HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted 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 Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kimura, A. Articles by Murata, Y. Search for Related Content PubMed PubMed Citation Articles by Kimura, A. Articles by Murata, Y. Social Bookmarking                      What's this?

J Biol Chem, Vol. 275, Issue 5, 3667-3674, February 4, 2000

Prolactin-releasing Peptide Activation of the Prolactin Promoter Is Differentially Mediated by Extracellular Signal-regulated Protein Kinase and c-Jun N-terminal Protein Kinase^*

Akiko Kimura, Masahide Ohmichi, Keiichi Tasaka, Yuki Kanda, Hiromasa Ikegami, Jun Hayakawa, Koji Hisamoto, Ken-ichirou Morishige, Shuji Hinuma^§, Hirohisa Kurachi, and Yuji Murata

From the Department of Obstetrics and Gynecology, Osaka University Medical School, 2-2, Yamadaoka, Suita, Osaka 565-0871, Japan and ^§ Discovery Research Laboratories I, Pharmaceutical Discovery Research Division, Takeda Chemical Industries Ltd., 10 Wadai, Tsukuba, Ibaraki 300-4293, Japan

Regulation of the mitogen-activated protein kinase (MAPK) family by prolactin-releasing peptide (PrRP) in both GH3 rat pituitary tumor cells and primary cultures of rat anterior pituitary cells was investigated. PrRP rapidly and transiently activated extracellular signal-regulated protein kinase (ERK) in both types of cells. Both pertussis toxin, which inactivates G_i/G_o proteins, and exogenous expression of a peptide derived from the carboxyl terminus of the -adrenergic receptor kinase I, which specifically blocks signaling mediated by the subunits of G proteins, completely blocked the PrRP-induced ERK activation, suggesting the involvement of G_i/G_o proteins in the PrRP-induced ERK activation. Down-regulation of cellular protein kinase C did not significantly inhibit the PrRP-induced ERK activation, suggesting that a protein kinase C-independent pathway is mainly involved. PrRP-induced ERK activation was not dependent on either extracellular Ca²⁺ or intracellular Ca²⁺. However, the ERK cascade was not the only route by which PrRP communicated with the nucleus. JNK was also shown to be significantly activated in response to PrRP. JNK activation in response to PrRP was slower than ERK activation. Moreover, to determine whether a MAPK family cascade regulates rat prolactin (rPRL) promoter activity, we transfected the intact rPRL promoter ligated to the firefly luciferase reporter gene into GH3 cells. PrRP activated the rPRL promoter activity in a time-dependent manner. Co-transfection with a catalytically inactive form of a MAPK construct or a dominant negative JNK, partially but significantly inhibited the induction of the rPRL promoter by PrRP. Furthermore, co-transfection with a dominant negative Ets completely abolished the response of the rPRL promoter to PrRP. These results suggest that PrRP differentially activates ERK and JNK, and both cascades are necessary to elicit rPRL promoter activity in an Ets-dependent mechanism.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				T Nanmoku, K Takekoshi, T Fukuda, K Ishii, K Isobe, and Y Kawakami Stimulation of catecholamine biosynthesis via the PKC pathway by prolactin-releasing peptide in PC12 rat pheochromocytoma cells J. Endocrinol., July 1, 2005; 186(1): 233 - 239. [Abstract] [Full Text] [PDF]

				S. Mabuchi, M. Ohmichi, Y. Nishio, T. Hayasaka, A. Kimura, T. Ohta, J. Kawagoe, K. Takahashi, N. Yada-Hashimoto, H. Seino-Noda, et al. Inhibition of Inhibitor of Nuclear Factor-{kappa}B Phosphorylation Increases the Efficacy of Paclitaxel in in Vitro and in Vivo Ovarian Cancer Models Clin. Cancer Res., November 15, 2004; 10(22): 7645 - 7654. [Abstract] [Full Text] [PDF]

				S. Mabuchi, M. Ohmichi, Y. Nishio, T. Hayasaka, A. Kimura, T. Ohta, M. Saito, J. Kawagoe, K. Takahashi, N. Yada-Hashimoto, et al. Inhibition of NF{kappa}B Increases the Efficacy of Cisplatin in in Vitro and in Vivo Ovarian Cancer Models J. Biol. Chem., May 28, 2004; 279(22): 23477 - 23485. [Abstract] [Full Text] [PDF]

