Regulation of alpha 1-beta 3-NA(+)-K(+)-ATPase isozyme during meiotic maturation of Xenopus laevis oocytes

Détails

ID Serval
serval:BIB_B73C2768CDF8
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Regulation of alpha 1-beta 3-NA(+)-K(+)-ATPase isozyme during meiotic maturation of Xenopus laevis oocytes
Périodique
American Journal of Physiology
Auteur(s)
Pralong-Zamofing  D., Yi  Q. H., Schmalzing  G., Good  P., Geering  K.
ISSN
0002-9513 (Print)
Statut éditorial
Publié
Date de publication
06/1992
Volume
262
Numéro
6 Pt 1
Pages
C1520-30
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Jun
Résumé
During progesterone-induced maturation of Xenopus oocytes, the transport and ouabain binding capacity of Na(+)-K(+)-ATPase at the plasma membrane is completely downregulated. To elucidate the mechanism and the physiological significance of this process, we have followed the fate of oocyte alpha-beta 3-Na(+)-K(+)-ATPase complexes during meiotic maturation and early embryonic development. An immunocytochemical follow-up of the catalytic alpha-subunit, ouabain binding studies, cell surface iodination, and oocyte cell fractionation combined with immunochemical subunit detection provides evidence that following progesterone treatment Na(+)-K(+)-ATPase molecules are retrieved from the oocyte plasma membrane. The enzyme complexes are recovered in an active form in an intracellular compartment in both in vitro and in vivo matured eggs. Exogenous Xenopus alpha 1- and beta 1-complexes expressed in the oocyte from injected cRNAs are regulated by progesterone similar to endogenous Na(+)-K(+)-ATPase complexes. Finally, active Na(+)-K+ pumps internalized during oocyte maturation appear to be redistributed to plasma membrane fractions during blastula formation in Xenopus embryos. In conclusion, our data suggest that endocytosis of alpha 1- and beta 3-complexes during meiotic maturation of Xenopus oocytes is responsible for downregulation of Na(+)-K(+)-ATPase activity and results in an intracellular pool of functional enzymes, which might be reexpressed during early development in response to physiological needs.
Mots-clé
Animals Cell Membrane/enzymology Embryo, Nonmammalian/*physiology Endocytosis Female Fertilization Isoenzymes/genetics/*metabolism Male Meiosis/physiology Microsomes/enzymology Na(+)-K(+)-Exchanging ATPase/genetics/*metabolism Oocytes/cytology/drug effects/*physiology Ouabain/metabolism Progesterone/*pharmacology Protein Binding RNA/genetics/metabolism Subcellular Fractions/enzymology Xenopus laevis
Pubmed
Web of science
Création de la notice
24/01/2008 12:28
Dernière modification de la notice
20/08/2019 15:25
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