Oral squamous cell carcinoma (OSCC) is associated with a high potential of tumor recurrence and metastasis, leading to poor prognosis. Cell motility is an important factor in the progression and metastasis of cancers. Recently, Fascin has been linked to tumor progression by induction of cell motility. However, the precise roles of Fascin in OSCC have not been elucidated clearly. The aim of this study was to analyze the roles of Fascin in OSCC progression using OSCC clinical samples. We demonstrated that Fascin over-expression was found in OSCC clinical samples and its expression was significantly associated with nodal metastasis (p=0.027), tumor recurrence (p<0.001) and poor patients' overall survival (p=0.013). Consistently, Fascin proteins were detected in all OSCC cell lines with the expression level corresponding to the invasion ability. To specifically investigate the mechanism of Fascin in OSCC, we examined the E-cadherin expression in the same set of OSCC specimens. Fascin was negatively correlated with E-cadherin expression (p=0.018, r=-0.513). In conclusion, our findings suggested that Fascin over-expression might enhance OSCC aggressiveness, possibly by interacting with E-cadherin expression.
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http://dx.doi.org/10.1016/j.canlet.2007.03.017 | DOI Listing |
Am J Med Sci
March 2020
Department of General Pathomorphology, Medical University of Bialystok, Bialystok, Poland.
Background: Fascin-1 and actinin-4 are involved in key processes of tumor cell adhesion, migration and metastasis. Actinin-4 plays an important role in promotion of cell proliferation, whereas fascin-1 regulates cellular motility. Its over-expression leads to the loss of cell adhesion and metastasis.
View Article and Find Full Text PDFCancer Manag Res
July 2019
Department of Obstetrics and Gynecology, The Second Affiliated Hospital of Wenzhou Medical University, Wenzhou 325027, People's Republic of China.
Objective: To investigate dynein light chain Tctex-type 3 (DYNLT3) protein expression in ovarian epithelial lesions and explore the effects and related mechanisms of DYNLT3 in terms of the biological behavior of ovarian cancer.
Materials And Methods: Initially, expression of the DYNLT3 protein in ovarian epithelial lesions was detected by immunohistochemical staining, and the prognostic value of DYNLT3 mRNA expression in ovarian cancer patients was assessed using the Kaplan-Meier plotter database. Then, the mRNA and protein expression of DYNLT3 in IOSE80 normal ovarian epithelial cells and SKOV3 ovarian cancer cells was evaluated by quantitative real-time polymerase chain reaction and Western blotting respectively, and the proliferation, apoptosis, migration and invasion of SKOV3 cells after DYNLT3 over-expression and under-expression were investigated by CCK-8 assays and immunofluorescence staining, flow cytometry, wound healing assays and Transwell invasion assays, respectively.
Med J Islam Repub Iran
December 2018
Department of Virology, School of Medicine, Iran University of Medical Sciences, Tehran, Iran.
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.
View Article and Find Full Text PDFAnn Diagn Pathol
October 2017
Scientist-D, Institute of Life Sciences, Bhubaneswar 751023, India.
Introduction: Oral squamous cell carcinoma (OSCC) has an aggressive behaviour with high incidence of nodal metastasis, even in the early stages, leading to poor prognosis. For progression and metastasis of cancers, the dominant element considered is cell motility. Fascin, an actin-binding protein has emerged as a protein of general importance for a diverse set of cell protrusions with functions in cell adhesion, cell interactions, and cell migration.
View Article and Find Full Text PDFEur J Pharmacol
December 2015
Key Laboratory of Applied Pharmacology in Universities of Sh andong, Department of Pharmacology, School of Pharmacy, Weifang Medical University, Weifang 261053, Shandong, China. Electronic address:
Leucine aminopeptidase 3 (LAP3) is a cell surface aminopeptidase that catalyzes the hydrolysis of leucine residues from the amino termini of protein or peptide substrates. The over-expression of LAP3 correlates with prognosis and malignant development of several human cell carcinomas. However, the molecular mechanism remains unknown.
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