Regulation of IGFBP-4 levels in human intestinal muscle by an IGF-I-activated, confluence-dependent protease.

@article{Kuemmerle2000RegulationOI,
  title={Regulation of IGFBP-4 levels in human intestinal muscle by an IGF-I-activated, confluence-dependent protease.},
  author={John F Kuemmerle and B Q Teng},
  journal={American journal of physiology. Gastrointestinal and liver physiology},
  year={2000},
  volume={279 5},
  pages={
          G975-82
        }
}
  • J. Kuemmerle, B. Teng
  • Published 1 November 2000
  • Biology, Medicine
  • American journal of physiology. Gastrointestinal and liver physiology
Human intestinal smooth muscle cells in culture produce insulin-like growth factor-I (IGF-I), IGF binding protein-3 (IGFBP-3), IGFBP-4, and IGFBP-5, which can modulate the effects of IGF-I on growth. This study examined the role of IGFBP-4 on IGF-I-induced growth and the mechanisms regulating IGFBP-4 levels. IGFBP-4 inhibited IGF-I-induced [(3)H]thymidine incorporation. IGFBP-4 mRNA levels were not altered by IGF-I. IGF-I caused a concentration-dependent activation of an endogenous IGFBP-4… 
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  • J. Kuemmerle
  • Biology, Medicine
    American journal of physiology. Gastrointestinal and liver physiology
  • 2005
TLDR
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The current knowledge about the link between IGFs and colon cancer is mainly based on in vitro investigations, and further in vivo study is needed to understand the exact role of the IGF system, especially its binding proteins, so that they can be manipulated for the prevention and treatment of colorectal cancer.
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TLDR
The available data regarding the following aspects of IGFBP-4 are summarized: genomic organization, protein structure-function relationship, expression and its regulation, as well as IGF-dependent and -independent actions.
IGF-I elicits growth of human intestinal smooth muscle cells by activation of PI3K, PDK-1, and p70S6 kinase.
  • J. Kuemmerle
  • Biology, Computer Science
    American journal of physiology. Gastrointestinal and liver physiology
  • 2003
TLDR
Transfection of muscle cells with kinase-inactive Akt1(K179M) showed that these events were not required for IGF-I to activate p70S6 kinase and stimulate proliferation of human intestinal muscle cells.
Blunted satellite cell response is associated with dysregulated IGF-1 expression after exercise with age
TLDR
The greater muscle-specific expression of IGF-1 family members with a blunted post-exercise SC expression may be a compensatory attempt to rescue age-related anabolic resistance.
Insulin-like growth factors in the gastrointestinal tract and liver.
  • J. Kuemmerle
  • Medicine, Biology
    Endocrinology and metabolism clinics of North America
  • 2012
The insulin-like growth factor system and colorectal cancer: clinical and experimental evidence
ObjectiveThe aim of this review is to clarify the involvement of the insulinlike growth factor (IGF) system in the development of colorectal malignancy.Materials and methodsMedline searches were used
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Endogenous IGF-I regulates IGF binding protein production in human intestinal smooth muscle cells.
  • J. Kuemmerle
  • Biology, Medicine
    American journal of physiology. Gastrointestinal and liver physiology
  • 2000
TLDR
Ex vivo regulation of IGFBP production by endogenous IGF-I is mediated by activation of distinct MAP kinase and PI 3-kinase pathways, the same pathways through which IGF- I stimulates growth.
Differential Expression and Biological Effects of Insulin-like Growth Factor-binding Protein-4 and -5 in Vascular Smooth Muscle Cells*
TLDR
IGBP-4 and IGFBP-5 appear to be differentially regulated by autocrine/paracrine IGF-I through distinct mechanisms, and these two proteins play opposing roles in modulating IGF- I action in stimulating VSMC proliferation.
Insulin-like growth factor-I (IGF-I) regulates IGFBP-3 and IGFBP-4 by multiple mechanisms in A549 human adenocarcinoma cells.
TLDR
The production and regulation of IGFBPs from A549 cells, a human adenocarcinoma-derived lung cell line, is examined to examine the role of IGF binding proteins (IGFBPs) in modulating IGF actions in lung and suggests that IGFBP-3 is post-transcriptionally regulated.
Expression and insulin-like growth factor-dependent proteolysis of insulin-like growth factor-binding protein-4 are regulated by cell confluence in vascular smooth muscle cells.
TLDR
In summary, SMCs elaborate a cation-dependent protease in a confluence-dependent fashion, which degrades bound IGFBP-4 and likely releases free structurally intact IGF-I, presumably to interact with the cell surface receptor and/or other IGFBPs.
Glucocorticoid regulation of an insulin-like growth factor-binding protein-4 protease produced by a rat neuronal cell line.
TLDR
Data indicate that B104 cells produce an IGFBP-4 protease that is regulated by glucocorticoids, and the actions of this protease reduce the affinity of IGF BP-4 for the IGFs without abolishing binding.
Studies on the Mechanisms by Which Insulin-like Growth Factor (IGF) Binding Protein-4 (IGFBP-4) and IGFBP-5 Modulate IGF Actions in Bone Cells (*)
TLDR
IGBP-5 may in part stimulate bone cell proliferation by an IGF-independent mechanism involving IGF BP-5-specific cell surface binding sites independent of IGF receptors, according to studies on the mechanism by which IGFBP- 5 increased the binding of I-IGF tracer to bone cells.
Regulation of insulin-like growth factor (IGF)-binding protein-4 availability in normal human osteoblast-like cells: role of endogenous IGFs.
TLDR
Levels of endogenous IGF peptide may determine IGFBP-4 availability in the bone microenvironment and, thus, modulate the local cell response to IGF-I and contribute to enhanced proteolysis of endogenous and exogenous IGFBP4 via a proteinase secreted by cultured hOB cells.
Insulin-like Growth Factor (IGF)-binding Protein-3 (IGFBP-3) Functions as an IGF-reversible Inhibitor of IGFBP-4 Proteolysis (*)
TLDR
It is demonstrated that rhIGFBP-3 inhibits IGFBP-4-degrading proteinase activity and binding of IGFs or glycosaminoglycans to IGF BP-3 may induce conformational changes in the binding protein, causing disinhibition of the proteinase.
Properties of an insulin-like growth factor-binding protein-4 protease that is secreted by smooth muscle cells.
TLDR
As IGFBP-4 is a potent inhibitor of IGF action, and the activity of this protease is regulated by IGF exposure, the protease represents a novel system for regulating the actions of IGF-I in this cell type.
Posttranslational regulation of insulin-like growth factor binding protein-4 in normal and transformed human fibroblasts. Insulin-like growth factor dependence and biological studies.
TLDR
Evidence is provided for a novel IGF-dependent IGFBP-4-specific protease that modifies IGF BP-4 structure and function, and indicate a preferential role for IGF-II in its activation.
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