scholarly journals A kinase inhibitor screen identifies Mcl-1 and Aurora kinase A as novel treatment targets in antiestrogen-resistant breast cancer cells

Oncogene ◽  
2014 ◽  
Vol 34 (32) ◽  
pp. 4199-4210 ◽  
Author(s):  
S Thrane ◽  
A M Pedersen ◽  
M B H Thomsen ◽  
T Kirkegaard ◽  
B B Rasmussen ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Kinase Inhibitor ◽  
Aurora Kinase ◽  
Aurora Kinase A ◽  
Treatment Targets ◽  
Novel Treatment ◽  
Inhibitor Screen ◽  
Kinase A

Polymer Nanovesicle-Mediated Delivery of MLN8237 Preferentially Inhibits Aurora Kinase A To Target RalA and Anchorage-Independent Growth in Breast Cancer Cells

2018 ◽  
Vol 15 (8) ◽  
pp. 3046-3059
Author(s):  
Siddhi Inchanalkar ◽  
Nilesh Umakant Deshpande ◽  
Vishakha Kasherwal ◽  
Manickam Jayakannan ◽  
Nagaraj Balasubramanian
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Aurora Kinase ◽  
Aurora Kinase A ◽  
Anchorage Independent Growth ◽  
Kinase A

scholarly journals San Huang Decoction Targets Aurora Kinase A to Inhibit Tumor Angiogenesis in Breast Cancer

2020 ◽  
Vol 19 ◽  
pp. 153473542098346
Author(s):  
Yanlei Xu ◽  
Cong Wang ◽  
Xiyan Chen ◽  
Yongfei Li ◽  
Weihe Bian ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Tumor Angiogenesis ◽  
Breast Cancer Cells ◽  
Chinese Herb ◽  
Xenograft Model ◽  
Aurora Kinase ◽  
Endothelial Cell Migration ◽  
Aurora Kinase A ◽  
Kinase A

San Huang Decoction (SHD), a Chinese herb formula, has been popularly prescribed in the clinical treatment of patients suffering from breast cancer. The aim of this study was to explore the anti-angiogenic effects of SHD in breast cancer and explain the underlying mechanism. Transwell and Matrigel assays showed that SHD reduced human umbilical vein endothelial cell migration and tubule formation and ELISA and qRT-PCR assays demonstrated its mediation of vascular endothelial growth factor (VEGF) expression. siRNA silencing of aurora kinase A (AURKA) produced results similar to those obtained by inhibition of AURKA with SHD. In addition, a chorioallantoic membrane assay was carried out to directly examine the effect of SHD on breast cancer anti-angiogenesis and immunofluorescence and immunohistochemical staining analysis showed that SHD reduced the expression of CD31, AURKA, and VEGF in a xenograft model. Furthermore, SHD regulated extracellular signal-regulated kinase expression in breast cancer cells, which was examined by western blotting. In conclusion, our findings indicated that SHD treatment mimicked the decrease in tumor neovascularization in breast cancer cells after the siRNA-mediated knockdown of AURKA. Thus, SHD may inhibit tumor angiogenesis in breast cancer by targeting AURKA and downregulating the ERK signaling pathway.

scholarly journals Resveratrol inhibits cell cycle progression by targeting Aurora kinase A and Polo-like kinase 1 in breast cancer cells

2016 ◽  
Vol 35 (6) ◽  
pp. 3696-3704 ◽  
Author(s):  
RUBICELI MEDINA-AGUILAR ◽  
LAURENCE A. MARCHAT ◽  
ELENA ARECHAGA OCAMPO ◽  
PATRICIO GARIGLIO ◽  
JAIME GARCÍA MENA ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cell Cycle ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Cell Cycle Progression ◽  
Aurora Kinase ◽  
Cycle Progression ◽  
Aurora Kinase A ◽  
Kinase A

scholarly journals Aurora kinase A suppresses metabolic stress-induced autophagic cell death by activating mTOR signaling in breast cancer cells

Oncotarget ◽  
2014 ◽  
Vol 5 (17) ◽  
pp. 7498-7511 ◽  
Author(s):  
Ling-Zhi Xu ◽  
Zi-Jie Long ◽  
Fei Peng ◽  
Yang Liu ◽  
Jie Xu ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cell Death ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Metabolic Stress ◽  
Aurora Kinase ◽  
Mtor Signaling ◽  
Autophagic Cell Death ◽  
Aurora Kinase A ◽  
Kinase A

scholarly journals Aurora kinase A inhibition-induced autophagy triggers drug resistance in breast cancer cells

Autophagy ◽  
2012 ◽  
Vol 8 (12) ◽  
pp. 1798-1810 ◽  
Author(s):  
Zhengzhi Zou ◽  
Zhongyu Yuan ◽  
Qiongxia Zhang ◽  
Zijie Long ◽  
Jinna Chen ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Drug Resistance ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Aurora Kinase ◽  
Aurora Kinase A ◽  
Kinase A

scholarly journals A Kinase Inhibitor Screen Reveals Protein Kinase C-dependent Endocytic Recycling of ErbB2 in Breast Cancer Cells

2014 ◽  
Vol 289 (44) ◽  
pp. 30443-30458 ◽  
Author(s):  
Tameka A. Bailey ◽  
Haitao Luan ◽  
Eric Tom ◽  
Timothy Alan Bielecki ◽  
Bhopal Mohapatra ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Breast Cancer Cells ◽  
Kinase Inhibitor ◽  
Hsp90 Inhibitor ◽  
Endocytic Recycling ◽  
Erk Phosphorylation ◽  
Endosomal Signaling ◽  
Inhibitor Screen ◽  
Endocytic Traffic

ErbB2 overexpression drives oncogenesis in 20–30% cases of breast cancer. Oncogenic potential of ErbB2 is linked to inefficient endocytic traffic into lysosomes and preferential recycling. However, regulation of ErbB2 recycling is incompletely understood. We used a high-content immunofluorescence imaging-based kinase inhibitor screen on SKBR-3 breast cancer cells to identify kinases whose inhibition alters the clearance of cell surface ErbB2 induced by Hsp90 inhibitor 17-AAG. Less ErbB2 clearance was observed with broad-spectrum PKC inhibitor Ro 31-8220. A similar effect was observed with Go 6976, a selective inhibitor of classical Ca2+-dependent PKCs (α, β1, βII, and γ). PKC activation by PMA promoted surface ErbB2 clearance but without degradation, and ErbB2 was observed to move into a juxtanuclear compartment where it colocalized with PKC-α and PKC-δ together with the endocytic recycling regulator Arf6. PKC-α knockdown impaired the juxtanuclear localization of ErbB2. ErbB2 transit to the recycling compartment was also impaired upon PKC-δ knockdown. PMA-induced Erk phosphorylation was reduced by ErbB2 inhibitor lapatinib, as well as by knockdown of PKC-δ but not that of PKC-α. Our results suggest that activation of PKC-α and -δ mediates a novel positive feedback loop by promoting ErbB2 entry into the endocytic recycling compartment, consistent with reported positive roles for these PKCs in ErbB2-mediated tumorigenesis. As the endocytic recycling compartment/pericentrion has emerged as a PKC-dependent signaling hub for G-protein-coupled receptors, our findings raise the possibility that oncogenesis by ErbB2 involves previously unexplored PKC-dependent endosomal signaling.

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