This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Copyright Permission Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Tessier, C. Articles by Gibori, G. Search for Related Content PubMed PubMed Citation Articles by Tessier, C. Articles by Gibori, G.

PRL Antiapoptotic Effect in the Rat Decidua Involves the PI3K/Protein Kinase B-Mediated Inhibition of Caspase-3 Activity

Department of Physiology and Biophysics, University of Illinois College of Medicine, Chicago, Illinois 60612

Address all correspondence and requests for reprints to: Dr. Geula Gibori, Department of Physiology and Biophysics (M/C 901), University of Illinois, 835 South Wolcott Avenue, Chicago, Illinois 60612-7342. E-mail: ggibori{at}uic.edu

During gestation, the uterus undergoes severe changes to accommodate and protect the developing conceptus. In particular, stromal endometrial cells proliferate and differentiate to form the decidual tissue, which produces PRL. Once the conceptus begins to grow, extensive regression by apoptosis take place in the decidua coincident with the loss of the PRL receptor in this tissue. In this report we have established for the first time that PRL, acting through the long form of the PRL receptor and the PI3K pathway, exerts an antiapoptotic effect in rat decidua. We have also shown that protein kinase B phosphorylation on serine 473 as well as its nuclear translocation are stimulated by PRL in decidual cells. Moreover, we have found that caspase-3, a well known effector of apoptosis, becomes expressed and active in the rat decidua just at a time when this tissue undergoes extensive apoptosis. PRL was able to down-regulate both caspase-3 mRNA levels as well as activity. Furthermore, using a protein kinase B dominant-negative expression vector, we provide evidence that PRL inhibition of caspase-3 requires an intact protein kinase B pathway. Finally, we have also found that rat placental lactogen I and II dose-dependently inhibit caspase-3 mRNA, suggesting multiple sources of PRL in the hormonal control of rat decidual regression. In summary, the results of this study have defined an important role for decidual PRL in the normal progress of pregnancy, specifically in the regression and reorganization of the decidua.

This article has been cited by other articles:

				Y. S. Devi, A. Shehu, C. Stocco, J. Halperin, J. Le, A. M. Seibold, M. Lahav, N. Binart, and G. Gibori Regulation of Transcription Factors and Repression of Sp1 by Prolactin Signaling Through the Short Isoform of Its Cognate Receptor Endocrinology, July 1, 2009; 150(7): 3327 - 3335. [Abstract] [Full Text] [PDF]

				S. M. K. Alam, T. Konno, N. Sahgal, L. Lu, and M. J. Soares Decidual Cells Produce a Heparin-binding Prolactin Family Cytokine with Putative Intrauterine Regulatory Actions J. Biol. Chem., July 4, 2008; 283(27): 18957 - 18968. [Abstract] [Full Text] [PDF]

				N. Ben-Jonathan, C. R. LaPensee, and E. W. LaPensee What Can We Learn from Rodents about Prolactin in Humans? Endocr. Rev., February 1, 2008; 29(1): 1 - 41. [Abstract] [Full Text] [PDF]

				Y. Fujinaka, K. Takane, H. Yamashita, and R. C. Vasavada Lactogens Promote Beta Cell Survival through JAK2/STAT5 Activation and Bcl-XL Upregulation J. Biol. Chem., October 19, 2007; 282(42): 30707 - 30717. [Abstract] [Full Text] [PDF]

				L. Bao, C. Tessier, A. Prigent-Tessier, F. Li, O. L. Buzzio, E. A. Callegari, N. D. Horseman, and G. Gibori Decidual Prolactin Silences the Expression of Genes Detrimental to Pregnancy Endocrinology, May 1, 2007; 148(5): 2326 - 2334. [Abstract] [Full Text] [PDF]

				A. Jasinska, Z. Strakova, M. Szmidt, and A. T. Fazleabas Human Chorionic Gonadotropin and Decidualization in Vitro Inhibits Cytochalasin-D-Induced Apoptosis in Cultured Endometrial Stromal Fibroblasts Endocrinology, September 1, 2006; 147(9): 4112 - 4121. [Abstract] [Full Text] [PDF]

				C Zermeno, J Guzman-Morales, Y Macotela, G Nava, F Lopez-Barrera, J B Kouri, C Lavalle, G M. de la Escalera, and C Clapp Prolactin inhibits the apoptosis of chondrocytes induced by serum starvation. J. Endocrinol., May 1, 2006; 189(2): R1 - R8. [Abstract] [Full Text] [PDF]

				A. Toyofuku, T. Hara, T. Taguchi, Y. Katsura, K. Ohama, and Y. Kudo Cyclic and characteristic expression of phosphorylated Akt in human endometrium and decidual cells in vivo and in vitro Hum. Reprod., May 1, 2006; 21(5): 1122 - 1128. [Abstract] [Full Text] [PDF]

				J. P. Bailey, K. M. Nieport, M. P. Herbst, S. Srivastava, R. A. Serra, and N. D. Horseman Prolactin and Transforming Growth Factor-{beta} Signaling Exert Opposing Effects on Mammary Gland Morphogenesis, Involution, and the Akt-Forkhead Pathway Mol. Endocrinol., May 1, 2004; 18(5): 1171 - 1184. [Abstract] [Full Text] [PDF]

				C. Tessier, A. Prigent-Tessier, L. Bao, C. M. Telleria, S. Ferguson-Gottschall, G. B. Gibori, Y. Gu, J. M. Bowen-Shauver, N. D. Horseman, and G. Gibori Decidual Activin: Its Role In the Apoptotic Process and Its Regulation by Prolactin Biol Reprod, May 1, 2003; 68(5): 1687 - 1694. [Abstract] [Full Text] [PDF]