Type V collagen and protein kinase C η down-regulation in 8701-BC breast cancer cells

2011 ◽  
Vol 52 (5) ◽  
pp. 348-358 ◽  
Author(s):  
Claudio Luparello ◽  
Rosalia Sirchia ◽  
Alessandra Longo
Keyword(s):  
Breast Cancer ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Down Regulation ◽  
Type V Collagen ◽  
Kinase C ◽  
Type V

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 Protein kinase C-α downregulates estrogen receptor-α by suppressing c-Jun phosphorylation in estrogen receptor-positive breast cancer cells

2013 ◽  
Vol 31 (3) ◽  
pp. 1423-1428 ◽  
Author(s):  
SANGMIN KIM ◽  
JEONGMIN LEE ◽  
SE KYUNG LEE ◽  
SOO YOUN BAE ◽  
JIYOUNG KIM ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Estrogen Receptor ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Estrogen Receptor Α ◽  
Kinase C ◽  
Estrogen Receptor Positive ◽  
Positive Breast Cancer

Involvement of protein kinase C in the growth regulation of human breast cancer cells

1991 ◽  
pp. 229-248 ◽  
Author(s):  
Doriano Fabbro ◽  
Willy Küng ◽  
Serban D. Costa ◽  
Christoph Borner ◽  
Urs Regenass ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Cancer Cells ◽  
Human Breast Cancer ◽  
Breast Cancer Cells ◽  
Growth Regulation ◽  
Human Breast Cancer Cells ◽  
Human Breast ◽  
Kinase C

Protein Kinase C β Enhances Growth and Expression of Cyclin D1 in Human Breast Cancer Cells

2006 ◽  
Vol 66 (23) ◽  
pp. 11399-11408 ◽  
Author(s):  
Haiyang Li ◽  
I. Bernard Weinstein
Keyword(s):  
Breast Cancer ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Cyclin D1 ◽  
Cancer Cells ◽  
Human Breast Cancer ◽  
Breast Cancer Cells ◽  
Human Breast Cancer Cells ◽  
Human Breast ◽  
Kinase C
Sign in / Sign up

Export Citation Format

Share Document