0852 Effect of cortisol on mammary epithelial cell Bax and Bcl-2 gene expression at lactation peak of goats

2016 ◽  
Vol 94 (suppl_5) ◽  
pp. 410-410
Author(s):  
G. F. Bomfim
2011 ◽  
Vol 11 (2) ◽  
pp. 464-474 ◽  
Author(s):  
Adriana Priscila Trapé ◽  
Maria Lucia Hirata Katayama ◽  
Rosimeire Aparecida Roela ◽  
Helena Brentani ◽  
Graziela Rosa Ravacci ◽  
...  

2006 ◽  
Vol 20 (10) ◽  
pp. 2304-2314 ◽  
Author(s):  
Wei Wu ◽  
Min Zou ◽  
Deanna R. Brickley ◽  
Travis Pew ◽  
Suzanne D. Conzen

Abstract Activation of the glucocorticoid receptor (GR) plays a critical role in the stress response of virtually all cell types. Despite recent advances in large-scale genomic and proteomic data acquisition, identification of physiologically relevant molecular events downstream of nuclear hormone receptor activation remains challenging. By analyzing gene expression changes 30 min after dexamethasone (Dex) treatment, we previously found that immediate induction of serum and glucocorticoid-regulated kinase-1 (SGK-1) expression is required for GR-mediated mammary epithelial cell survival signaling. We now report that activation of the GR mediates Forkhead transcription factor 3a (FOXO3a) phosphorylation and inactivation in mammary epithelial cells. GR-mediated induction of SGK-1 expression is required for FOXO3a inactivation; additional growth factor stimulation is not required. To further explore the gene expression changes that occur downstream of GR-mediated FOXO3a inactivation, we analyzed temporal gene expression data and selected GR-down-regulated genes containing core FOXO3a binding motifs in their proximal promoters. This approach revealed several previously unrecognized transcriptional target genes of FOXO3a, including IGF binding protein-3 (IGFBP-3). Endogenous IGFBP-3 expression was confirmed to be dependent on the GR-SGK-1-FOXO3a signaling pathway. Moreover, GR activation decreased FOXO3a-induced apoptosis in SK-BR-3 breast cancer cells. Collectively, our data suggest that GR-mediated FOXO3a inactivation is an important mechanism contributing to glucocorticoid-mediated mammary epithelial cell survival.


2000 ◽  
Vol 2 (S1) ◽  
Author(s):  
GV Vutskits ◽  
P Salmon ◽  
JV Soriano ◽  
C Cudre-Mauroux ◽  
D Trono ◽  
...  

2011 ◽  
Vol 78 (3) ◽  
pp. 365-372 ◽  
Author(s):  
Georgios Theodorou ◽  
Chiara Pecorini ◽  
Raffaella Rebucci ◽  
Francesca Saccone ◽  
Christina Lecchi ◽  
...  

There is conflicting evidence in the literature as to whether up-regulation of urokinase plasminogen activator (u-PA) expression is related to bovine mammary epithelial cell growth. The role of u-PA receptor (u-PAR) and that of the plasminogen activator inhibitors type 1 and type 2 (PAI-1 and PAI-2) in bovine mammary epithelial cell proliferation is not known. The effect of growth factors and various hormones known to affect mammary function on expression of u-PA, u-PAR, PAI-1, PAI-2 and cell proliferation using the BME-UV1 bovine mammary epithelial cell line was examined. Cell proliferation was measured using the MTT assay and direct cell enumeration. Results showed that both IGF-1 and EGF increased cell proliferation but EGF was a more potent mitogen than IGF-1. Furthermore, IGF-1 increased by 2-fold expression of both u-PA and u-PAR while EGF increased by 3·8-fold the expression of only u-PAR. Both growth factors had no effect on expression of PAI-1 and PAI-2. In a manner consistent with changes in gene expression, EGF and to a lesser extent IGF-1 up-regulated total cell associated, membrane-bound and secreted u-PA activity. Thus, a strong correlation exists between u-PAR gene expression along with the activity of u-PA present on cell membranes and cell proliferation. Dexamethasone, prolactin and surprisingly insulin had no effect on cell proliferation. Dexamethasone alone and when combined with insulin or prolactin up-regulated gene expression of both PAI- and PAI-2 but not that of u-PA and u-PAR. Decreased total cell-associated, membrane-bound and secreted u-PA activity was detected in cells cultured in the presence of dexamethasone when combined with insulin or prolactin. However no such effect was observed in the presence of dexamethasone alone. Thus, dexamethasone acting synergistically with prolactin or insulin inhibits the activation of the plasmin-plasminogen system but this inhibition is not correlated with any changes in cell proliferation.


2008 ◽  
Vol 22 (10) ◽  
pp. 2307-2321 ◽  
Author(s):  
Rebecca S. Muraoka-Cook ◽  
Melissa Sandahl ◽  
Debra Hunter ◽  
Leah Miraglia ◽  
H. Shelton Earp

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