Myosin light-chain kinase contributes to the proliferation and migration of breast cancer cells through cross-talk with activated ERK1/2

Zhou, Xiaolei; Liu, Yi; You, Jiacong; Zhang, Hang; Zhang, Xiaodong; Ye, Lihong

doi:10.1016/j.canlet.2008.05.028

Cited by 69 publications

(74 citation statements)

References 33 publications

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“…We have reported that a positive feedback cascade of Gi/o proteins-PLC-PKC-pERK1/2 mediated by cyclooxygenase (COX) and lipoxygenase (LOX) contributes to the high proliferation of LM-MCF-7 breast cancer cells [4] . Additionally, a cross-talk between myosin light chain kinase (MLCK) and phosphorylated ERK1/2 also leads to the high proliferation of LM-MCF-7 breast cancer cells [3] . In the present study, we investigated the mechanism of high proliferation of LM-MCF-7 cells involving Wnt/β-catenin signaling.…”

Section: Discussionmentioning

confidence: 99%

“…Plasmids pGL3-sur containing Survivin promoter gene and pcDNA-Tcf4δ containing a dominant-negative Tcf-4 gene lacking the portion responsible for the protein binding to DNA were constructed previously in our lab [3] . Short interfering RNA (siRNA) duplex composed of sense and antisense strands were synthesized (Guangzhou RiboBio Co, Ltd, China).…”

Section: Rna Isolation and Rt-pcrmentioning

confidence: 99%

“…Results of gene chips assay, containing 21,329 kinds of human genes, demonstrated that 67 kinds of genes were markedly different between LM-MCF-7 cells and MCF-7 cells [2] , suggesting that the two cell lines were remarkably different in molecular events associated with malignance. Therefore, the two cell lines, having the similar genetic background, are ideal parallel cell lines to investigate the mechanism of proliferation of breast cancer cells [1,3,4] . However, the endogenous signal pathways which are responsible for the high proliferation ability of LM-MCF-7 cells remain unclear.…”

Section: Introductionmentioning

confidence: 99%

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Downregulation of Dickkopf-1 is responsible for high proliferation of breast cancer cells via losing control of Wnt/β-catenin signaling

et al. 2010

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Aim: To investigate the role of DKK-1/Wnt/β-catenin signaling in high proliferation of LM-MCF-7 breast cancer cells, a sub-clone of MCF-7 cell line. Methods: Two cell lines (MCF-7 and LM-MCF-7) with different proliferation abilities were used. LM-MCF-7 cells were transiently transfected with the pcDNA3-DKK-1 plasmid encoding the DKK-1 gene (or MCF-7 cells were transfected siRNA targeting DKK-1 mRNA). Flow cytometry analysis and 5-bromo-2′-deoxyuridine (BrdU) incorporation assay were applied to detect the cell proliferation. The expression levels of β-catenin, phosphorylated β-catenin, c-Myc, cyclin D1 and Survivin were examined by Western blot analysis. The regulation of Survivin was investigated by Luciferase reporter gene assay. Results: Western blot and RT-PCR analysis showed that the expression level of DKK-1 was downregulated in LM-MCF-7 relative to MCF-7 cells. Flow cytometry and BrdU incorporation assay showed DKK-1 could suppress growth of breast cancer cells. Overexpression of DKK-1 was able to accelerate phosphorylation-dependent degradation of β-catenin and downregulate the expression of β-catenin, c-Myc, cyclin D1 and Survivin. Luciferase reporter gene assay demonstrated that Survivin could be regulated by β-catenin/ TCF4 pathway. Conclusion: We conclude that the downregulation of DKK-1 is responsible for the high proliferation ability of LM-MCF-7 breast cancer cells via losing control of Wnt/β-catenin signaling pathway, in which c-Myc, cyclinD1 and Survivin serve as essential downstream effectors. Our finding provides a new insight into the mechanism of breast cancer cell proliferation.

