Involvement of pregnancy-associated plasma protein-A2 in insulin-like growth factor (IGF) binding protein-5 proteolysis during pregnancy: a potential mechanism for increasing IGF bioavailability

The Journal of Clinical Endocrinology and Metabolism
Xiaolang YanSue M Firth

Abstract

During pregnancy, circulating IGF binding protein-5 (IGFBP-5) undergoes substantial molecular redistribution from ternary complexes to either binary complexes or the uncomplexed protein. This study aimed to characterize the proteolysis of circulating IGFBP-5 during pregnancy and to determine whether it can increase IGF bioavailability. Biochemical methods were used to purify and characterize IGFBP-5 fragments and IGFBP-5-specific proteolytic activity from pregnancy plasma. Circulating IGFBP-5 was fully proteolyzed at all stages of pregnancy. Cleavage after either Ser143 or Lys144 resulted in two complementary fragments. Of two pools of proteolytic activity (>150 kDa and approximately 40 kDa) identified in pregnancy plasma, only the greater than 150-kDa proteolytic activity was specific to pregnancy. The approximately 40-kDa proteolytic activity, also present in nonpregnancy plasma, appeared largely inactive against IGF-I-complexed IGFBP-5. The greater than 150-kDa proteolytic activity was inhibited by alpha-PAPP-A2 but not alpha-PAPP-A1 antibody, cleaved recombinant IGFBP-5 at Ser143-Lys144 similar to PAPP-A2, and was inactive against IGFBP-5 (Ala128), a PAPP-A2-resistant analog. Compared to nonpregnancy plasma, incubation with...Continue Reading

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Citations

Apr 12, 2012·Proceedings of the National Academy of Sciences of the United States of America·Geneviève Oligny-LongpréMichel Bouvier
Jul 21, 2010·Reproductive Biology and Endocrinology : RB&E·Pamela K Wagner, Julian K Christians
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Jan 27, 2015·Journal of Cell Communication and Signaling·Claus Oxvig
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