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J Biol Chem, Vol. 273, Issue 11, 6074-6079, March 13, 1998
Kolling Institute of Medical Research, University of Sydney, Royal
North Shore Hospital, St. Leonards,
New South Wales 2065, Australia
Up to 90% of circulating insulin-like growth
factors (IGF-I and IGF-II) are carried in heterotrimeric complexes with
a binding protein (IGFBP) and a liver-derived glycoprotein known as
the acid-labile subunit. IGFBP-3 is considered unique among the six well characterized IGFBPs in its ability to complex with the
acid-labile subunit. However, a basic carboxyl-terminal domain of
IGFBP-3, known to be involved in its interaction with the acid-labile
subunit, is shared by IGFBP-5, suggesting the possibility of ternary
complexes containing IGFBP-5. We now demonstrate using three
independent methods that human IGFBP-5, when occupied by IGF-I or
IGF-II, forms ternary complexes of approximately 130 kDa with the
acid-labile subunit. IGFBP-3 competes with approximately twice the
potency of IGFBP-5 for the formation of such complexes. No other IGFBP complexes with the acid-labile subunit itself or competes with IGFBP-5
for complex formation. As observed for IGFBP-3, ternary complexes
containing IGFBP-5 form preferentially in the presence of IGF-I,
even though IGFBP-5 has a preferential affinity for IGF-II over
IGF-I. By size fractionation chromatography, serum IGFBP-5 co-elutes
predominantly with ternary complexes. The demonstration of
IGFBP-5-containing ternary complexes indicates an unrecognized form of
IGF transport in the circulation and an additional mechanism for
regulating IGF bioavailability.
Insulin-like Growth Factor (IGF)-binding Protein 5 Forms an
Alternative Ternary Complex with IGFs and the Acid-labile
Subunit
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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