B. Tancini et al., Evidence for the regulation of beta-N-acetylhexosaminidase expression during pregnancy in the rat, BBA-GEN SUB, 1475(2), 2000, pp. 184-190
It is believed that the lysosomal glycohydrolase beta-N-acetylhexosaminidas
e plays a part in several important processes of reproduction and it has be
en postulated that this enzyme is subject to hormonal regulation. During pr
egnancy, activity levels of the enzyme are strongly increased in both human
and rat serum. However. little is known about the expression of this enzym
e in the female reproductive apparatus and there is no evidence linking the
production of hexosaminidase alpha- and beta-subunits to pregnancy. To cla
rify these aspects better. we examined the enzyme activity, isoenzyme subun
it composition and distribution, as well as steady state levels of alpha- a
nd beta-subunit mRNAs in the female reproductive organs and in other select
ed tissues of pregnant and non-pregnant rats. Among the female rat tissues
tested, the ovary and kidney had the highest specific activity. Pregnancy m
odulated the hexosaminidase activity differently in the tissues examined. I
n pregnant rats, the activity decreased in the ovary but increased signific
antly in the uterus, liver and to a lesser extent in other tissues. The dec
reased hexosaminidase activity in the ovary from pregnant rats appeared to
be accompanied by a disproportionately large decrease in beta-subunit mRNA
abundance, whereas in the uterus and liver, an increased abundance of this
transcript was detectable. The abundance of alpha-subunit mRNA was comparab
le in pregnant and control rat tissues. Hexosaminidase histochemical staini
ng of tissue sections clearly demonstrates that the greatly increased activ
ity of hexosaminidase in the uterus during pregnancy is largely due to the
enzyme in the endometrium. and not to the uterus as a whole. The overall re
sults provide evidence that, during pregnancy, a mechanism(s) of regulation
of beta-N-acetylhexosaminidase expression is in operation, and that the en
zyme is differentially regulated in rat tissues. (C) 2000 Elsevier Science
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