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Hormonal control of enzyme activity during the plasma membrane transformation of uterine epithelial cells.
- Source :
-
Cell biology international [Cell Biol Int] 2001; Vol. 25 (9), pp. 859-71. - Publication Year :
- 2001
-
Abstract
- Ultrastructural and light microscopic catalytic histochemical methods were used to study the distribution and changes in distribution of four phosphatase enzymes; alkaline phosphatase, 5'-nucleotidase, thiamine pyrophosphatase and adenosine triphosphatase in uterine epithelial cells in response to the ovarian hormones, oestrogen, progesterone or a combination of both used in different regimes on ovariectomised rats. Reaction product for all four enzymes was clearly localised in the epithelial cells, especially with oestrogen priming. However, the four enzymes showed markedly different patterns of organisation of reaction product in response to other hormonal treatments. Our findings clearly show that the expression of these enzymes is under ovarian hormonal control. However, while all of the enzymes are upregulated by oestrogen, the response to progesterone is variable, which can upregulate or downregulate different enzymes. The findings are particularly obvious at the electron microscopic level on the apical plasma membrane of the uterine epithelial cells, which was the main focus of our study.<br /> (Copyright 2001 Academic Press.)
- Subjects :
- 5'-Nucleotidase metabolism
Adenosine Triphosphatases metabolism
Alkaline Phosphatase metabolism
Animals
Cell Membrane drug effects
Cell Membrane enzymology
Epithelial Cells drug effects
Female
Histocytochemistry
Rats
Rats, Wistar
Thiamine Pyrophosphatase metabolism
Up-Regulation
Cell Membrane ultrastructure
Epithelial Cells enzymology
Epithelial Cells ultrastructure
Estrogens pharmacology
Progesterone pharmacology
Uterus cytology
Subjects
Details
- Language :
- English
- ISSN :
- 1065-6995
- Volume :
- 25
- Issue :
- 9
- Database :
- MEDLINE
- Journal :
- Cell biology international
- Publication Type :
- Academic Journal
- Accession number :
- 11518493
- Full Text :
- https://doi.org/10.1006/cbir.2001.0771