• Fascin-1
• Gefitinib
• STAT3
• Triple-negative breast cancer
• miR-221-3p

• Humans
• MicroRNAs/genetics
• MicroRNAs/metabolism
• Triple Negative Breast Neoplasms/drug therapy
• Triple Negative Breast Neoplasms/genetics
• Triple Negative Breast Neoplasms/pathology
• Triple Negative Breast Neoplasms/metabolism
• STAT3 Transcription Factor/metabolism
• STAT3 Transcription Factor/genetics
• Drug Resistance, Neoplasm/drug effects
• ErbB Receptors/metabolism
• ErbB Receptors/genetics
• Gefitinib/pharmacology
• Female
• Microfilament Proteins/metabolism
• Microfilament Proteins/genetics
• Cell Line, Tumor
• Carrier Proteins/metabolism
• Carrier Proteins/genetics
• Protein Kinase Inhibitors/pharmacology
• Gene Expression Regulation, Neoplastic/drug effects
• Neoplasm Proteins/metabolism
• Neoplasm Proteins/genetics
• Neoplasm Proteins/biosynthesis
• RNA, Neoplasm/genetics
• RNA, Neoplasm/metabolism
• RNA, Neoplasm/biosynthesis

• 81802660 National Natural Science Foundation of China

• Fascin-1
• Hepatocellular carcinoma
• Immunohistochemistry
• Intrahepatic cholangiocarcinoma
• Liver cancer

• Humans
• Liver Neoplasms/diagnosis
• Liver Neoplasms/metabolism
• Microfilament Proteins/metabolism
• Carrier Proteins/metabolism
• Male
• Female
• Middle Aged
• Carcinoma, Hepatocellular/diagnosis
• Carcinoma, Hepatocellular/metabolism
• Biomarkers, Tumor/metabolism
• Cholangiocarcinoma/diagnosis
• Cholangiocarcinoma/metabolism
• Aged
• Adult
• Liver Cirrhosis/diagnosis
• Liver Cirrhosis/metabolism
• Diagnosis, Differential
• Bile Duct Neoplasms/diagnosis
• Bile Duct Neoplasms/metabolism
• Bile Duct Neoplasms/pathology
• Sensitivity and Specificity

• 22-303 Science and Technology Project of Dongyang City
• LY24H160021 Natural Science Foundation of Zhejiang Province

• Cancer
• Cytoskeleton
• EMT
• Fascin
• Metastasis

• Female
• Humans
• beta Catenin/genetics
• Breast Neoplasms/pathology
• Cell Line, Tumor
• Cell Proliferation
• Neoplasm Invasiveness
• Phosphatidylinositol 3-Kinases/metabolism

• Beta-catenin
• Differentiation
• Fascin-1
• Hepatoblastoma

• Cancer
• Cellular retinoic acid bioavailability
• Oncogene
• Retinoic acid
• Retinoic acid-metabolizing enzyme CYP26
• Vitamin A

• Humans
• Retinoic Acid 4-Hydroxylase
• Vitamin A
• Feasibility Studies
• Tretinoin/metabolism
• Cytochrome P450 Family 26
• Neoplasms

Expression of the actin-bundling protein Fascin-1 (Fscn1) is largely restricted to neuronal cells and to activated dendritic cells (DCs). DCs are important inducers of (antitumor) immune responses. In tumor cells, de novo expression of Fscn-1 correlates with their invasive and metastatic activities. Pharmacological Fscn1 inhibitors, which are currently under clinical trials for tumor therapy, were demonstrated to counteract tumor metastasis. Within this study, we were interested in better understanding the effects of Fscn1 inhibitors on DCs and discovered that two distinct Fascin-1 inhibitors affect the immune-phenotype and T-cell stimulatory activity of DCs. Our results suggest that systemic application of Fscn1 inhibitors for tumor therapy may also modulate antitumor immune responses.

