IGF dependent modulation of IGF binding protein (IGFBP) proteolysis by pregnancy-associated plasma protein-A (PAPP-A): multiple PAPP-A-IGFBP interaction sites.

@article{Gaidamauskas2013IGFDM,
  title={IGF dependent modulation of IGF binding protein (IGFBP) proteolysis by pregnancy-associated plasma protein-A (PAPP-A): multiple PAPP-A-IGFBP interaction sites.},
  author={Ervinas Gaidamauskas and Claus Gyrup and Henning B{\"u}nsow Boldt and Vivien Rodacker Schack and Michael Toft Overgaard and Lisbeth S Laursen and Claus Oxvig},
  journal={Biochimica et biophysica acta},
  year={2013},
  volume={1830 3},
  pages={2701-9}
}
BACKGROUND Pregnancy-associated plasma protein-A (PAPP-A) is a local regulator of insulin-like growth factor (IGF) bioavailability in physiological systems, but many structural and functional aspects of the metzincin metalloproteinase remain to be elucidated. PAPP-A cleaves IGF binding protein (IGFBP)-4 and IGFBP-5. Cleavage of IGFBP-4, but not IGFBP-5, depends on the binding of IGF before proteolysis by PAPP-A can occur. The paralogue PAPP-A2 has two substrates among the six IGFBPs: IGFBP-3… CONTINUE READING