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) 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 Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Iemura, S.-i. Articles by Ueno, N. Search for Related Content PubMed PubMed Citation Articles by Iemura, S.-i. Articles by Ueno, N. Social Bookmarking                      What's this?

J Biol Chem, Vol. 274, Issue 38, 26843-26849, September 17, 1999

Isolation and Characterization of Bone Morphogenetic Protein-binding Proteins from the Early Xenopus Embryo

Shun-ichiro Iemura, Takamasa S. Yamamoto, Chiyo Takagi, Hideyuki Kobayashi^§, and Naoto Ueno^¶

From the  Department of Developmental Biology, National Institute for Basic Biology, 38 Nishigonaka, Myodaiji, Okazaki, 444-8585 Japan, the ^§ National Food Research Institute, Ministry of Agriculture, Forestry and Fisheries, 2-1-2 Kannondai, Tsukuba, 305-8642 Japan, and the ^¶ Department of Molecular Biomechamics, School of Life Science, The Graduate University for Advanced Studies, 38 Nishigonaka, Myodaiji, Okazaki, 444-8585 Japan

Using a surface plasmon resonance biosensor as a sensitive and specific monitor, we have isolated two distinct bone morphogenetic protein (BMP)-binding proteins, and identified them as lipovitellin 1 and Ep45, respectively. Lipovitellin 1 is an egg yolk protein that is processed from vitellogenin. Both vitellogenin and Ep45 are synthesized under estrogen control in the liver, secreted, and taken up by developing oocytes. In this paper, we have shown that of the TGF- family members tested, Ep45 can bind only to BMP-4, whereas lipovitellin 1 can bind to both BMP-4 and activin A. Because of this difference in specificity, we have focused on and further studied Ep45. Kinetic parameters were determined by surface plasmon resonance studies and showed that Ep45 associated rapidly with BMP-4 (k_a = 1.06 × 10⁴ M¹s¹) and dissociated slowly (k_d = 1.6 × 10⁴ s¹). In Xenopus embryos microinjected with Ep45 mRNA, Ep45 blocked the ability of follistatin to inhibit BMP activity and to induce a secondary body axis in a dose-dependent manner, whereas it had no effect on other BMP antagonists, chordin and noggin. These results support the possibility that Ep45 interacts with BMP to modulate its activities in vivo.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				Z.-J. Shen, T. Nakamoto, K. Tsuji, A. Nifuji, K. Miyazono, T. Komori, H. Hirai, and M. Noda Negative Regulation of Bone Morphogenetic Protein/Smad Signaling by Cas-interacting Zinc Finger Protein in Osteoblasts J. Biol. Chem., August 9, 2002; 277(33): 29840 - 29846. [Abstract] [Full Text] [PDF]

				Y. Sidis, A. L. Schneyer, P. M. Sluss, L. N. Johnson, and H. T. Keutmann Follistatin: Essential Role for the N-terminal Domain in Activin Binding and Neutralization J. Biol. Chem., May 18, 2001; 276(21): 17718 - 17726. [Abstract] [Full Text] [PDF]