scholarly journals Protein Kinase D1 (PKD1) Is a New Functional Non-Genomic Target of Bisphenol A in Breast Cancer Cells

2020 ◽  
Vol 10 ◽  
Author(s):  
Messaouda Merzoug-Larabi ◽  
Ilige Youssef ◽  
Ai Thu Bui ◽  
Christine Legay ◽  
Sophia Loiodice ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Protein Kinase ◽  
Bisphenol A ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Protein Kinase D1

scholarly journals Preferential Dependence of Breast Cancer Cells versus Normal Cells on Integrin-Linked Kinase for Protein Kinase B/Akt Activation and Cell Survival

2006 ◽  
Vol 66 (1) ◽  
pp. 393-403 ◽  
Author(s):  
Armelle A. Troussard ◽  
Paul C. McDonald ◽  
Elizabeth D. Wederell ◽  
Nasrin M. Mawji ◽  
Nolan R. Filipenko ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Protein Kinase ◽  
Cell Survival ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Protein Kinase B ◽  
Normal Cells ◽  
Akt Activation ◽  
Integrin Linked Kinase

scholarly journals Inhibition of growth-factor-induced phosphorylation and activation of protein kinase B/Akt by atypical protein kinase C in breast cancer cells

2000 ◽  
Vol 352 (2) ◽  
pp. 475-482 ◽  
Author(s):  
Muling MAO ◽  
Xianjun FANG ◽  
Yiling LU ◽  
Ruth LAPUSHIN ◽  
Robert C. BAST ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Protein Kinase B ◽  
Akt Phosphorylation ◽  
Kinase C ◽  
Pkc Inhibitors

The protein kinase B/Akt serine/threonine kinase, located downstream of phosphoinositide 3-kinase (PI-3K), is a major regulator of cellular survival and proliferation. Atypical protein kinase C (aPKC) family members are activated by PI-3K and also contribute to cell proliferation, suggesting that Akt and aPKC might interact to activate signalling through the PI-3K cascade. Here we demonstrate that blocking PKC activity in MDA-MB-468 breast cancer cells increased the phosphorylation and activity of Akt. Functional PI-3K was required for the PKC inhibitors to increase Akt phosphorylation and activation, potentially owing to the activation of specific PKC isoforms by PI-3K. The concentration dependence of the action of the PKC inhibitors implicates aPKC in the inhibition of Akt phosphorylation and activity. In support of a role for aPKC in the regulation of Akt, Akt and PKCζ or PKCλ/ℓ were readily co-precipitated from the BT-549 breast cancer cell line. Furthermore, the overexpression of PKCζ inhibited growth-factor-induced increases in Akt phosphorylation and activity. Thus PKCζ associates physically with Akt and decreases Akt phosphorylation and enzyme activity. The effects of PKC on Akt were transmitted through the PI-3K cascade as indicated by changes in p70 s6 kinase (p70s6k) phosphorylation. Thus PKCζ, and potentially other PKC isoenzymes, regulate growth-factor-mediated Akt phosphorylation and activation, which is consistent with a generalized role for PKCζ in limiting growth factor signalling through the PI-3K/Akt pathway.

scholarly journals Hormone-Like Effects of Bisphenol A on p53 and Estrogen Receptor Alpha in Breast Cancer Cells

2019 ◽  
Vol 8 (1) ◽  
pp. 169-184 ◽  
Author(s):  
Victoria Lloyd ◽  
Mia Morse ◽  
Betsy Purakal ◽  
Jordan Parker ◽  
Paige Benard ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Estrogen Receptor ◽  
Bisphenol A ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Estrogen Receptor Alpha ◽  
Receptor Alpha
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