Background: Stimulated dendritic cells (DCs), which constitute the most potent population of antigen-presenting cells (APCs), express the actin-bundling protein Fascin-1 (Fscn1). In tumor cells, de novo expression of Fscn1 correlates with their invasive and metastatic properties. Therefore, Fscn1 inhibitors have been developed to serve as antitumor agents. In this study, we were interested in better understanding the impact of Fscn1 inhibitors on DCs. Methods: In parallel settings, murine spleen cells and bone-marrow-derived DCs (BMDCs) were stimulated with lipopolysaccharide in the presence of Fscn1 inhibitors (NP-G2-044 and BDP-13176). An analysis of surface expression of costimulatory and coinhibitory receptors, as well as cytokine production, was performed by flow cytometry. Cytoskeletal alterations were assessed by confocal microscopy. The effects on the interactions of BMDCs with antigen-specific T cells were monitored by time lapse microscopy. The T-cell stimulatory and polarizing capacity of BMDCs were measured in proliferation assays and cytokine studies. Results: Administration of Fscn1 inhibitors diminished Fscn1 expression and the formation of dendritic processes by stimulated BMDCs and elevated CD273 (PD-L2) expression. Fscn1 inhibition attenuated the interaction of DCs with antigen-specific T cells and concomitant T-cell proliferation. Conclusions: Systemic administration of Fscn1 inhibitors for tumor therapy may also modulate DC-induced antitumor immune responses.

• BDP-13176
• CD273
• CD86
• Fascin-1
• NP-G2-044
• dendritic cells

• antioxidant
• enzyme mechanism
• oxidative stress

Fascin, an actin-binding protein, is upregulated in different types of human cancers. It is reportedly responsible for increasing the invasive and metastatic ability of cancer cells by reducing cell–cell adhesions. This review provides a brief overview of fascin and its interactions with other genes and oncoviruses to induce the onset and progression of cancer.

Fascin is an actin-binding protein that is encoded by the FSCN1 gene (located on chromosome 7). It triggers membrane projections and stimulates cell motility in cancer cells. Fascin overexpression has been described in different types of human cancers in which its expression correlated with tumor growth, migration, invasion, and metastasis. Moreover, overexpression of fascin was found in oncovirus-infected cells, such as human papillomaviruses (HPVs) and Epstein-Barr virus (EBV), disrupting the cell–cell adhesion and enhancing cancer progression. Based on these findings, several studies reported fascin as a potential biomarker and a therapeutic target in various cancers. This review provides a brief overview of the FSCN1 role in various cancers with emphasis on gynecological malignancies. We also discuss fascin interactions with other genes and oncoviruses through which it might induce cancer development and progression.

• biomarker
• cervical cancer
• fascin
• gynecological cancer
• ovarian cancer

A key regulator of collective cell migrations, which drive development and cancer metastasis, is substrate stiffness. Increased substrate stiffness promotes migration and is controlled by Myosin. Using Drosophila border cell migration as a model of collective cell migration, we identify, for the first time, that the actin bundling protein Fascin limits Myosin activity in vivo. Loss of Fascin results in: increased activated Myosin on the border cells and their substrate, the nurse cells; decreased border cell Myosin dynamics; and increased nurse cell stiffness as measured by atomic force microscopy. Reducing Myosin restores on-time border cell migration in fascin mutant follicles. Further, Fascin’s actin bundling activity is required to limit Myosin activation. Surprisingly, we find that Fascin regulates Myosin activity in the border cells to control nurse cell stiffness to promote migration. Thus, these data shift the paradigm from a substrate stiffness-centric model of regulating migration, to uncover that collectively migrating cells play a critical role in controlling the mechanical properties of their substrate in order to promote their own migration. This understudied means of mechanical regulation of migration is likely conserved across contexts and organisms, as Fascin and Myosin are common regulators of cell migration.

• D. melanogaster
• Fascin
• border cells
• cell biology
• collective cell migration
• developmental biology
• mechanotransduction
• myosin
• stiffness

• il-6
• il-6rα
• fascin
• dendritic cells
• chemotaxis
• ccr7 internalization

• Animals
• Antibodies, Blocking/pharmacology
• Antigens, Differentiation/genetics
• Antigens, Differentiation/metabolism
• Cell Differentiation
• Cells, Cultured
• Chemotaxis
• Dendritic Cells/immunology
• Gene Expression Regulation
• Interleukin-6/metabolism
• Mice
• Mice, Knockout
• Microfilament Proteins/genetics
• Microfilament Proteins/metabolism
• Receptors, CCR7/metabolism
• Receptors, Interleukin-6/genetics
• Receptors, Interleukin-6/immunology
• Receptors, Interleukin-6/metabolism
• Receptors, Odorant/genetics
• Receptors, Odorant/metabolism
• Signal Transduction

• R03 AI099315 NIAID NIH HHS

• FSCN1
• biomarker
• cancer
• metastasis
• therapeutic target

Cell migration is an essential biological process that regulates both development and diseases, such as cancer metastasis. Therefore, understanding the factors that promote cell migration is crucial. One of the factors known to regulate cell migration is the actin-binding protein, Fascin. Fascin is typically thought to promote cell migration through bundling actin to form migratory structures such as filopodia and invadapodia. However, Fascin has many other functions in the cell that may contribute to cell migration. How these novel functions promote cell migration and are regulated is still not well understood. Here, we review the structure of Fascin, the many functions of Fascin and how they may promote cell migration, how Fascin is regulated, and Fascin’s role in diseases such as cancer metastasis.

