| First Author | Tsuchida K | Year | 2000 |
| Journal | J Biol Chem | Volume | 275 |
| Issue | 52 | Pages | 40788-96 |
| PubMed ID | 11010968 | Mgi Jnum | J:66713 |
| Mgi Id | MGI:1929020 | Doi | 10.1074/jbc.M006114200 |
| Citation | Tsuchida K, et al. (2000) Identification and characterization of a novel follistatin-like protein as a binding protein for the TGF-beta family. J Biol Chem 275(52):40788-96 |
| abstractText | 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 (125)I-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. |
