Abstract:Background/Aims: Epithelial-mesenchymal transition (EMT) is one of the key mechanisms mediating cancer progression. Snail1 has a pivotal role in the regulation of EMT, involving the loss of E-cadherin and concomitant upregulation of vimentin, among other biomarkers. We have found FSCN1 promoted EMT in ovarian cancer cells, but the precise mechanism of FSCN1 in EMT process has not been clearly elucidated. Methods: The levels of FSCN1 and snail1 were determined in epithelial ovarian cancer(EOC) specimen and in o… Show more
“…Later, nesprin‐2 was found to bind to FSCN1 and play a key role in nuclear movement and deformation . Moreover, two serine/threonine kinases (mammalian STE20‐like 1/2; [MST1/2]) and an epithelial‐mesenchymal transition (EMT)‐promoting factor (Snail) were found physiologically interact with FSCN1, and the interaction serves to modulate cancer progression …”
Fascin actin-bundling protein 1 (FSCN1) is an evolutionarily conserved actinbundling protein that plays a critical role in cell migration, motility, adhesion, and cellular interactions. Although multiple clinical studies have implicated the expression of FSCN1 in laryngeal squamous cell carcinoma (LSCC) progression, the precise mechanism of FSCN1 in the process has not been clearly elucidated. To define FSCN1 function, we characterized FSCN1-interacting proteins in LSCC cells by immunoprecipitation followed by mass spectrometry (MS). After data filtering, 119 proteins with expression in both the Hep-2 and TU-177 cell samples were identified as FSCN1-interacting partners. With in-depth bioinformatics analysis, we linked FSCN1 to critical cellular processes including cell adhesion, glycolysis/gluconeogenesis, regulation of protein ubiquitination, ribosomal RNA processing, and small molecule metabolism. We discuss the interactions between FSCN1 and some of the newly validated partners. The identification of these potential partners of FSCN1 expands our knowledge of the FSCN1 interactome and provides a valuable resource for understanding the functions of this protein in LSCC progression.
“…Later, nesprin‐2 was found to bind to FSCN1 and play a key role in nuclear movement and deformation . Moreover, two serine/threonine kinases (mammalian STE20‐like 1/2; [MST1/2]) and an epithelial‐mesenchymal transition (EMT)‐promoting factor (Snail) were found physiologically interact with FSCN1, and the interaction serves to modulate cancer progression …”
Fascin actin-bundling protein 1 (FSCN1) is an evolutionarily conserved actinbundling protein that plays a critical role in cell migration, motility, adhesion, and cellular interactions. Although multiple clinical studies have implicated the expression of FSCN1 in laryngeal squamous cell carcinoma (LSCC) progression, the precise mechanism of FSCN1 in the process has not been clearly elucidated. To define FSCN1 function, we characterized FSCN1-interacting proteins in LSCC cells by immunoprecipitation followed by mass spectrometry (MS). After data filtering, 119 proteins with expression in both the Hep-2 and TU-177 cell samples were identified as FSCN1-interacting partners. With in-depth bioinformatics analysis, we linked FSCN1 to critical cellular processes including cell adhesion, glycolysis/gluconeogenesis, regulation of protein ubiquitination, ribosomal RNA processing, and small molecule metabolism. We discuss the interactions between FSCN1 and some of the newly validated partners. The identification of these potential partners of FSCN1 expands our knowledge of the FSCN1 interactome and provides a valuable resource for understanding the functions of this protein in LSCC progression.
“…The process of epithelial-mesenchymal transition (EMT) confers stem cell properties that involve molecular changes, increased cell motility, and decreased cell-cell junctions and adhesion [28–30]. Cancer stem cells represent undifferentiated cancer cells, and EMT maintains stem cell features.…”
Background
The spalt-like transcription factor 1 (SALL1) gene is a member of the Krüppel-associated box-containing zinc finger proteins (KRAB-ZFPs) and has been shown to modulate the onset and progression of human tumors. This study aimed to investigate the regulatory effects and mechanisms of SALL1 gene expression in human glioblastoma and glioma cells and tissue samples from patients with cerebral glioma.
Material/Methods
The human glioblastoma cell lines, LN229, U87-MG, U-251, U343, and the Hs683 glioma cell line were studied. The cell counting kit-8 (CCK-8) assay, cell cycle assay, wound-healing assay, transwell assay, Western blot, and quantitative real-time polymerase chain reaction (qRT-PCR) were used to evaluate cell proliferation, cell migration, and the cell cycle and expression of SALL1. Expression of SALL1 mRNA in 120 samples of cerebral glioma and 20 samples of normal brain were studied. Overall survival data from patients with cerebral glioma were analyzed.
Results
SALL1 expression was down-regulated in human glioblastoma and glioma cells and in cerebral glioma tissues. Down-regulation of SALL1 expression was associated with reduced overall survival. Overexpression of SALL1 was associated with inhibition of cell proliferation associated with cell cycle arrest at the G0/G1 phase. SALL1 inhibited cell migration by preventing epithelial-mesenchymal transition (EMT) and down-regulating the expression of stem cell markers. Reduced levels of β-catenin and downregulation of c-Myc and cyclin D1 and upregulation of p21and p27 expression were associated with SALL1 expression.
Conclusions
In human glioblastoma cells and cerebral glioma tissues, SALL1 acted as a tumor suppressor gene by inhibiting Wnt/β-catenin signaling.
“…The absence or very low expression of fascin protein has usually been reported in normal epithelial cells (20). However, fascin overexpression has been detected in several human cancers, such as breast (21), ovarian (22), esophagus (23), stomach (24), pancreatic (25), colon (26), skin (6) and lung (27) tumors. In this context, up-regulation of fascin expression has clinical significance and poor prognosis.…”
Background:
Human papilloma virus (HPV) is involved in development of almost all cervical cancers, mainly through the subversion of cellular mechanisms of growth control. Fascin plays central role in subsequent cell transformation events. Fascin mediates stabilization of parallel actin bundles where cellular protrusions are formed; this represents primary stages of cell migration and metastasis. Immunohistochemical assays have shown up-regulation of fascin expression in many epithelial and non-epithelial neoplasms. Therefore, the aim of this study was to investigate HPV infection and fascin expression in samples of cervical cancer.
Methods:
Of 66 patients with confirmed SCC, formalin-fixed specimens, embedded in paraffin blocks were evaluated for HPV infection with nested multiplex polymerase chain reaction (NM-PCR) and for fascin expression with immunohistochemical assays. Statistical analysis was performed using Wilcoxon rank-sum test and SPSS software. A p<0.05 was considered for statistical significance.
Results:
Of 66 samples, 52 (78.7%) were found positive for HPV infection and fascin over-expression was shown in all squamous cell carcinoma samples.
Conclusion:
This study showed fascin overexpression in squamous cell carcinoma of the cervix which might be involved in metastasis of cancers induced by some types of HPV, hypothetically through attenuation of inter-cellular adhesions, and induction of cell motility
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