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(Received for publication, July 30, 1997, and in revised form, September 19, 1997)
From the Department of Pediatrics, School of Medicine, Oregon
Health Sciences University, Portland, Oregon 97201
The insulin-like growth factors (IGFs) are
transported by a family of high-affinity binding proteins (IGFBPs) that
protect IGFs from degradation, limit their binding to IGF receptors,
and modulate IGF actions. The six classical IGFBPs have been believed to have no affinity for insulin. We now demonstrate that IGFBP-7/mac25, a newly identified member of the IGFBP superfamily that binds IGFs
specifically with low affinity is a high-affinity insulin binding
protein. IGFBP-7 blocks insulin binding to the insulin receptor and
thereby inhibiting the earliest steps in insulin action, such as
autophosphorylation of the insulin receptor
Volume 272, Number 49,
Issue of December 5, 1997
pp. 30729-30734
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Inhibition of Insulin Receptor Activation by Insulin-like Growth
Factor Binding Proteins
subunit and
phosphorylation of IRS-1, indicating that IGFBP-7 is a functional
insulin-binding protein. The affinity of other IGFBPs for insulin can
be enhanced by modifications that disrupt disulfide bonds or remove the
conserved COOH terminus. Like IGFBP-7, an
NH2-terminal fragment of IGFBP-3
(IGFBP-3(1-87)), also binds insulin with high affinity and
blocks insulin action. IGFBPs with enhanced affinity for insulin might
contribute to the insulin resistance of pregnancy, type II diabetes
mellitus, and other pathological conditions.
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