Autoregulation of phospholipase D activity is coupled to selective induction of phospholipase D1 expression to promote invasion of breast cancer cells

2010 ◽  
Vol 128 (4) ◽  
pp. 805-816 ◽  
Author(s):  
Dong Woo Kang ◽  
Mi Hee Park ◽  
Young Jun Lee ◽  
Hyung Sik Kim ◽  
Craig W. Lindsley ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Phospholipase D ◽  
Breast Cancer Cells ◽  
Phospholipase D1

Target-controlled gating liposome “off–on” cascade amplification for sensitive and accurate detection of phospholipase D in breast cancer cells with a low-background signal

2016 ◽  
Vol 52 (70) ◽  
pp. 10660-10663 ◽  
Author(s):  
Qingwang Xue ◽  
Wei Jiang ◽  
Lei Wang
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Phospholipase D ◽  
Breast Cancer Cells ◽  
Detection Method ◽  
Background Signal ◽  
Low Background ◽  
Accurate Detection ◽  
Cascade Amplification

Here we developed a simple, sensitive and accurate PLD detection method based on a target-controlled gating liposome (TCGL) “off–on” cascade amplified strategy and personal glucose meters (PGMs).

Phospholipase D prevents apoptosis in v-Src-transformed rat fibroblasts and MDA-MB-231 breast cancer cells

2003 ◽  
Vol 302 (3) ◽  
pp. 615-619 ◽  
Author(s):  
Minghao Zhong ◽  
Yingjie Shen ◽  
Yang Zheng ◽  
Troy Joseph ◽  
Desmond Jackson ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Phospholipase D ◽  
Breast Cancer Cells ◽  
Rat Fibroblasts

scholarly journals Phospholipase D inhibitor enhances radiosensitivity of breast cancer cells

2013 ◽  
Vol 45 (8) ◽  
pp. e38-e38 ◽  
Author(s):  
Ju Cheol Son ◽  
Dong Woo Kang ◽  
Kwang Mo Yang ◽  
Kang-Yell Choi ◽  
Tae Gen Son ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Phospholipase D ◽  
Breast Cancer Cells

scholarly journals The phospholipase D inhibitor FIPI potently blocks EGF-induced calcium signaling in human breast cancer cells

2021 ◽  
Vol 19 (1) ◽  
Author(s):  
Helena M. Stricker ◽  
Nadine Rommerswinkel ◽  
Silvia Keil ◽  
Sandina A. Gnoth ◽  
Bernd Niggemann ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Calcium Signaling ◽  
Cancer Cells ◽  
Phospholipase D ◽  
Human Breast Cancer ◽  
Breast Cancer Cells ◽  
Calcium Release ◽  
Human Breast Cancer Cells ◽  
Human Breast ◽  
Expression Levels

Abstract Background Phosphotyrosine kinase (PTK)-mediated phospholipase C-γ1 (PLC-γ1) signaling plays a crucial role in the release of the universal second messenger calcium from intracellular stores, which is mandatory for several cellular processes, including cell migration. However, PLC-γ1 could also be activated in a PTK-independent manner by phospholipase D (PLD)-derived phosphatidic acid (PA). Because both higher PLD expression levels and PLD activity have also been associated with breast cancer cell invasion and migration, we wondered whether there might be a link between PLD and PLC-γ1, which was investigated in this study. Materials MDA-MB-468-NEO (EGFR positive) and MDA-MB-468-HER2 (EGFR and HER2 positive) human breast cancer cells were used in this study. The migratory behavior of the cells in the presence of epidermal growth factor (EGF) and the PLD inhibitor 5-fluoro-2-indolyl-des-chlorohalopemide (FIPI) was analyzed using the 3D collagen matrix migration assay. Changes in cytosolic calcium levels in the presence of EGF, FIPI and Sig-1R agonists and antagonists as well as in PLD1 siRNA knockdown cells were determined by flow cytometry. Western blot analyses were performed to determine the basal expression levels and phosphorylation patterns of EGFR, HER2, AKT, MAPKp42/44, PLC-γ1 and Sig-1R. Results The EGF-induced migration of MDA-MB-468-NEO and MDA-MB-468-HER2 cells was significantly impaired by FIPI. Likewise, FIPI also significantly abolished EGF-induced calcium release in both cell lines. However, neither the expression levels nor the phosphorylation patterns of EGFR, HER2, AKT, MAPKp42/44 and PLC-γ1 were markedly changed by FIPI. Knockdown of PLD1 expression by siRNA also significantly impaired EGF-induced calcium release in both cell lines. Targeting Sig-1R, which interacts with IP3R, with the antagonist BD1047 also abrogated EGF-induced calcium release. However, EGF-induced calcium release was also impaired if cells were treated with the Sig-1R agonists PRE084 and PPBP maleate. Conclusion In summary, blocking PLD activity with the specific inhibitor FIPI or knocking down PDL1 expression by siRNA significantly impaired EGF-induced calcium release in MDA-MB-468-NEO and MDA-MB-468-HER2 cells, likely indicating a connection between PLD activity and PLC-γ1-mediated calcium signaling. However, how PLD activity interferes with the release of calcium from intracellular stores remains unclear.

scholarly journals A New Signaling Pathway (JAK-Fes-phospholipase D) That Is Enhanced in Highly Proliferative Breast Cancer Cells

2013 ◽  
Vol 288 (14) ◽  
pp. 9881-9891 ◽  
Author(s):  
Qing Ye ◽  
Samuel Kantonen ◽  
Karen M. Henkels ◽  
Julian Gomez-Cambronero
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Signaling Pathway ◽  
Phospholipase D ◽  
Breast Cancer Cells

scholarly journals Triptolide-induced suppression of phospholipase D expression inhibits proliferation of MDA-MB-231 breast cancer cells

2009 ◽  
Vol 41 (9) ◽  
pp. 678 ◽  
Author(s):  
Dong Woo Kang ◽  
Ji Young Lee ◽  
Deuk-hee Oh ◽  
Seon Yang Park ◽  
Tae Min Woo ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Phospholipase D ◽  
Breast Cancer Cells
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