The Type V Transforming Growth Factor β Receptor Is the Putative Insulin-like Growth Factor-binding Protein 3 Receptor*

  title={The Type V Transforming Growth Factor $\beta$ Receptor Is the Putative Insulin-like Growth Factor-binding Protein 3 Receptor*},
  author={Sandra M Leal and Qianjin Liu and Shuan Shian Huang and Jung San Huang},
  journal={The Journal of Biological Chemistry},
  pages={20572 - 20576}
Insulin-like growth factor-binding protein 3 (IGFBP-3) has been shown to inhibit cell growth by IGF-dependent and -independent mechanisms. The putative cell-surface IGFBP-3 receptor that mediates the IGF-independent growth inhibition has not been identified. Here we show that recombinant human IGFBP-3 inhibits125I-transforming growth factor (TGF)-β1 binding to the type V TGF-β receptor (M r 400,000) in mink lung epithelial cells. We also demonstrate that the ∼400-kDa125I-IGFBP-3 affinity… 

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Interactions of High Affinity Insulin-like Growth Factor-binding Proteins with the Type V Transforming Growth Factor-β Receptor in Mink Lung Epithelial Cells*
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Insulin-like growth factor-binding protein-3 has intrinsic activity capable of inhibiting or enhancing the growth and survival of breast epithelial cells depending on the cell line and exposure to other cytokines.
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.
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IGFBP-3 mediates TGF-beta1-induced cell growth in human airway smooth muscle cells.
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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.
Insulin-like growth factor binding protein-3 in extracellular matrix stimulates adhesion of breast epithelial cells and activation of p44/42 mitogen-activated protein kinase.
IGF-binding protein-3 binds to ECM deposited by human breast epithelial and cancer cells and neonatal human fibroblasts, indicating a previously unrecognized and potentially important role for IGFBP-3 in the extracellular matrix.
Oncogenic ras Causes Resistance to the Growth Inhibitor Insulin-like Growth Factor Binding Protein-3 (IGFBP-3) in Breast Cancer Cells*
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A unique receptor-independent mechanism by which insulinlike growth factor I regulates the availability of insulinlike growth factor binding proteins in normal and transformed human fibroblasts.
  • C. Conover
  • Biology, Medicine
    The Journal of clinical investigation
  • 1991
In conclusion, IGF-I regulates the availability of specific IGFBPs in cultured human fibroblasts by a novel receptor-independent mechanism and may constitute an important level of control in IGF cellular physiology.
Function of the Type V Transforming Growth Factor β Receptor in Transforming Growth Factor β-induced Growth Inhibition of Mink Lung Epithelial Cells*
TGF-β stimulation resulted in the growth inhibition of wild-type mink lung epithelial cells and to a lesser extent of the type I and type II T GF-β receptor-defective mutants, although higher concentrations of TGF- β were required for thegrowth inhibition of these mutants.
Insulin-like Growth Factor Binding Protein 3 Mediates Retinoic Acid- and Transforming Growth Factor β2-induced Growth Inhibition in Human Breast Cancer Cells
Evidence is provided that IGFBP-3 is an important mediator of RA-and TGF-β2-induced cell growth inhibition in human breast cancer cells, and an antisense IGF BP-3 oligodeoxynucleotide (ODN) which specifically inhibits IGFBP -3 expression is used to test this hypothesis.
Transforming Growth Factor- β-induced Cell Growth Inhibition in Human Breast Cancer Cells Is Mediated through Insulin-like Growth Factor-binding Protein-3 Action (*)
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Insulin‐like growth factor binding protein (IGFBP‐3), an inhibitor of serum growth factors other than IGF‐I and ‐II
Rat IGFBP‐3 and IDF45 (an inhibitory diffusible factor secreted by mouse cells) had the same activities, confirming that they have an intrinsic capacity to inhibit serum stimulation and may be considered as growth inhibitors.
Distinct transforming growth factor-beta (TGF-beta) receptor subsets as determinants of cellular responsiveness to three TGF-beta isoforms.
Evaluated TGF-beta receptors indicate that a subset of receptors I and II has been identified in Mv1Lu cells which has high affinity for T GF-beta 2 (KD approximately 10 pM) and binds this factor at concentrations that are biologically active in M v1 Lu cells.