11010 250 250 1 2 Yaoting Gui Liam J. Murphy ljmurph@cc.umanitoba.ca Department of Physiology University of Manitoba Winnipeg Canada Departments of Physiology and Internal Medicine University of Manitoba Winnipeg R3E 0W3 Canada Abstract Insulin-like growth factor binding protein-3 (IGFBP-3) inhibits the replication and promotes apoptosis in various cell lines in an IGF-independent manner. We utilized a yeast two-hybrid system to identify binding partners for IGFBP-3 in a mouse embryo cDNA library. A partial cDNA encoding mouse latent transforming growth factor beta (TGF-β) binding protein-1 (LTBP-1) was identified. This cDNA encoded a mouse LTBP-1 mRNA fragment corresponding to amino acid residues 1160–1712. Analysis of C-terminal deleted mutants indicated that the IGFBP-3 interacting domain resides in the 552 residue C-terminal fragment encoding amino acids 831–1383. The interaction of IGFBP-3 with recombinant human LTBP-1 immobilized on nitrocellulose was also demonstrated. Neither binding of IGF-I to IGFBP-3 nor binding of latency associated protein (LAP) with LTBP-1 inhibited the interaction of IGFBP-3 with LTBP-1. Furthermore the large latent complex, 125 I-TGF-β/LAP/LTBP-1 was able to bind to immobilized IGFBP-3. These data demonstrate that IGFBP-3 can bind to LTBP-1 and provide a potential mechanism whereby IGFBP-3 can interact with the TGF-β system.
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Interaction of insulin-like growth factor binding protein-3 with latent transforming growth factor-beta binding protein-1
Yaoting, Gui; Liam, Murphy
Follow Molecular and Cellular Biochemistry
, Volume 250 (1)
Springer Journals – Aug 1, 2003
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