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Folding of insulin-like growth factor I is thermodynamically controlled by insulin-like growth factor binding protein.
KTH, Superseded Departments, Biochemistry and Biotechnology.ORCID iD: 0000-0003-0605-8417
KTH, Superseded Departments, Biochemistry and Biotechnology.ORCID iD: 0000-0001-8993-048X
1994 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 33, no 22Article in journal (Refereed) Published
Abstract [en]

Insulin-like growth factor I (IGF-I) is thermodynamically unable to quantitatively form its native disulfides under reversible redox conditions in vitro [Hober et al. (1992) Biochemistry 31, 1749-1756]. These results prompted the question of how IGF-I may overcome this energetic problem in its folding in vivo. Here, we report that an IGF-I precursor, IGF-I-Ea, shows disulfide-exchange folding properties similar to those of mature IGF-I and, thus, is concluded not to overcome the identified folding problem of mature IGF-I. However, correct disulfide bonds are formed very efficiently when insulin-like growth factor binding protein 1 is added in equimolar amounts to IGF-I to the refolding mixture. On the basis of these results, we propose that one important function of at least one of the six homologous insulin-like growth factor binding proteins is to assist in the formation and maintenance of the native disulfides of IGF-I. To our knowledge, this is the first example where the folding of a mammalian protein or peptide in circulation has been demonstrated to be thermodynamically controlled by its binding protein. Speculatively, this could provide a mechanism to regulate the half-life of IGF-I in vivo by altering the interaction with insulin-like growth factor binding proteins.

Place, publisher, year, edition, pages
1994. Vol. 33, no 22
National Category
Biological Sciences Industrial Biotechnology
URN: urn:nbn:se:kth:diva-184213PubMedID: 7515683OAI: diva2:915604

NR 20160331

Available from: 2016-03-30 Created: 2016-03-30 Last updated: 2016-03-31Bibliographically approved

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