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Section: Discussionmentioning

confidence: 99%

Section: Rna Isolation and Rt-pcrmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Downregulation of Dickkopf-1 is responsible for high proliferation of breast cancer cells via losing control of Wnt/β-catenin signaling

et al. 2010

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“…The detailed 5-Bromo-20-deoxyuridine (BrdU) incorporation assay procedure was described as previously [13] . In brief, LM-MCF-7 and MCF-7 cells were seeded in 6-well culture plate and were grown overnight prior to treatment.…”

Section: Brdu Incorporation Assaymentioning

confidence: 99%

“…Cheng et al [9] identified a positive feedback loop in which Ras signaling promoted CD44v6 splicing, and CD44v6 then sustained late Ras signaling. Moreover, ERK occurs crosstalk with other pathways, including activated stress activated protein kinase (SAPK)-p38 [10] , phosphatidylinositol 3-kinase (PI3K) [11] , Wnt [12] and myosin light-chain kinase (MLCK) [13] . Thus, p-ERK1/2 may serve as a key hub in the network.…”

Section: Introductionmentioning

confidence: 99%

A novel positive feedback loop involving FASN/p-ERK1/2/5-LOX/LTB4/FASN sustains high growth of breast cancer cells

Zhao

et al. 2011

Acta Pharmacol Sin

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Aim:To investigate the endogenous signaling pathways associated with high proliferation potential of breast cancer cells. Methods: Breast cancer cell lines LM-MCF-7 and MCF-7 with high and low proliferation capability were used. The promoter activity of fatty acid synthase (FASN) was examined using luciferase reporter gene assay. The expression level of FASN mRNA was measured using RT-PCR and real time PCR, respectively. The level of leukotriene B4 (LTB4) was determined with ELISA. The expression levels of 5-lipoxygenase (5-LOX) was analyzed using RT-PCR and Western blot, respectively. 5-Bromo-20-deoxyuridine (BrdU) incorporation assay was used to study the proliferation of LM-MCF-7 and MCF-7 cells.

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Inhibition of fucosylation in human invasive ductal carcinoma reduces E‐selectin ligand expression, cell proliferation, and ERK1/2 and p38 MAPK activation

et al. 2018

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Breast cancer tissue overexpresses fucosylated glycans, such as sialyl‐Lewis X/A (sLeX /A), and α‐1,3/4‐fucosyltransferases (FUTs) in relation to increased disease progression and metastasis. These glycans in tumor circulating cells mediate binding to vascular E‐selectin, initiating tumor extravasation. However, their role in breast carcinogenesis is still unknown. Here, we aimed to define the contribution of the fucosylated structures, including sLeX /A, to cell adhesion, cell signaling, and cell proliferation in invasive ductal carcinomas (IDC), the most frequent type of breast cancer. We first analyzed expression of E‐selectin ligands in IDC tissue and established primary cell cultures from the tissue. We observed strong reactivity with E‐selectin and anti‐sLeX /A antibodies in both IDC tissue and cell lines, and expression of α‐1,3/4 FUTs FUT4, FUT5, FUT6, FUT10, and FUT11. To further assess the role of fucosylation in IDC biology, we immortalized a primary IDC cell line with human telomerase reverse transcriptase to create the ‘CF1_T cell line’. Treatment with 2‐fluorofucose (2‐FF), a fucosylation inhibitor, completely abrogated its sLeX /A expression and dramatically reduced adherence of CF1_T cells to E‐selectin under hemodynamic flow conditions. In addition, 2‐FF‐treated CF1_T cells showed a reduced migratory ability, as well as decreased cell proliferation rate. Notably, 2‐FF treatment lowered the growth factor expression of CF1_T cells, prominently for FGF2, vascular endothelial growth factor, and transforming growth factor beta, and negatively affected activation of signal‐regulating protein kinases 1 and 2 and p38 mitogen‐activated protein kinase signaling pathways. These data indicate that fucosylation licenses several malignant features of IDC, such as cell adhesion, migration, proliferation, and growth factor expression, contributing to tumor progression.

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Myosin light-chain kinase contributes to the proliferation and migration of breast cancer cells through cross-talk with activated ERK1/2

Cited by 69 publications

References 33 publications

Downregulation of Dickkopf-1 is responsible for high proliferation of breast cancer cells via losing control of Wnt/β-catenin signaling

Downregulation of Dickkopf-1 is responsible for high proliferation of breast cancer cells via losing control of Wnt/β-catenin signaling

A novel positive feedback loop involving FASN/p-ERK1/2/5-LOX/LTB4/FASN sustains high growth of breast cancer cells

Inhibition of fucosylation in human invasive ductal carcinoma reduces E‐selectin ligand expression, cell proliferation, and ERK1/2 and p38 MAPK activation

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