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Originally published In Press as doi:10.1074/jbc.M006114200 on September 28, 2000

J. Biol. Chem., Vol. 275, Issue 52, 40788-40796, December 29, 2000
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Identification and Characterization of a Novel Follistatin-like Protein as a Binding Protein for the TGF-beta Family*

Kunihiro TsuchidaDagger §, Koji Y. AraiDagger , Yoji KuramotoDagger , Norio YamakawaDagger , Yoshihisa Hasegawa||, and Hiromu SuginoDagger

From the Dagger  Institute for Enzyme Research, University of Tokushima, 3-18-15 Kuramoto, Tokushima 770-8503, Japan and the || Laboratories of Experimental Animal Science, Kitasato University School of Veterinary Medicine and Animal Sciences, Towada, Aomori 034-8628, Japan

Follistatin is an activin-binding protein that prevents activin from binding to its receptors and neutralizes its activity. Follistatin also binds bone morphogenetic proteins (BMPs). In this study, we report the identification of a novel follistatin-like protein from mouse. The mouse cDNA encodes a 256-residue precursor and most likely a mouse homologue of human FLRG, which was found at the breakpoint of the chromosomal rearrangement in a B-cell line. Whereas follistatin has three follistatin domains, which are presumed to be growth factor binding motifs, FLRG possesses only two follistatin domains. Northern blotting revealed that mRNAs for FLRG were abundantly expressed in heart, lung, kidney, and testis in mouse. The recombinant mouse FLRG proteins were found to have binding activity for both activin and bone morphogenetic protein-2. Like follistatin, FLRG has higher affinity for activin than for BMP-2. The FLRG protein inhibited activin-induced and BMP-2-induced transcriptional responses in a dose-dependent manner. Glutathione S-transferase fusion proteins encoding various regions of FLRG were produced and studied. Ligand blotting using 125I-activin revealed that the COOH-terminal region containing the second follistatin domain was able to bind activin. Our finding implies that cellular signaling by activin and BMPs is tightly regulated by multiple members of the follistatin family.

* This work was supported by grants from the Ministry of Education, Science, Sports and Culture of Japan (to K. T. and H. S.) and by grants from the Takeda Science Foundation, Uehara Memorial Foundation, and the Inamori Foundation for Research (to K. T.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

This paper is dedicated to Kishiko Sugino.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF276238.

§ To whom correspondence should be addressed: Inst. for Enzyme Research, University of Tokushima, 3-18-15 Kuramoto, Tokushima 770-8503, Japan. Tel.: 81-88-633-7439; Fax: 81-88-633-7440; E-mail: tsuchida@ier.tokushima-u.ac.jp.

Present address: Dept. of Tissue Physiology, Faculty of Agriculture, Tokyo University of Agriculture and Technology, 3-5-8 Saiwai-cho, Fuchu, Tokyo 183-8509, Japan.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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