Gene interactions and pathways from curated databases and text-mining

◀ Back to IGF1

ESR1 — IGF1

Pathways - manually collected, often from reviews:

Text-mined interactions from Literome

Campagnoli et al., Gynecol Endocrinol 1999 (Breast Neoplasms...) : Actually, estrogens and IGF-I have a synergistic effect on cell proliferation, and IGF-I is necessary for maximum estrogen-receptor activation in breast cancer cell lines
Klotz et al., Endocrinology 2000 : The dose of chemical necessary to activate IGF-I signaling varied, with the order of potency : E2 = diethylstilbestrol > LY353381 > 4-hydroxytamoxifen > genistein > HPTE > bisphenol A. Administration of the chemicals to ERalpha knockout mice did not activate IGF-IR, indicating that ERalpha is required for activation of uterine IGF-IR by these diverse chemicals
Martin et al., Endocrinology 2000 : Stable transfection of cells with a dominant negative Akt mutant blocked the effects of EGF and IGF-I on ER-alpha expression and activity, whereas stable transfection of cells with a constitutively active Akt mutant mimicked the effects of EGF and IGF-I
Oesterreich et al., Cancer Res 2001 (Breast Neoplasms) : To prove that loss of IGF and estrogen mediated signaling and growth was a consequence of loss of ERalpha , we re-expressed ERalpha in C4-12 cells by stable transfection with HA-tagged ERalpha
Klotz et al., J Biol Chem 2002 : To determine whether ER alpha can be activated in vivo by IGF-1 signaling, transgenic mice carrying a luciferase gene driven by two estrogen response elements ( ERE-luciferase mice ) were utilized ... Together these data demonstrate that 1 ) functional signaling proximal to IGF-1R is maintained in the alpha ERKO mouse uterus, 2 ) ER alpha is necessary for IGF-1 induction of uterine nuclear proliferative responses, and 3 ) cross-talk between IGF-1R and ER signaling pathways exists in vivo
Martin et al., J Nutr 2002 (Breast Neoplasms) : Recent studies show that the effects of IGF-I on estrogen receptor activity are mediated in part by the protein kinase A and phosphatidylinositol-3-kinase/Akt pathways
Movérare et al., Proc Natl Acad Sci U S A 2003 (Osteoporosis) : ERalpha activation increased serum levels of insulin-like growth factor I , which were positively correlated with all the cortical and trabecular bone parameters that were specifically preserved by ERalpha activation but not by AR activation, suggesting that insulin-like growth factor I might mediate these effects of ERalpha activation
Surmacz et al., J Exp Clin Cancer Res 2004 (Breast Neoplasms) : Most notably, activation of ERalpha upregulates the expression of IRS-1, IGF-IR , and IGF-1, which results in amplification of IGF-I responses ... Reciprocally, stimulation of IGF-IR increases the phosphorylation and activity of ERalpha
Reizner et al., J Mol Endocrinol 2005 (Breast Neoplasms) : Triple cotransfection experiments using an ERalpha expression vector in the absence or presence of WT1 expression vectors, along with an IGF-IR promoter reporter plasmid, revealed that ERalpha stimulated IGF-IR promoter activity whereas coexpression of WT1 abrogated the effect of ERalpha
Garcia-Segura et al., Neuroendocrinology 2006 : Conversely, IGF-I regulates ERalpha transcriptional activity in neuroblastoma cells and the PI3K/Akt/GSK3 signaling pathway is involved in this effect
Maor et al., J Endocrinol 2006 (Breast Neoplasms) : The aim of our study was to examine the transcriptional mechanisms involved in regulation of IGF-IR gene expression by the estrogen receptor ( ER ) ... In summary, our studies demonstrate that IGF-IR gene transcription in breast cancer cells is controlled by interactions between ERalpha and Sp1
Baron et al., J Biol Chem 2007 : We demonstrate that on a complex promoter such as the pS2/TFF1 promoter, which contains binding sites for ERalpha and for the activating protein-1 (AP1) complex, transcriptional activation by IGF-I requires both ERalpha and the AP1 complex
Sisci et al., Ann Oncol 2007 (Breast Neoplasms) : IRS-1 knock down abrogated IGF-1 dependent transcriptional activity of unliganded ERalpha , but induced the activity of liganded ERalpha
Di et al., Hum Reprod 2008 (Leiomyoma...) : Additionally, extracellular regulated kinase (ERK), Src homology/collagen (Shc) and ER alpha were transiently activated, and interactions between ER alpha and IGF-I receptor (IGF-IR) were rapidly induced by genistein in LM cells
Marin et al., J Steroid Biochem Mol Biol 2009 : ERalpha interacts with the signaling of IGF-1 receptor in neural cells : ERalpha transcriptional activity is regulated by IGF-1 receptor signaling and estradiol regulates IGF-1 receptor signaling
Hewitt et al., J Biol Chem 2010 : This proliferation and IGF1 synthesis requires the estrogen receptor ( ER ) , which binds directly to target DNA sequences ( estrogen-responsive elements or EREs ), or interacts with other transcription factors, such as AP1, to impact transcription ... Together, these observations suggest in contrast to previous in vitro studies of IGF-1 regulation involving AP1 motifs that direct ER alpha-DNA interaction is required to increase Igf1 transcription
Sunters et al., J Biol Chem 2010 : Strain related IGF-IR activation of AKT requires estrogen receptor alpha (ERalpha) with which IGF-1R physically associates
Lee et al., Biomed Pharmacother 1995 (Breast Neoplasms) : In addition, recent data now indicate that IGF ligands can also activate estrogen receptor ( ER ) in a ligand independent manner
Duenas et al., Neuroscience 1996 : These findings suggest that estradiol induced activation of the estrogen receptor in developing hypothalamic cells requires the presence of insulin-like growth factor-I , and that both estradiol and insulin-like growth factor-I use the estrogen receptor as a mediator of their trophic effects on hypothalamic neurons
García-Segura et al., Horm Res 1996 : These findings indicate that estrogen induced activation of the estrogen receptor in developing hypothalamic neurons requires the presence of IGF-I and that both estradiol and IGF-I use the estrogen receptor to mediate their trophic effects on hypothalamic cells