Bone morphogenetic protein 1 prodomain specifically binds and regulates signaling by bone morphogenetic proteins 2 and 4
- Jasuja, R., Ge, G., Voss, N.G., Lyman-Gingerich, J., Branam, A.M., Pelegri, F.J., and Greenspan, D.S.
- The Journal of biological chemistry 282(12): 9053-9062 (Journal)
- Registered Authors
- Lyman-Gingerich, Jamie, Pelegri, Francisco, Voss, Nik
- MeSH Terms
- Bone Morphogenetic Protein 1
- Bone Morphogenetic Protein 2
- Bone Morphogenetic Protein 4
- Bone Morphogenetic Proteins/chemistry*
- Cell Membrane/metabolism
- Nucleic Acid Hybridization
- Protein Binding
- Protein Structure, Tertiary
- Signal Transduction
- Surface Plasmon Resonance
- Transforming Growth Factor beta/chemistry*
- Zebrafish Proteins
- 17255107 Full text @ J. Biol. Chem.
Jasuja, R., Ge, G., Voss, N.G., Lyman-Gingerich, J., Branam, A.M., Pelegri, F.J., and Greenspan, D.S. (2007) Bone morphogenetic protein 1 prodomain specifically binds and regulates signaling by bone morphogenetic proteins 2 and 4. The Journal of biological chemistry. 282(12):9053-9062.
Highly purified fractions of bone extracts capable of inducing ectopic bone formation have been reported to contain peptides corresponding to the mature active regions of the TGF-beta-like bone morphogenetic proteins (BMPs) 2-7, and to the prodomain region of the metalloproteinase BMP1. Co-purification of BMPs 2-7 with BMP1 prodomain sequences through the multiple biochemical steps used in these previous reports has suggested the possibility of interactions between the BMP1 prodomain and BMPs 2-7. Here we demonstrate that the BMP1 prodomain binds BMPs 2 and 4 with high specificity and with a KD of approximately 11 nM, in the physiological range. It is further demonstrated that the BMP1 prodomain is capable of modulating signaling by BMPs 2 and 4 in vitro and in vivo, and that endogenous BMP1 prodomain-BMP4 complexes exist in cell culture media and in tissues.
Genes / Markers
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Engineered Foreign Genes