A central domain binding site in insulin-like growth factor binding protein-5 for the acid-labile subunit.

Abstract:

:Like insulin-like growth factor binding protein-3 (IGFBP-3), IGFBP-5 forms a ternary complex with insulin-like growth factor (IGF)-I or IGF-II, and the acid-labile subunit (ALS). The study of IGFBP-5/IGFBP-6 chimeric proteins with amino-terminal and middle domain swaps, has revealed the existence of a site in the middle domain of IGFBP-5, that binds to ALS in the absence of the IGFBP-5 carboxy-terminal domain. An IGFBP-6 chimeric protein containing the central domain of IGFBP-5 complexed efficiently with ALS, and a carboxy-terminally truncated IGFBP-5 mutant, IGFBP-5'(1-169), also bound to ALS in the presence of IGFs, although with much less potency than full length rhIGFBP-5. In contrast to the latter, IGFBP-5(1-169) preferentially formed ternary complexes with IGF-II rather than IGF-I. These results indicate that a site which binds ALS exists in IGFBP-5 mutants which lack the IGFBP-5 carboxy-terminal domain.

journal_name

Endocrinology

journal_title

Endocrinology

authors

Twigg SM,Kiefer MC,Zapf J,Baxter RC

doi

10.1210/endo.141.1.7375

subject

Has Abstract

pub_date

2000-01-01 00:00:00

pages

454-7

issue

1

eissn

0013-7227

issn

1945-7170

journal_volume

141

pub_type

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