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- W2025366890 abstract "Insulin-like growth factors (IGF-I and -II) bind with high affinity to IGF-binding proteins (IGFBPs). IGFBP-3 contains vicinal cysteines in a sequence which is similar to the active sites in thioredoxin and protein disulfide isomerase. We tested if, in analogy with these redox enzymes, IGFBP-3 could catalyze the isomerization of intramolecular disulfide bridges in protein substrates. IGFBP-3 (30 μM) was able to reactivate reduced ribonuclease at a rate of 38% of that of thioredoxin. Also recombinant IGF-I induced the regeneration of ribonuclease activity. Thiol redox reactions are known to play a role in regulating conformational changes in the insulin receptor and possibly also in the IGF-I receptor. Therefore, the intrinsic isomerase activities of IGF-I may be important in the activation of its receptor. The observed effects of IGFBP-3 may help to elucidate the mechanism by which this binding protein can modulate the actions of IGF-I." @default.
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- W2025366890 date "1994-02-01" @default.
- W2025366890 modified "2023-09-26" @default.
- W2025366890 title "Insulin-like Growth Factors (IGFs) and IGF Binding Protein 3 Display Disulfide Isomerase Activity" @default.
- W2025366890 doi "https://doi.org/10.1006/bbrc.1994.1173" @default.
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