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      Isolation and Characterization of Proteolytic Fragments of Insulin-Like Growth Factor-Binding Protein-3

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          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.

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          Author and article information

          Horm Res Paediatr
          Hormone Research in Paediatrics
          S. Karger AG
          09 December 2008
          : 45
          : 3-5
          : 156-159
          Institut National de la Santé et de la Recherche Médicale, Unité 142, Hôpital Saint-Antoine, Paris, France
          184779 Horm Res 1996;45:156–159
          © 1996 S. Karger AG, Basel

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          Page count
          Pages: 4
          Hormone Binding Proteins: Physiology and Clinical Implications


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