CG&D
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kim, S. Y.
Right arrow Articles by Lee, K.-J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kim, S. Y.
Right arrow Articles by Lee, K.-J.
Cell Growth & Differentiation Vol. 11, 485-490, September 2000
© 2000 American Association for Cancer Research


Articles

Inhibition of Progesterone-induced Xenopus Oocyte Maturation by Nm231

Sun Young Kim, James E. Ferrell, Jr., Suhn-Kee Chae and Kong-Joo Lee2

Center for Cell Signaling Research, Division of Molecular Life Sciences and College of Pharmacy, Ewha Womans University, Seoul 120-750, Korea [S. Y. K., K-J. L.]; Department of Molecular Pharmacology, Stanford University School of Medicine, Stanford, California 94305-5332 [J. E. F.]; and Division of Life Sciences, Paichai University, Taejon 302-735, Korea [S-K. C.]

Abstract

The Nm23 protein has been implicated in a wide variety of biological processes, including suppression of metastasis, phytochrome responses in plants, and regulation of differentiation. Here we examine whether Nm23 is involved in Xenopus laevis oocyte maturation. We found that Nm23 is present in oocytes, indicating that it has the potential to be a regulator of maturation. Furthermore, modest overexpression of Nm23 inhibited progesterone-induced oocyte maturation. This maturation-inhibitory activity was shared by both the acidic Nm23-H1 isoform and the basic Nm23-H2 isoform and by Nm23 mutants that lack nucleoside diphosphate kinase activity (Nm23-H1 H118F and Nm23-H2 H118F). Expression of Nm23 proteins delayed the accumulation of Mos and the activation of p42 mitogen-activated protein kinase (MAPK) in progesterone-treated oocytes but had no discernible effect on Mos-induced p42 MAPK activation. Therefore, Nm23 appears to act upstream of the Mos/mitogen-activated protein/extracellular signal-regulated kinase kinase/p42 MAPK cascade. These findings suggest a novel biological role for Nm23.







HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation
Copyright © 2000 by the American Association of Cancer Research.