Isolation and characterization of proteolytic fragments of insulin-like growth factor-binding protein-3

Hormone Research
C LalouM Binoux

Abstract

Limited proteolysis of insulin-like growth factor-binding protein-3 (IGFBP-3) is a normal process in the regulation of insulin-like growth factor (IGF) activity, which we have reproduced in vitro using plasmin and recombinant human non-glycosylated IGFBP-3 in order to isolate and characterize the fragments obtained. Two major fragments of 22-25 and 16 kD were purified by RP-HPLC. The 22- to 25-kD fragment had severely reduced affinity for IGF-I, compared with intact IGFBP-3. It weakly inhibited cell proliferation stimulated by IGF-I and had no effect on insulin-induced stimulation. The 16-kD fragment, which had lost all affinity for IGFs, unexpectedly proved to be a potent inhibitor of both IGF-I-induced and insulin-induced cell growth. This proteolytic fragment of IGFBP-3 therefore exhibits intrinsic inhibitory activity.

Citations

May 5, 2004·Growth Hormone & IGF Research : Official Journal of the Growth Hormone Research Society and the International IGF Research Society·Sabine MazerbourgPhilippe Monget
Apr 26, 2003·Trends in Endocrinology and Metabolism : TEM·R Clay Bunn, John L Fowlkes
Feb 13, 2001·Growth Hormone & IGF Research : Official Journal of the Growth Hormone Research Society and the International IGF Research Society·M HouangY Le Bouc
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