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

Ervinas Gaidamauskas, Claus Gyrup Nielsen, Henning Bünsow Boldt, Vivien R Schack, Michael Toft Overgaard, Lisbeth S Laursen, Claus Oxvig

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22 Citations (Scopus)

Abstract

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

Keywords

  • 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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