A novel inhibitor of the tyrosine kinase Src suppresses phosphorylation of its major cellular substrates and reduces bone resorption in vitro and in rodent models in vivo.

@article{Missbach1999ANI,
  title={A novel inhibitor of the tyrosine kinase Src suppresses phosphorylation of its major cellular substrates and reduces bone resorption in vitro and in rodent models in vivo.},
  author={Martin Missbach and Margit Jeschke and Jean H M Feyen and Klaus M{\"u}ller and Markus Glatt and Jonathan Green and Mira Susa},
  journal={Bone},
  year={1999},
  volume={24 5},
  pages={437-49}
}
The tyrosine kinase Src has been implicated in the process of osteoclast-mediated bone resorption. Here, we describe a novel class of Src inhibitors, substituted 5,7-diphenyl-pyrrolo[2,3-d]pyrimidines, and characterize one of them, CGP77675, in vitro and in models of bone resorption in vivo. In vitro, CGP77675 inhibited phosphorylation of peptide substrates and autophosphorylation of purified Src (concentration producing half-maximal inhibition [IC50] values 5-20 and 40 nmol/L, respectively… CONTINUE READING

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The tyrosine kinase Src has been implicated in the process of osteoclast - mediated bone resorption .
The tyrosine kinase Src has been implicated in the process of osteoclast - mediated bone resorption .
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