Fascin, an actin-binding protein, regulates many developmental migrations and contributes to cancer metastasis. Specifically, Fascin promotes cell motility, invasion, and adhesion by forming filopodia and invadopodia through its canonical actin bundling function. In addition to bundling actin, Fascin has non-canonical roles in the cell that are thought to promote cell migration. These non-canonical functions include regulating the activity of other actin-binding proteins, binding to and regulating microtubules, mediating mechanotransduction to the nucleus via interaction with the Linker of the Nucleoskeleton and Cytoskeleton (LINC) Complex, and localizing to the nucleus to regulate nuclear actin, the nucleolus, and chromatin modifications. The many functions of Fascin must be coordinately regulated to control cell migration. While much remains to be learned about such mechanisms, Fascin is regulated by post-translational modifications, prostaglandin signaling, protein–protein interactions, and transcriptional means. Here, we review the structure of Fascin, the various functions of Fascin and how they contribute to cell migration, the mechanisms regulating Fascin, and how Fascin contributes to diseases, specifically cancer metastasis.

• LINC Complex
• actin
• cancer metastasis
• fascin
• mechanotransduction
• microtubules
• migration
• nuclear actin
• nucleolus
• prostaglandins

• P30 CA086862 NCI NIH HHS
• R01 GM116885 NIGMS NIH HHS
• R01GM116885 NIH HHS

• Fascin-1
• Glioblastoma multiforme
• Integrin-linked kinase (ILK)
• Invasion
• Matrix metalloproteinase 13 (MMP13)
• Migration
• ROCK1

• FSCN1
• Immunohistochemistry
• Methylation
• Promoter
• Thyroid cancer

• FRG1
• Immunohistochemistry
• angiogenesis
• cell invasion
• cell migration
• oncogenesis

• Breast cancer
• Fascin
• Invasion
• Linoleic acid
• Migration

Transforming growth factor-β–induced epithelial–mesenchymal transition (EMT) is one of the main causes of posterior capsular opacification (PCO) or secondary cataract; however, the signaling events involved in TGF-β–induced PCO have not been fully characterized. Here, we focus on examining the role of β-catenin/cyclic AMP response element–binding protein (CREB)-binding protein (CBP) and β-catenin/T-cell factor (TCF)-dependent signaling in regulating cytoskeletal dynamics during TGF-β–induced EMT in lens epithelial explants.

Rat lens epithelial explants were cultured in medium M199 in the absence of serum. Explants were treated with TGF-β2 in the presence or absence of the β-catenin/CBP interaction inhibitor, ICG-001, or the β-catenin/TCF interaction inhibitor, PNU-74654. Western blot and immunofluorescence experiments were carried out and analyzed.

An increase in the expression of fascin, an actin-bundling protein, was observed in the lens explants upon stimulation with TGF-β, and colocalized with F-actin filaments. Inhibition of β-catenin/CBP interactions, but not β-catenin/TCF interactions, led to a decrease in TGF-β–induced fascin and stress fiber formation, as well as a decrease in the expression of known markers of EMT, α-smooth muscle actin (α-SMA) and matrix metalloproteinase 9 (MMP9). In addition, inhibition of β-catenin/CBP–dependent signaling also prevented TGF-β–induced downregulation of epithelial cadherin (E-cadherin) in lens explants.

