE-DISMUTASE AND XANTHINE-OXIDASE IN MYOMETRIUM, FETAL MEMBRANES AND PLACENTA DURING NORMAL HUMAN-PREGNANCY AND PARTURITION, Human reproduction, 12(10), 1997, pp. 2306-2312
Superoxide, an agent which attenuates the half-life of nitric oxide, i
s metabolized and synthesized by superoxide dismutase (SOD) and xanthi
ne oxidase, respectively. Over the last few Sears much work has focuse
d on the role of nitric oxide in human parturition. The aim of this st
udy was to determine whether the onset of human parturition is associa
ted with a change in the expression of copper/zinc superoxide dismutas
e (Cu/Zn SOD), manganese superoxide dismutase (Mn SOD) or xanthine oxi
dase within the uterus. Samples of myometrium, placenta, decidua and f
etal membranes were obtained from women before and after the onset of
labour at term. Immunocytochemistry was used to localize Cu/Zn SOD, Mn
SOD and xanthine oxidase and measure SOD enzyme activity. Cu/Zn and M
n SOD-like immunoreactivity was detected in syncytiotrophoblast cells,
villous stromal cells and endothelial cells of blood vessels in the p
lacenta. In the myometrium Cu/Zn and Mn SOD were localized to myocytes
and endothelial cells and to some vascular smooth muscle cells. In th
e fetal membranes we observed staining for Cu/Zn SOD and;Mn SOD in the
amnion, chorion, extravillous trophoblast and decidua. There was no d
ifference in SOD enzyme activity or staining intensity for SOD between
different cell types before and during labour, Xanthine oxidase immun
oreactivity was identified in each of the tissues examined and again t
here was no difference in immunostaining in tissues obtained from wome
n delivered before or after the onset of labour. These results show th
at the pregnant uterus is capable of both synthesizing and degrading s
uperoxide and suggest that superoxide dismutase and xanthine oxidase m
ay play a role in the maintenance of uterine quiescence during pregnan
cy, but not in the initiation of parturition.