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Insulin-like growth factor system in cancer: novel targeted therapies.

Brahmkhatri VP, Prasanna C, Atreya HS - Biomed Res Int (2015)

Bottom Line: These effects depend on the bioavailability of IGFs, which is regulated by IGF binding proteins (IGFBPs).We have attempted to expand the general viewpoint on IGF-1R, its inhibitors, potential limitations of IGF-1R, antibodies and tyrosine kinase inhibitors, and IGFBP actions.This can lead to the development of novel cancer therapies.

View Article: PubMed Central - PubMed

Affiliation: NMR Research Centre, Indian Institute of Science, Bangalore 560012, India.

ABSTRACT
Insulin-like growth factors (IGFs) are essential for growth and survival that suppress apoptosis and promote cell cycle progression, angiogenesis, and metastatic activities in various cancers. The IGFs actions are mediated through the IGF-1 receptor that is involved in cell transformation induced by tumour. These effects depend on the bioavailability of IGFs, which is regulated by IGF binding proteins (IGFBPs). We describe here the role of the IGF system in cancer, proposing new strategies targeting this system. We have attempted to expand the general viewpoint on IGF-1R, its inhibitors, potential limitations of IGF-1R, antibodies and tyrosine kinase inhibitors, and IGFBP actions. This review discusses the emerging view that blocking IGF via IGFBP is a better option than blocking IGF receptors. This can lead to the development of novel cancer therapies.

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Related in: MedlinePlus

(a) 2D [15N-1H] HSQC spectrum of purified full-length hIGFBP-2 (1.0 mM; nondeuterated) recorded at a 1H resonance frequency of 800 MHz at 285 K. (b) TEM images of (hollow) nanotubular structures formed by the C-terminal fragment of human IGFBP-2.
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fig6: (a) 2D [15N-1H] HSQC spectrum of purified full-length hIGFBP-2 (1.0 mM; nondeuterated) recorded at a 1H resonance frequency of 800 MHz at 285 K. (b) TEM images of (hollow) nanotubular structures formed by the C-terminal fragment of human IGFBP-2.

Mentions: We recently discovered that the C-terminal fragment of hIGFBP-2 (residues 249–289) self-assembles spontaneously and reversibly into nanotubular structures under nonreducing conditions and remains as a monomer under reducing condition. These nanotubular structures were studied extensively by transmission electron microscopy (TEM), NMR spectroscopy (Figures 6(a) and 6(b)), and circular dichroism (CD) and a mechanism for their formation has been worked out [105].


Insulin-like growth factor system in cancer: novel targeted therapies.

Brahmkhatri VP, Prasanna C, Atreya HS - Biomed Res Int (2015)

(a) 2D [15N-1H] HSQC spectrum of purified full-length hIGFBP-2 (1.0 mM; nondeuterated) recorded at a 1H resonance frequency of 800 MHz at 285 K. (b) TEM images of (hollow) nanotubular structures formed by the C-terminal fragment of human IGFBP-2.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4383470&req=5

fig6: (a) 2D [15N-1H] HSQC spectrum of purified full-length hIGFBP-2 (1.0 mM; nondeuterated) recorded at a 1H resonance frequency of 800 MHz at 285 K. (b) TEM images of (hollow) nanotubular structures formed by the C-terminal fragment of human IGFBP-2.
Mentions: We recently discovered that the C-terminal fragment of hIGFBP-2 (residues 249–289) self-assembles spontaneously and reversibly into nanotubular structures under nonreducing conditions and remains as a monomer under reducing condition. These nanotubular structures were studied extensively by transmission electron microscopy (TEM), NMR spectroscopy (Figures 6(a) and 6(b)), and circular dichroism (CD) and a mechanism for their formation has been worked out [105].

Bottom Line: These effects depend on the bioavailability of IGFs, which is regulated by IGF binding proteins (IGFBPs).We have attempted to expand the general viewpoint on IGF-1R, its inhibitors, potential limitations of IGF-1R, antibodies and tyrosine kinase inhibitors, and IGFBP actions.This can lead to the development of novel cancer therapies.

View Article: PubMed Central - PubMed

Affiliation: NMR Research Centre, Indian Institute of Science, Bangalore 560012, India.

ABSTRACT
Insulin-like growth factors (IGFs) are essential for growth and survival that suppress apoptosis and promote cell cycle progression, angiogenesis, and metastatic activities in various cancers. The IGFs actions are mediated through the IGF-1 receptor that is involved in cell transformation induced by tumour. These effects depend on the bioavailability of IGFs, which is regulated by IGF binding proteins (IGFBPs). We describe here the role of the IGF system in cancer, proposing new strategies targeting this system. We have attempted to expand the general viewpoint on IGF-1R, its inhibitors, potential limitations of IGF-1R, antibodies and tyrosine kinase inhibitors, and IGFBP actions. This review discusses the emerging view that blocking IGF via IGFBP is a better option than blocking IGF receptors. This can lead to the development of novel cancer therapies.

Show MeSH
Related in: MedlinePlus