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 language | English |
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Journal | BBA General Subjects |
Volume | 1830 |
Issue | 3 |
Pages (from-to) | 2701-2709 |
Number of pages | 9 |
ISSN | 0304-4165 |
Publication status | Published - 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