We show that β-catenin/CBP–dependent signaling regulates fascin, MMP9, and α-SMA expression during TGF-β–induced EMT. We demonstrate that β-catenin/CBP–dependent signaling is crucial for TGF-β–induced EMT in the lens.

p53 mutation is known to contribute to cancer progression. Fascin is an actin-bundling protein and has been recently identified to promote cancer cell migration and invasion through its role in formation of cellular protrusions such as filopodia and invadopodia. However, the relationship between p53 and Fascin is not understood. Here, we have found a new link between them. In colorectal adenocarcinomas, p53 mutation correlated with high NF-κB, Fascin and low E-cadherin expression. Moreover, this expression profile was shown to contribute to poor overall survival in patients with colorectal cancer. Wild-type p53 could inhibit NF-κB activity that repressed the expression of Fascin and cancer cell invasiveness. In contrast, in p53-deficient primary cultured cells, NF-κB activity was enhanced and then activation of NF-κB increased the expression of Fascin. In further analysis, we showed that NF-κB was a key determinant for p53 deletion-stimulated Fascin expression. Inhibition of NF-κB /p65 expression by pharmacological compound or p65 siRNA suppressed Fascin activity in p53-deficient cells. Moreover, restoration of p53 expression decreased the activation of Fascin through suppression of the NF-κB pathway. Taken together, these data suggest that a negative-feedback loop exists, whereby p53 can suppress colorectal cancer cell invasion by inhibiting the NF-κB-mediated activation of Fascin.

• Fascin
• NF-κB
• cancer
• cell invasion
• p53

Although MUC13, a transmembrane mucin, is aberrantly expressed in pancreatic ductal adenocarcinoma (PDAC) and generally correlates with increased expression of HER2, the underlying mechanism remains poorly understood. Herein, we found that MUC13 co-localizes and interacts with HER2 in PDAC cells (reciprocal co-immunoprecipitation, immunofluorescence, proximity ligation, co-capping assays) and tissues (immunohistofluorescence). The results from this study demonstrate that MUC13 functionally interacts and activates HER2 at p1248 in PDAC cells, leading to stimulation of HER2 signaling cascade including, ERK1/2, FAK, AKT and PAK1 as well as regulation of the growth, cytoskeleton remodeling and motility and invasion of PDAC cells - all collectively contributing to PDAC progression. Interestingly, all of these phenotypic effects of MUC13-HER2 co-localization could be effectively compromised by depleting MUC13 and mediated by the first and second EGF-like domains of MUC13. Further, MUC13-HER2 co-localization also holds true in PDAC tissues with a strong functional correlation with events contributing to increased degree of disorder and cancer aggressiveness. In brief, findings presented here provide compelling evidence of a functional ramification of MUC13-HER2: this interaction could be potentially exploited for targeted therapeutics in a subset of patients harboring an aggressive form of PDAC.

• carcinomas
• fascin1
• prognostic marker

• Animals
• Carcinoma/metabolism
• Carcinoma/pathology
• Cell Movement/physiology
• Humans
• Microfilament Proteins/metabolism
• Neoplasm Invasiveness/pathology
• Prognosis

• 15673 Cancer Research UK

• ATL
• Fascin
• HTLV-1
• NF‐kappa B (NF‐KB)
• Oncogene
• PP2
• Promoter
• Tax
• Transcription regulation
• Tumor virus

• E-cadherin
• cholangiocarcinoma
• fascin
• invasion
• migration
• proliferation

• Body axis elongation
• Brachyury
• Epithelial–mesenchymal transition
• Migration
• Mouse embryo
• Serum Response Factor (SRF)

The actin-bundling protein Fascin (FSCN1) is a tumor marker that is highly expressed in numerous types of cancer including lymphomas and is important for migration and metastasis of tumor cells. Fascin has also been detected in B lymphocytes that are freshly-infected with Epstein-Barr virus (EBV), however, both the inducers and the mechanisms of Fascin upregulation are still unclear.

Here we show that the EBV-encoded oncoprotein latent membrane protein 1 (LMP1), a potent regulator of cellular signaling and transformation, is sufficient to induce both Fascin mRNA and protein in lymphocytes. Fascin expression is mainly regulated by LMP1 via the C-terminal activation region 2 (CTAR2). Block of canonical NF-κB signaling using a chemical inhibitor of IκB kinase β (IKKβ) or cotransfection of a dominant-negative inhibitor of IκBα (NFKBIA) reduced not only expression of p100, a classical target of the canonical NF-κB-pathway, but also LMP1-induced Fascin expression. Furthermore, chemical inhibition of IKKβ reduced both Fascin mRNA and protein levels in EBV-transformed lymphoblastoid cell lines, indicating that canonical NF-κB signaling is required for LMP1-mediated regulation of Fascin both in transfected and transformed lymphocytes. Beyond that, chemical inhibition of IKKβ significantly reduced invasive migration of EBV-transformed lymphoblastoid cells through extracellular matrix. Transient transfection experiments revealed that Fascin contributed to LMP1-mediated enhancement of invasive migration through extracellular matrix. While LMP1 enhanced the number of invaded cells, functional knockdown of Fascin by two different small hairpin RNAs resulted in significant reduction of invaded, non-attached cells.

