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

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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.

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Journal ID (publisher-id): HRE

Journal ID (nlm-ta): Horm Res Paediatr

Journal ID (doi): 10.1159/issn.1663-2818

Title: Hormone Research in Paediatrics

Publisher: S. Karger AG

ISBN: 978-3-8055-6290-4

ISBN: 978-3-318-00047-4

ISSN (Print): 1663-2818

ISSN (Electronic): 1663-2826

Publication date Subscription-year: 1996

Publication date (Print): 1996

Publication date (Electronic): 09 December 2008

Volume: 45

Issue: 3-5

Pages: 156-159

Affiliations

Institut National de la Santé et de la Recherche Médicale, Unité 142, Hôpital Saint-Antoine, Paris, France

Article

Publisher ID: 184779 Other ID: Horm Res 1996;45:156–159

DOI: 10.1159/000184779

PubMed ID: 8964575

SO-VID: 25bb1ca3-7d5d-40e6-ab8c-3cc34b739640

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

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Karger: Endocrinology

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