				E. Arimoto-Ishida, M. Ohmichi, S. Mabuchi, T. Takahashi, C. Ohshima, J. Hayakawa, A. Kimura, K. Takahashi, Y. Nishio, M. Sakata, et al. Inhibition of Phosphorylation of a Forkhead Transcription Factor Sensitizes Human Ovarian Cancer Cells to Cisplatin Endocrinology, April 1, 2004; 145(4): 2014 - 2022. [Abstract] [Full Text] [PDF]

				S. Mabuchi, M. Ohmichi, A. Kimura, Y. Ikebuchi, K. Hisamoto, E. Arimoto-Ishida, Y. Nishio, K. Takahashi, K. Tasaka, and Y. Murata Tamoxifen Inhibits Cell Proliferation via Mitogen-Activated Protein Kinase Cascades in Human Ovarian Cancer Cell Lines in a Manner Not Dependent on the Expression of Estrogen Receptor or the Sensitivity to Cisplatin Endocrinology, March 1, 2004; 145(3): 1302 - 1313. [Abstract] [Full Text] [PDF]

				T. A. Jackson, D. M. Koterwas, M. A. Morgan, and A. P. Bradford Fibroblast Growth Factors Regulate Prolactin Transcription via an Atypical Rac-Dependent Signaling Pathway Mol. Endocrinol., October 1, 2003; 17(10): 1921 - 1930. [Abstract] [Full Text] [PDF]

				M. Engstrom, A. Brandt, S. Wurster, J.-M. Savola, and P. Panula Prolactin Releasing Peptide Has High Affinity and Efficacy at Neuropeptide FF2 Receptors J. Pharmacol. Exp. Ther., June 1, 2003; 305(3): 825 - 832. [Abstract] [Full Text] [PDF]

				D. L. Duval and A. Gutierrez-Hartmann Editorial: PRL-Releasing Peptide Stimulation of PRL Gene Transcription--Enter AKT Endocrinology, January 1, 2002; 143(1): 11 - 12. [Full Text] [PDF]

				J. Hayakawa, M. Ohmichi, K. Tasaka, Y. Kanda, K. Adachi, Y. Nishio, K. Hisamoto, S. Mabuchi, S. Hinuma, and Y. Murata Regulation of the PRL Promoter by Akt through cAMP Response Element Binding Protein Endocrinology, January 1, 2002; 143(1): 13 - 22. [Abstract] [Full Text] [PDF]

				K. Hisamoto, M. Ohmichi, Y. Kanda, K. Adachi, Y. Nishio, J. Hayakawa, S. Mabuchi, K. Takahashi, K. Tasaka, Y. Miyamoto, et al. Induction of Endothelial Nitric-oxide Synthase Phosphorylation by the Raloxifene Analog LY117018 Is Differentially Mediated by Akt and Extracellular Signal-regulated Protein Kinase in Vascular Endothelial Cells J. Biol. Chem., December 7, 2001; 276(50): 47642 - 47649. [Abstract] [Full Text] [PDF]

				T. Rubinek, M. Hadani, G. Barkai, S. Melmed, and I. Shimon Prolactin (PRL)-Releasing Peptide Stimulates PRL Secretion from Human Fetal Pituitary Cultures and Growth Hormone Release from Cultured Pituitary Adenomas J. Clin. Endocrinol. Metab., June 1, 2001; 86(6): 2826 - 2830. [Abstract] [Full Text] [PDF]

				K. Hisamoto, M. Ohmichi, H. Kurachi, J. Hayakawa, Y. Kanda, Y. Nishio, K. Adachi, K. Tasaka, E. Miyoshi, N. Fujiwara, et al. Estrogen Induces the Akt-dependent Activation of Endothelial Nitric-oxide Synthase in Vascular Endothelial Cells J. Biol. Chem., January 26, 2001; 276(5): 3459 - 3467. [Abstract] [Full Text] [PDF]

				T. Yokoi, M. Ohmichi, K. Tasaka, A. Kimura, Y. Kanda, J. Hayakawa, M. Tahara, K. Hisamoto, H. Kurachi, and Y. Murata Activation of the Luteinizing Hormone beta Promoter by Gonadotropin-releasing Hormone Requires c-Jun NH2-terminal Protein Kinase J. Biol. Chem., July 7, 2000; 275(28): 21639 - 21647. [Abstract] [Full Text] [PDF]