ZFIN ID: ZDB-PUB-070711-2
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.
Date: 2007
Source: The Journal of biological chemistry   282(12): 9053-9062 (Journal)
Registered Authors: Lyman-Gingerich, Jamie, Pelegri, Francisco, Voss, Nik
Keywords: none
MeSH Terms:
  • Animals
  • Bone Morphogenetic Protein 1
  • Bone Morphogenetic Protein 2
  • Bone Morphogenetic Protein 4
  • Bone Morphogenetic Proteins/chemistry*
  • Cell Membrane/metabolism
  • Humans
  • Kinetics
  • Metalloendopeptidases/chemistry*
  • Nucleic Acid Hybridization
  • Osteoblasts/metabolism
  • Phenotype
  • Protein Binding
  • Protein Structure, Tertiary
  • Signal Transduction
  • Surface Plasmon Resonance
  • Transforming Growth Factor beta/chemistry*
  • Zebrafish
  • Zebrafish Proteins
PubMed: 17255107 Full text @ J. Biol. Chem.
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.