Thus, our data show that LMP1-mediated upregulation of Fascin depends on NF-κB and both NF-κB and Fascin contribute to invasive migration of LMP1-expressing lymphocytes.

The virtual slide(s) for this article can be found here: http://www.diagnosticpathology.diagnomx.eu/vs/1421167695121127.

• Biomarkers, Tumor/genetics
• Carcinoma, Squamous Cell/genetics
• Carrier Proteins/antagonists & inhibitors
• Carrier Proteins/genetics
• Computational Biology
• Esophageal Neoplasms/genetics
• Gene Expression Profiling
• Gene Expression Regulation, Neoplastic
• Humans
• Microfilament Proteins/antagonists & inhibitors
• Microfilament Proteins/genetics
• Oligonucleotide Array Sequence Analysis
• RNA, Messenger/genetics
• RNA, Small Interfering/genetics
• Real-Time Polymerase Chain Reaction
• Reverse Transcriptase Polymerase Chain Reaction

Invasion and metastasis are major reasons for poor prognosis of digestive system carcinomas. Motility and migratory capacity are important in contributing to tumor cell invasion and metastasis. Fascin-1 is a globular actin crosslinking protein that can form parallel actin bundles in cell protrusions and is involved in cell adhesion, movement, and signal transduction. In vitro up-regulation of Fascin-1 can increase migration and invasion capacity of cells, while down-regulation of Fascin-1 can decrease migration and invasion capacity of cells. Many studies show that up-regulation of Fascin-1 expression is significantly associated with worse prognosis, poorer differentiation, advanced TNM stage, lymph node metastasis, and distant metastasis in patients with digestive system carcinomas. Therefore, Fascin-1 may have prognostic value as an early biomarker for more aggressive digestive system carcinomas and may be a potential therapeutic target for tumor invasion and metastasis.

• Fascin
• Invasion
• Metastasis
• Carcinoma
• Digestive system

miRNAs, endogenous oligonucleotide RNAs, play an important role in mammary gland carcinogenesis and tumor progression. Detection of their expression and investigation of their functions could lead to discovery of novel biomarkers for breast cancer.

In situ hybridization was used to detect miR-133a expression in formalin-fixed paraffin-embedded breast surgical specimens from 26 benign, 34 pericancerously normal and 90 cancerous tissues. qRT-PCR was performed to assess miR-133a levels in 6 breast cell lines and 10 benign and 18 cancerous fresh breast tissue specimens. Cell viability, migration, and invasion assays were used to determine the role of miR-133a in regulation of breast cancer cell growth, migration, and invasion, respectively. Luciferase assay was performed to assess miR-133a binding to FSCN1 gene.

Expression of miR-133a was reduced from normal through benign to cancerous breast tissues. Expression of miR-133a was also low in breast cancer cell lines. The reduced miR-133a expression was associated with lymph nodes metastasis, high clinical stages, and shorter relapse-free survivals of patients with breast cancer. Furthermore, transfection of miR-133a oligonucleotides slightly inhibited growth but significantly decreased migration and invasion capacity of breast cancer cells, compared with negative controls, whereas knockdown of miR-133a expression induced breast cancer cell migration and invasion. In addition, we identified a putative miR-133a binding site in the 3'-untranslated region (UTR) of Fascin1 (FSCN1) gene using an online bioinformatical tool. We found that miR-133a transfection significantly reduced expression of FSCN1 mRNA and protein. The luciferase reporter assay confirmed that FSCN1 was the direct target gene of miR-133a.

miR-133a expression was lost in breast cancer tissues, loss of which was associated with lymph nodes metastasis, high clinical stages and shorter relapse-free survivals of patients with breast cancer. Functionally, miR-133a can suppress tumor cell invasion and migration and targeted the expression of FSCN1. Future study will verify whether detection of miR-133a expression can served as a novel biomarker for breast cancer progression and patient prognosis.

