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Old 07-16-2017, 04:20 PM
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rss IGF - S-nitrosylation of the IGF-1 receptor disrupts the cell proliferative action of

S-nitrosylation of the IGF-1 receptor disrupts the cell proliferative action of IGF-1.

Biochem Biophys Res Commun. 2017 Jul 11;:

Authors: Okada K, Zhu BT

Abstract
The insulin-like growth factor 1 receptor (IGF-1R) is a disulfide-linked heterotetramer containing two ?-subunits and two ?-subunits. Earlier studies demonstrate that nitric oxide (NO) can adversely affect IGF-1 action in the central nervous system. It is known that NO can induce S-nitrosylation of the cysteine residues in proteins, thereby partly contributing to the regulation of protein function. In the present study, we sought to determine whether S-nitrosylation of the cysteine residues in IGF-1R is an important post-translational modification that regulates its response to IGF-1. Using cultured SH-SY5Y human neuroblastoma cells as an in vitro model, we found that treatment of cells with S-nitroso-cysteine (SNOC), a NO donor that can nitrosylate the cysteine residues in proteins, induces S-nitrosylation of the ? subunit of IGF-1R but not its ?-subunit. IGF-1R? S-nitrosylation by SNOC is coupled with increased dissociation of the IGF-1R protein complex. In addition, disruption of the IGF-1R function resulting from S-nitrosylation of the IGF-1R? subunit is associated with disruption of the phosphoinositide 3-kinase (PI3K) and mitogen-activated protein kinase (MAPK) signaling pathways. Further, we observed that SNOC-induced IGF-1R? S-nitrosylation results in a dose-dependent inhibition of cell proliferation and survival. Together, these results suggest that elevated nitrosative stress may result in dysfunction of cellular IGF-1R signaling through S-nitrosylation of the cysteine residues in the IGF-1R? subunit, thereby disrupting the downstream PI3K and MAPK signaling functions and ultimately resulting in inhibition of cell proliferation and survival.


PMID: 28709872 [PubMed - as supplied by publisher]



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Insulin like growth factors
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