Editors' ChoiceProteomics

Signaling Bone Formation

See allHide authors and affiliations

Science's STKE  07 Jun 2005:
Vol. 2005, Issue 287, pp. tw212
DOI: 10.1126/stke.2872005tw212

Improvements in mass spectrometry now allow global quantitation of phosphorylated proteins from cultured cells and comparison of signaling networks. Kratchmarova et al. immunoprecipitated tyrosine phosphorylated proteins (and associated proteins) and determined the relative abundance of peptides in the mixture to characterize the spectrum of signals initiated by two related receptor tyrosine kinases--the epidermal growth factor (EGF) receptor and the platelet-derived growth factor (PDGF) receptor. Human mesenchymal stem cells were induced to differentiate into bone-forming cells by EGF but not by PDGF, and comparison of the two signaling networks revealed that the PDGF activated the phosphatidylinositol 3-kinase (PI3K) pathway, whereas EGF did not. When the PI3K pathway was inhibited, PDGF could promote bone differentiation as effectively as EGF.

I. Kratchmarova, B. Blagoev, M. Haack-Sorensen, M. Kassem, M. Mann, Mechanism of divergent growth factor effects in mesenchymal stem cell differentiation. Science 308, 1472-1477 (2005). [Abstract] [Full Text]

Stay Connected to Science Signaling