Key result
Exposure of IGFBP-3 to plasmin, thrombin, and serum generated multiple proteolytic fragments with differential affinities for IGF and heparin.
Population
Insulin-like growth factor binding protein (IGFBP)-3 (in vitro model)
Design
Preclinical
Authors
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May influence vascular IGF bioavailability experimentally; leaves open effects on endothelial function in vivo.
Proteolysis of IGFBP-3 by endothelial surface substances generates fragments with varying affinities for IGF and heparin, which may influence vascular IGF concentrations and endothelial function.
Booth et al. (1996) studied this question. Plasmin, thrombin, and pregnancy serum was evaluated on Proteolytic fragmentation of IGFBP-3 and binding ability to IGF and heparin. Exposure of IGFBP-3 to plasmin, thrombin, and serum generated multiple proteolytic fragments with differential affinities for IGF and heparin.
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