Rikke Søe - Academia.edu (original) (raw)
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Papers by Rikke Søe
European Journal of Biochemistry, 2002
Murine pregnancy‐associated plasma protein‐A (PAPP‐A) cDNA encoding a 1545 amino‐acid protein has... more Murine pregnancy‐associated plasma protein‐A (PAPP‐A) cDNA encoding a 1545 amino‐acid protein has been cloned. We have also identified and cloned cDNA that encodes a novel variant of PAPP‐A, PAPP‐Ai, carrying a 29‐residue highly basic insert. The point of insertion corresponds to a junction between two exons in the human PAPP‐A gene. The human intron flanked by these exons does not encode a homologous corresponding insert, which is unique to the mouse. The overall sequence identity between murine and human PAPP‐A is 91%, and murine PAPP‐A contains sequence motifs previously described in the sequence of human PAPP‐A. Through expression in mammalian cells, we show that murine PAPP‐A and PAPP‐Ai are active metalloproteinases, both capable of cleaving insulin‐like growth factor binding protein (IGFBP)‐4 and ‐5. Cleavage of IGFBP‐4 is dramatically enhanced by the addition of IGF, whereas cleavage of IGFBP‐5 is slightly inhibited by IGF, as previously established with human PAPP‐A. Surpri...
Biochimica et Biophysica Acta (BBA) - Biomembranes, 2009
European Journal of Biochemistry, 2002
Murine pregnancy‐associated plasma protein‐A (PAPP‐A) cDNA encoding a 1545 amino‐acid protein has... more Murine pregnancy‐associated plasma protein‐A (PAPP‐A) cDNA encoding a 1545 amino‐acid protein has been cloned. We have also identified and cloned cDNA that encodes a novel variant of PAPP‐A, PAPP‐Ai, carrying a 29‐residue highly basic insert. The point of insertion corresponds to a junction between two exons in the human PAPP‐A gene. The human intron flanked by these exons does not encode a homologous corresponding insert, which is unique to the mouse. The overall sequence identity between murine and human PAPP‐A is 91%, and murine PAPP‐A contains sequence motifs previously described in the sequence of human PAPP‐A. Through expression in mammalian cells, we show that murine PAPP‐A and PAPP‐Ai are active metalloproteinases, both capable of cleaving insulin‐like growth factor binding protein (IGFBP)‐4 and ‐5. Cleavage of IGFBP‐4 is dramatically enhanced by the addition of IGF, whereas cleavage of IGFBP‐5 is slightly inhibited by IGF, as previously established with human PAPP‐A. Surpri...
Biochimica et Biophysica Acta (BBA) - Biomembranes, 2009