• fascin
• cell migration
• invasion
• metastasis
• oscc

• Actins/ultrastructure
• Animals
• Blotting, Western
• Carcinoma, Squamous Cell/metabolism
• Carcinoma, Squamous Cell/pathology
• Carrier Proteins/metabolism
• Cell Movement/physiology
• Cell Proliferation
• Cytoskeleton/ultrastructure
• Disease Progression
• Humans
• Immunohistochemistry
• Matrix Metalloproteinase 2/metabolism
• Mice
• Mice, SCID
• Microfilament Proteins/metabolism
• Mouth Neoplasms/metabolism
• Mouth Neoplasms/pathology
• Neoplasm Invasiveness/pathology
• Neoplasm Proteins/metabolism
• Tumor Cells, Cultured
• Wound Healing/physiology

AIM: To explore the role of actin-bundling protein, fascin during the progression of pancreatic cancer.

METHODS: The plasmid expressing human fascin-1 was stably transfected into the pancreatic cancer cell line MIA PaCa-2. The proliferation, cell cycle, motility, scattering, invasiveness and organization of the actin filament system in fascin-transfected MIA PaCa-2 cells and control non-transfected cells were determined.

RESULTS: Heterogeneous overexpression of fascin markedly enhanced the motility, scattering, and invasiveness of MIA PaCa-2 cells. However, overexpression of fascin had minimal effect on MIA PaCa-2 cell proliferation and cell cycle. In addition, cell morphology and organization of the actin filament system were distinctly altered in fascin overexpressed cells. When transplanted into BALB/c-nu mice, fascin-transfected pancreatic cancer cells developed solid tumors at a slightly slower rate, but these tumors displayed more aggressive behavior in comparison with control tumors.

CONCLUSION: Fascin promotes pancreatic cancer cell migration, invasion and scattering, thus contributes to the aggressive behavior of pancreatic cancer cells.

• Fascin
• Invasiveness
• Motility
• Pancreatic cancer

• Animals
• Antibodies, Monoclonal/immunology
• Cell Line, Tumor
• Cell Movement
• Cell Proliferation
• Cell Transformation, Neoplastic
• Extracellular Signal-Regulated MAP Kinases/metabolism
• Humans
• Mice
• Mice, Nude
• Mucins/immunology
• Mucins/metabolism
• Neoplasm Invasiveness
• Neoplasm Transplantation
• Pancreatic Neoplasms/metabolism
• RNA Interference
• RNA, Small Interfering
• Receptor, ErbB-2/metabolism
• S100 Calcium-Binding Protein A4
• S100 Proteins/metabolism
• Signal Transduction/physiology
• Tumor Suppressor Protein p53/metabolism
• p21-Activated Kinases/metabolism

• P20RR024219 NCRR NIH HHS
• PC073887 NCI NIH HHS
• U01 CA162106 NCI NIH HHS
• P20 RR024219 NCRR NIH HHS
• P20 RR17662 NCRR NIH HHS
• PC073643 NCI NIH HHS
• R01 CA142736 NCI NIH HHS
• P20 RR017662 NCRR NIH HHS

• epithelial cell
• fascin
• villin
• actin bundling
• pip₂ binding
• collective cell migration
• microvilli
• emt
• metastases

• Actins/chemistry
• Actins/metabolism
• Carrier Proteins/chemistry
• Carrier Proteins/metabolism
• Cell Movement
• Epithelial Cells/metabolism
• Humans
• Microfilament Proteins/chemistry
• Microfilament Proteins/genetics
• Microfilament Proteins/metabolism
• Microvilli/chemistry
• Microvilli/metabolism
• Models, Molecular
• Neoplasm Metastasis
• Pseudopodia/chemistry
• Pseudopodia/genetics
• Pseudopodia/metabolism

• R01 DK054755 NIDDK NIH HHS
• DK-54755 NIDDK NIH HHS

• fascin
• sp1
• egf
• erk1/2
• esophageal squamous cell carcinoma
• fscn1

• Carcinoma, Squamous Cell/genetics
• Carcinoma, Squamous Cell/pathology
• Carrier Proteins
• Down-Regulation/drug effects
• Epidermal Growth Factor/genetics
• Epidermal Growth Factor/metabolism
• Epidermal Growth Factor/pharmacology
• Esophageal Neoplasms/genetics
• Extracellular Signal-Regulated MAP Kinases/genetics
• Extracellular Signal-Regulated MAP Kinases/metabolism
• Humans
• Microfilament Proteins
• Mitogen-Activated Protein Kinases/genetics
• Mitogen-Activated Protein Kinases/metabolism
• Phosphorylation
• Proteins/metabolism
• Signal Transduction/drug effects
• Signal Transduction/genetics