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J Biol Chem, Vol. 273, Issue 44, 28791-28798, October 30, 1998
From the We have recently shown that insulin-like growth
factor (IGF)-binding protein 5 forms ternary complexes with IGF-I or
IGF-II and the acid-labile subunit (ALS) (Twigg, S. M., and
Baxter, R. C. (1998) J. Biol. Chem. 273, 6074-6079). Because IGF-binding protein 3 (IGFBP-3) binds to ALS
through its basic carboxyl-terminal domain, we tested whether a
homologous region present in IGFBP-5 is involved in IGFBP-5 binding to
ALS. Chimeric peptides were generated by carboxyl-terminal domain
interchange between recombinant human IGF-BP-5 and IGFBP-6,
producing two IGFBP peptides designated 5-5-6 and 6-6-5. Determined by
immunoprecipitation and by Superose chromatography, 6-6-5 formed
ternary complexes, albeit less potently than IGF-BP-5. In contrast,
5-5-6, like IGFBP-6, did not form ternary complexes by these methods.
Whereas 6-6-5, like IGFBP-6, had a marked preference for binary complex
formation with IGF-II rather than IGF-I, it formed ternary complexes
more efficiently with IGF-I, like IGF-BP-5. The glycosaminoglycans
heparin and heparan sulfate bind to IGFBP-5 through its basic
carboxyl-terminal domain. At high concentrations, these
glycosaminoglycans inhibited ALS binding to binary complexed
IGF-BP-5. In addition, in the absence of IGFs, IGFBP-5, a synthetic
peptide representing the basic carboxyl-terminal sequence
IGFBP-5(201-218), and the corresponding IGFBP-3 basic sequence
IGFBP-3(215-232), competed weakly for ALS binding to covalent
IGF-IGFBP-5 complex, as did a random-sequence synthetic peptide with
the same composition as IGFBP-5(201-218). These findings are
consistent with the basic carboxyl-terminal domain on IGFBP-5 being the
principal site in IGFBP-5 that binds to ALS.
Insulin-like Growth Factor-binding Protein 5 Complexes with the
Acid-labile Subunit
ROLE OF THE CARBOXYL-TERMINAL DOMAIN
,
Kolling Institute of Medical Research,
University of Sydney, Royal North Shore Hospital, St. Leonards,
New South Wales 2065, Australia, the § Chiron Corporation,
Emeryville, California 94608, and the ¶ Division of Endocrinology
and Metabolism, Internal Medicine, University Hospital, 8091 Zurich,
Switzerland
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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