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Claus Oxvig

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

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  • Ervinas Gaidamauskas, Denmark
  • Claus Gyrup Nielsen
  • ,
  • Henning Bünsow Boldt, Denmark
  • Vivien R Schack
  • Michael Toft Overgaard, Institut for Kemi og Bioteknologi, Denmark
  • Lisbeth S Laursen, Denmark
  • Claus Oxvig
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 and IGFBP-5.
Original languageEnglish
JournalBBA General Subjects
Volume1830
Issue3
Pages (from-to)2701-2709
Number of pages9
ISSN0304-4165
Publication statusPublished - Mar 2013

    Research areas

  • Amino Acid Sequence, Binding Sites, Female, HEK293 Cells, Humans, Insulin-Like Growth Factor Binding Protein 3, Insulin-Like Growth Factor Binding Protein 5, Models, Molecular, Molecular Sequence Data, Pregnancy, Pregnancy-Associated Plasma Protein-A, Protein Binding, Protein Interaction Domains and Motifs, Proteolysis, Recombinant Fusion Proteins, Somatomedins, Substrate Specificity, Transfection

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