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Insulin-like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions.
KTH, Superseded Departments, Biochemistry and Biotechnology.ORCID iD: 0000-0003-0605-8417
KTH, Superseded Departments, Biochemistry and Biotechnology.ORCID iD: 0000-0001-8993-048X
1999 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 443, no 3Article in journal (Refereed) Published
Abstract [en]

Insulin-like growth factor (IGF) I does not quantitatively form its three native disulfide bonds in the presence of 10 mM reduced and 1 mM oxidized glutathione in vitro [Hober, S. et al. (1992) Biochemistry 31, 1749-1756]. In this paper, we show (i) that both IGF-I and IGF-II are unable to form and maintain their native disulfide bonds at redox conditions that are similar to the situation in the secretory vesicles in vivo and (ii) that the presence of protein disulfide isomerase does not overcome this problem. The results indicate that the previously described thermodynamic disulfide exchange folding problem of IGF-I in vitro is also present in vivo. Speculatively, we suggest that the thermodynamic disulfide exchange properties of IGF-I and II are biologically significant for inactivation of the unbound growth factors by disulfide exchange reactions to generate variants destined for rapid clearance.

Place, publisher, year, edition, pages
1999. Vol. 443, no 3
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:kth:diva-184214PubMedID: 10025946OAI: oai:DiVA.org:kth-184214DiVA: diva2:915607
Note

NR 20160331

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

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