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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

IGFBP-3 and IGFBP-5 association with endothelial cells: role of C-terminal heparin binding domain.

IGFBP-3 and IGFBP-5, but not the other 4 IGF binding proteins, specifically bound to endothelial cell (EC) monolayers. Charged compounds, such as heparin and heparan sulfate, competed for this binding. Of the 6 IGFBPs, IGFBP-3 and IGFBP-5 had the greatest heparin affinity. Peptides of 18 amino acids were synthesized, corresponding to a common basic region of IGFBP-3 (P3), IGFBP-5 and IGFBP-6 (P6) which contained a heparin binding sequence. P3 and P6 inhibited IGFBP-3 and -5 binding to endothelial cell monolayers and the peptides bound directly to EC extracellular matrix. This suggested that the C-terminal basic segment of IGFBP-3/-5 is important for the association of the binding protein with the EC monolayer.[1]

References

  1. IGFBP-3 and IGFBP-5 association with endothelial cells: role of C-terminal heparin binding domain. Booth, B.A., Boes, M., Andress, D.L., Dake, B.L., Kiefer, M.C., Maack, C., Linhardt, R.J., Bar, K., Caldwell, E.E., Weiler, J. Growth Regul. (1995) [Pubmed]
 
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