| First Author | Kamimura M | Year | 2004 |
| Journal | Dev Dyn | Volume | 230 |
| Issue | 3 | Pages | 434-45 |
| PubMed ID | 15188429 | Mgi Jnum | J:91215 |
| Mgi Id | MGI:3046131 | Doi | 10.1002/dvdy.20069 |
| Citation | Kamimura M, et al. (2004) Vertebrate crossveinless 2 is secreted and acts as an extracellular modulator of the BMP signaling cascade. Dev Dyn 230(3):434-45 |
| abstractText | In vertebrates and invertebrates, BMP/Dpp (Bone Morphogenetic Protein/Decapentaplegic) signaling regulates the orchestrated processes of embryogenesis. Recent studies have revealed that BMP/Dpp signaling is controlled extracellularly as well as intracellularly. One extracellular regulatory molecule is the Chordin/Short gastrulation protein (Chordin/Sog), a secreted protein that acts as an antagonist to BMP/Dpp. Chordin/Sog contains four cysteine-rich (CR) domains that bind to and inactivate BMP/Dpp. In contrast, a positive regulator has been identified in Drosophila. Named crossveinless 2 (cv-2), this molecule contains five CR domains at the N-terminal half and a von Willebrand factor D domain at the C-terminal part. Genetic data suggest that Cv-2 potentiates Dpp signaling. We isolated chick and mouse CV-2 genes and found that CV-2 is secreted and enhances BMP signaling. Expression patterns were closely related to those of BMPs, supporting the likelihood of a tight link. Our data show for the first time that CV-2 is a conserved, positive regulator of BMP signaling and that CR domain proteins act as both positive and negative modulators of BMP signaling. |
