It is believed that the lysosomal glycohydrolase beta-N-acetylhexosaminidase plays a part in several important processes of reproduction and it has been postulated that this enzyme is subject to hormonal regulation. During pregnancy, activity levels of the enzyme are strongly increased in both human and rat serum. However. little is known about the expression of this enzyme in the female reproductive apparatus and there is no evidence linking the production of hexosaminidase alpha- and beta-subunits to pregnancy. To clarify these aspects better. we examined the enzyme activity, isoenzyme subunit composition and distribution, as well as steady state levels of alpha- and beta-subunit mRNAs in the female reproductive organs and in other selected tissues of pregnant and non-pregnant rats. Among the female rat tissues tested, the ovary and kidney had the highest specific activity. Pregnancy modulated the hexosaminidase activity differently in the tissues examined. In pregnant rats, the activity decreased in the ovary but increased significantly in the uterus, liver and to a lesser extent in other tissues. The decreased 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 comparable in pregnant and control rat tissues. Hexosaminidase histochemical staining of tissue sections clearly demonstrates that the greatly increased activity 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 results provide evidence that, during pregnancy, a mechanism(s) of regulation of beta-N-acetylhexosaminidase expression is in operation, and that the enzyme is differentially regulated in rat tissues. (C) 2000 Elsevier Science B.V. All rights reserved.
Evidence for the regulation of beta-N-acetylhexosaminidase expression during pregnancy in the rat
TANCINI, Brunella;EMILIANI, Carla;MENCARELLI, Simona;CAVALIERI, Cristina;ORLACCHIO, Aldo
2000
Abstract
It is believed that the lysosomal glycohydrolase beta-N-acetylhexosaminidase plays a part in several important processes of reproduction and it has been postulated that this enzyme is subject to hormonal regulation. During pregnancy, activity levels of the enzyme are strongly increased in both human and rat serum. However. little is known about the expression of this enzyme in the female reproductive apparatus and there is no evidence linking the production of hexosaminidase alpha- and beta-subunits to pregnancy. To clarify these aspects better. we examined the enzyme activity, isoenzyme subunit composition and distribution, as well as steady state levels of alpha- and beta-subunit mRNAs in the female reproductive organs and in other selected tissues of pregnant and non-pregnant rats. Among the female rat tissues tested, the ovary and kidney had the highest specific activity. Pregnancy modulated the hexosaminidase activity differently in the tissues examined. In pregnant rats, the activity decreased in the ovary but increased significantly in the uterus, liver and to a lesser extent in other tissues. The decreased 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 comparable in pregnant and control rat tissues. Hexosaminidase histochemical staining of tissue sections clearly demonstrates that the greatly increased activity 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 results provide evidence that, during pregnancy, a mechanism(s) of regulation of beta-N-acetylhexosaminidase expression is in operation, and that the enzyme is differentially regulated in rat tissues. (C) 2000 Elsevier Science B.V. All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
