Up-regulation of nuclear IGF-I receptor by short term exposure of stilbene estrogen, diethylstilbestrol

Chen, Chiao-Wen; Roy, Deodutta

doi:10.1016/0303-7207(96)03751-3

Cited by 21 publications

(12 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…An initial report of intact IGF-1 receptors present in the nucleus (Chen and Roy 1996) has been confirmed and extended in recent reports from two groups (Aleksic et al 2010;Deng et al 2010;Sehat et al 2010). Both groups indicate that this relocalization from plasma membrane to nucleus is IGF-1 dependent and that the nuclear receptor may function as a transcriptional coactivator.…”

Section: Igf-1mentioning

confidence: 65%

Receptor Tyrosine Kinases in the Nucleus

Carpenter

Liao

2013

Cold Spring Harbor Perspectives in Biology

View full text Add to dashboard Cite

To date, 18 distinct receptor tyrosine kinases (RTKs) are reported to be trafficked from the cell surface to the nucleus in response to ligand binding or heterologous agonist exposure. In most cases, an intracellular domain (ICD) fragment of the receptor is generated at the cell surface and translocated to the nucleus, whereas for a few others the intact receptor is translocated to the nucleus. ICD fragments are generated by several mechanisms, including proteolysis, internal translation initiation, and messenger RNA (mRNA) splicing. The most prevalent mechanism is intramembrane cleavage by g-secretase. In some cases, more than one mechanism has been reported for the nuclear localization of a specific RTK. The generation and use of RTK ICD fragments to directly communicate with the nucleus and influence gene expression parallels the production of ICD fragments by a number of non-RTK cell-surface molecules that also influence cell proliferation. This review will be focused on the individual RTKs and to a lesser extent on other growth-related cell-surface transmembrane proteins.

show abstract

Section: Igf-1mentioning

confidence: 65%

Receptor Tyrosine Kinases in the Nucleus

Carpenter

Liao

2013

Cold Spring Harbor Perspectives in Biology

View full text Add to dashboard Cite

show abstract

“…Alteration of EGF-R expression in hamster kidney (Narayan and Roy, unpublished) and in mouse reproductive tract tissue in response to DES exposure has also been reported (72,73). Recently, we have shown the enhanced expression of both plasma membrane and nuclear IGF-I receptors and an increase in the IGF-1 mediated phosphorylation in DES-treated hamster kidney membranes as compared to that of age-matched controls (75)(76)(77)(78). The higher expression of c-fos, c-jun and c-myc in hamster kidney tumor tissues and of c-myc and mdm-2 in murine uterine adenocarcinoma cells compared to that of the control has been observed (79)(80)(81).…”

Section: Impaired Expression Of Transcription-regulating and Dna Repamentioning

confidence: 70%

Is exposure to environmental or industrial endocrine disrupting estrogen-like chemicals able to cause genomic instability

Roy

Colerangle²,

Singh³

1998

Front Biosci

Self Cite

View full text Add to dashboard Cite

“…Nuclear localization of IGF-1R was first reported in hamster kidney cells in 1996 [35]. Treatment of hamster kidney cells with diethylstilbestrol (a synthetic nonsteroidal estrogen) induced nIGF-1R.…”

Section: Discussionmentioning

confidence: 99%

Nuclearly translocated insulin-like growth factor 1 receptor phosphorylates histone H3 at tyrosine 41 and inducesSNAI2expressionviaBrg1 chromatin remodeling protein

et al. 2016

View full text Add to dashboard Cite

The insulin-like growth factor-1 receptor (IGF-1R) is a receptor tyrosine kinase that has crucial roles in cell proliferation and protection from apoptosis. It is therefore not surprising that IGF-1R is often found overexpressed in many types of tumors. This has made IGF-1R a prominent target molecule for pharmacological companies to develop new anti-cancer agents. However, several clinical trials during the last 5 years using IGF-1R specific antibodies have shown disappointing results. We have previously shown that upon IGF-1 stimulation, the receptor becomes SUMOylated and translocates into the nucleus of cancer cells to act as a transcription co-factor. Soon after our original study, several others have reported nuclear IGF-1R (nIGF-1R) as well, and some of them have demonstrated a prognostic value of nIGF-1R expression in cancer. In the current study we demonstrate that nIGF-1R binds to and phosphorylates histone H3 at tyrosine 41 (H3Y41) in HeLa cells. Furthermore, our results suggest that phosphorylation of H3Y41 by nIGF-1R, stabilizes the binding of Brg1 chromatin remodeling protein to Histone H3. Our findings suggest that phosphorylated nIGF-1R, rather than total nIGF-1R, plays a superior role in these contexts. We identified SNAI2 oncogene as a target gene for nIGF-1R and its expression was decreased upon mutation of H3Y41 or by Brg1 knockdown. Furthermore, we demonstrate that both IGF-1R and Brg1 binds to the SNAI2 promoter. As SNAI2 protein is implicated in e.g. cancer invasion and metastasis, the nIGF-1R-mediated effects shown in this study may influence such important tumor phenotypic actions.

show abstract

Up-regulation of nuclear IGF-I receptor by short term exposure of stilbene estrogen, diethylstilbestrol

Cited by 21 publications

References 13 publications

Receptor Tyrosine Kinases in the Nucleus

Receptor Tyrosine Kinases in the Nucleus

Is exposure to environmental or industrial endocrine disrupting estrogen-like chemicals able to cause genomic instability

Nuclearly translocated insulin-like growth factor 1 receptor phosphorylates histone H3 at tyrosine 41 and inducesSNAI2expressionviaBrg1 chromatin remodeling protein

Contact Info

Product

Resources

About