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Kolling Institute of Medical Research, University of Sydney, Royal North Shore Hospital, Sydney, New South Wales 2065, Australia
The insulin-like
growth factor (IGF)-binding proteins (IGFBPs) are a family of six
homologous proteins with high binding affinity for IGF-I and IGF-II.
Information from NMR and mutagenesis studies is advancing knowledge of
the key residues involved in these interactions. IGF binding may be
modulated by IGFBP modifications, such as phosphorylation and
proteolysis, and by cell or matrix association of the IGFBPs. All six
IGFBPs have been shown to inhibit IGF action, but stimulatory effects
have also been established for IGFBP-1, -3, and -5. These generally
involve a decrease in IGFBP affinity and may require cell association
of the IGFBP, but precise mechanisms are unknown. The same three IGFBPs
have well established effects that are independent of type I IGF
receptor signaling. IGFBP-1 exerts these effects by signaling through
5
1-integrin, whereas IGFBP-3 and -5 may have specific cell-surface receptors with serine kinase activity. The
regulation of cell sensitivity to inhibitory IGFBP signaling may play a
role in the growth control of malignant cells.
structural determinants; type I insulin-like growth factor receptor; cancer cell growth
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