Interaction of insulin-like growth factor binding protein-3 with latent transforming growth factor-beta binding protein-1

  title={Interaction of insulin-like growth factor binding protein-3 with latent transforming growth factor-beta binding protein-1},
  author={Yaoting Gui and Liam J. Murphy},
  journal={Molecular and Cellular Biochemistry},
  • Y. Gui, L. Murphy
  • Published 1 August 2003
  • Biology
  • Molecular and Cellular Biochemistry
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… 
Ribonucleic acid polymerase II binding subunit 3 (Rpb3), a potential nuclear target of insulin-like growth factor binding protein-3.
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Insulin-like growth factor binding protein-3 is required for the regulation of rat oval cell proliferation and differentiation in the 2AAF/PHX model
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Perspectives in mammalian IGFBP-3 biology: local vs. systemic action.
The purpose of this review is to highlight IGFBP-3 as a novel effector molecule and not just another "binding protein" by discussing its IGF-independent actions on metabolism and cell growth.
Insulin-like growth factor-binding protein-3 promotes transforming growth factor-{beta}1-mediated epithelial-to-mesenchymal transition and motility in transformed human esophageal cells.
It is found that IGFBP3 facilitates transforming growth factor (TGF)-beta1-mediated epithelial-to-mesenchymal transition (EMT) in transformed human esophageal epithelial cells, EPC2-hTERT-EGFR-p53(R175H), and may have a novel IGF-binding independent biological function in regulation of TGF-beta 1-mediated EMT and cell invasion.
Signaling cross-talk between IGF-binding protein-3 and transforming growth factor-(beta) in mesenchymal chondroprogenitor cell growth.
Cross-talk between the IGFBP-3-dependent STAT-1 signaling and the TGF-beta-dependent ERK pathway that regulates MCC proliferation is demonstrated.
IGFBP-3/IGFBP-3 Receptor System as an Anti-Tumor and Anti-Metastatic Signaling in Cancer
This review delineates the potential underlying mechanisms involved and the subsequent biological significance, emphasizing the clinical significance of the IGFBP-3/TMEM219 axis in assessing both the diagnosis and the prognosis of cancer as well as the therapeutic potential of TMEM219 agonists for cancer treatment.
Latent TGF-β-binding proteins.
Interactions between IGFBP-3 and Nuclear Receptors in Prostate Cancer Apoptosis
It is shown that IGFBP-3's critical role in castration-induced apoptosis is shown and the protein regions in each of these important cell death molecules that essential for apoptotic action are determined.
Myocardial insulin-like growth factor-1 and insulin-like growth factor binding protein-3 gene expression in failing hearts harvested from patients undergoing cardiac transplantation.
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  • Medicine, Biology
    The Journal of heart and lung transplantation : the official publication of the International Society for Heart Transplantation
  • 2009


The Type V Transforming Growth Factor β Receptor Is the Putative Insulin-like Growth Factor-binding Protein 3 Receptor*
It is shown that recombinant human IGFBP-3 inhibits125I-transforming growth factor (TGF)-β1 binding to the type V TGF-β receptor in mink lung epithelial cells and indicates that IGF BP-3 is a functional ligand for thetype V T GF- β receptor.
Insulin-like growth factor (IGF)-binding protein-3 (IGFBP-3) binds to fibronectin (FN): demonstration of IGF-I/IGFBP-3/fn ternary complexes in human plasma.
  • Y. Gui, L. Murphy
  • Biology, Medicine
    The Journal of clinical endocrinology and metabolism
  • 2001
Data indicate that FN may have a role in the transportation of IGFBP-3 and IGF-I in the circulation and the sequestration of these proteins in tissues.
Direct Functional Interactions between Insulin-like Growth Factor-binding Protein-3 and Retinoid X Receptor-α Regulate Transcriptional Signaling and Apoptosis*
RXR- α-IGFBP-3 interaction leads to modulation of the transcriptional activity of RXR-α and is essential for mediating the effects of IGFBP- 3 on apoptosis.
Transforming growth factor-beta stimulates production of insulin-like growth factor-binding protein-3 by human skin fibroblasts.
It is reported that transforming growth factor-beta (TGF beta) is a potent stimulator of IGFBP-3 production by fibroblasts, raising the possibility that TGF beta may modulate IGF actions in these cells by stimulating the production of IGF BP-3.
Transferrin is an insulin-like growth factor-binding protein-3 binding protein.
A combination of techniques are employed to demonstrate that Tf specifically binds IGFBP-3, and it is shown that this interaction has important physiological effects on cellular events.
The 16-kDa proteolytic fragment of insulin-like growth factor (IGF) binding protein-3 inhibits the mitogenic action of fibroblast growth factor on mouse fibroblasts with a targeted disruption of the type 1 IGF receptor gene.
The 16-kDa proteolytic fragment of IGF Binding Protein-3 (IGFBP-3) appears to be a potent inhibitor of mitogenic signals resulting from activation of both the type 1 IGF and FGF receptors.
Insulin-like Growth Factor (IGF)-binding Protein-3 Induces Apoptosis and Mediates the Effects of Transforming Growth Factor-β1 on Programmed Cell Death through a p53- and IGF-independent Mechanism*
It is suggested that IGFBP-3 induces apoptosis through a novel pathway independent of either p53 or the IGF·IGF receptor-mediated cell survival pathway and that IGF BP-3 mediates TGF-β1 induced apoptosis in PC-3 cells.
A proteolytic fragment of insulin-like growth factor (IGF) binding protein-3 that fails to bind IGFs inhibits the mitogenic effects of IGF-I and insulin.
Limited proteolysis of insulin-like growth factor binding protein-3 (IGFBP-3) is increasingly becoming recognized as an essential mechanism in the regulation of insulin-like growth factor (IGF)
Interactions of recombinant and platelet transforming growth factor-beta 1 precursor with the insulin-like growth factor II/mannose 6-phosphate receptor.
Characterization of insulin-like growth factor binding protein-3 (IGFBP-3) binding to human breast cancer cells: kinetics of IGFBP-3 binding and identification of receptor binding domain on the IGFBP-3 molecule.
It is demonstrated that specific, high-affinity IGFBP-3 receptors are located on breast cancer cell membranes, and these receptors have properties that support the notion that they may mediate the IGF-independent inhibitory actions of IGF BP-3 in breast cancer cells.