Protease-resistant insulin-like growth factor (IGF)-binding protein-4 inhibits IGF-I actions and neointimal expansion in a porcine model of neointimal hyperplasia.

@article{Nichols2007ProteaseresistantIG,
  title={Protease-resistant insulin-like growth factor (IGF)-binding protein-4 inhibits IGF-I actions and neointimal expansion in a porcine model of neointimal hyperplasia.},
  author={Timothy C. Nichols and Walker H. Busby and Elizabeth P. Merricks and Jennifer Sipos and Michael Rowland and Kevin R. Sitko and David R Clemmons},
  journal={Endocrinology},
  year={2007},
  volume={148 10},
  pages={
          5002-10
        }
}
IGF-I has been shown to play a role in the progression of atherosclerosis in experimental animal models. IGF-binding protein-4 (IGFBP-4) binds to IGF-I and prevents its association with receptors. Overexpression of a protease-resistant form of IGFBP-4 has been shown to inhibit the ability of IGF-I to stimulate normal smooth muscle cell growth in mice. Based on these observations, we prepared a protease-resistant form of IGFBP-4 and infused it into hypercholesterolemic pigs. Infusion of the… 
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Expression of a protease-resistant insulin-like growth factor-binding protein-4 inhibits tumour growth in a murine model of breast cancer
TLDR
Protease-resistant IGFBP4 blocks IGF activity, tumour growth and angiogenesis, and was accompanied by the increased endothelial cell apoptosis.
Insulin-like growth factor (IGF) binding protein-4 is both a positive and negative regulator of IGF activity in vivo.
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Results indicate not only that IGFBP-4 functions as a local reservoir to optimize IGF-II actions needed for normal embryogenesis, but also establish that IGF BP-4 proteolysis is required to activate most, if not all, IGF- II mediated growth-promoting activity.
Recombinant PAPPA resistant insulin-like growth factor binding protein 4 ( dBP 4 ) inhibits angiogenesis and metastasis in a murine model of breast cancer
TLDR
DBP4 inhibited IGF1induced angiogenesis in vitro and in Matrigel implants in vivo, and highlights the therapeutic potential of dBP4 as an approach to block the tumour-promoting actions of IGF1.
Recombinant PAPP-A resistant insulin-like growth factor binding protein 4 (dBP4) inhibits angiogenesis and metastasis in a murine model of breast cancer
TLDR
The engineered, PAPP-A resistant IGFBP4 (dBP4) retained IGF1 binding capacity and inhibited IGF1 activation of Akt as well as IGF1-induced migration and invasion by 4T1.2luc cells, highlighting the therapeutic potential of dBP4 as an approach to block the tumour-promoting actions of IGF1.
IGF binding protein-4 is required for the growth effects of glucagon-like peptide-2 in murine intestine.
TLDR
Results indicate that the IGF-I-modulating protein, IGFBP-4, exerts a negative effect on basal intestinal growth but plays a positive regulatory role in the intestinotropic actions of GLP-2.
The role of insulin-like growth factor (IGF) binding protein-2 in the insulin-mediated decrease in IGF-I bioactivity.
TLDR
The data indicate that insulin acutely decreases IGF-I bioactivity through differential modulation of IGFBPs, thereby providing a further explanation for its association with the metabolic syndrome.
Smooth Muscle Cell-Specific Insulin-Like Growth Factor-1 Overexpression in Apoe−/− Mice Does Not Alter Atherosclerotic Plaque Burden but Increases Features of Plaque Stability
TLDR
Findings indicate that stimulation of VSMC IGF-1 signaling does not alter total atherosclerotic plaque burden and may improve atherosclerosis plaque stability.
IGF-I increases markers of osteoblastic activity and reduces bone resorption via osteoprotegerin and RANK-ligand
TLDR
This work confirms that the simple partial IGF-I deficiency is responsible for osteopenia, determined by densitometry and histopathology, and identifies a reduced gene expression of osteoprotegerin, sclerostin, calcitonin receptor, insulin-like growth factor binding protein 5 and RUNX2.
Insulin-Like Growth Factor Signaling during Myogenesis.
TLDR
It is suggested that IGFBP-5 promotes muscle cell differentiation by binding to and switching on the IGF-II auto-regulation loop.
IGF-Binding Proteins: Why Do They Exist and Why Are There So Many?
TLDR
The emerging explanation that many IGFBP functions have evolved to allow the targeted adjustment of IGF signaling under stressful or irregular conditions, which would likely not be revealed in a standard laboratory setting are explored.
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References

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TLDR
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TLDR
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Insulin-like growth factor I (IGF-I) has been postulated to function as a smooth muscle cell (SMC) mitogen and to play a role in the pathogenesis of bladder hypertrophy, estrogen-induced uterine…
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TLDR
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