Open Access Highly Accessed Research article

Fascin overexpression promotes neoplastic progression in oral squamous cell carcinoma

Hunain Alam1, Amruta V Bhate1, Prakash Gangadaran1, Sharda S Sawant1, Shimul Salot1, Lalit Sehgal1, Prerana P Dange1, Devendra A Chaukar2, Anil K D'cruz2, Sadhna Kannanl1, Rajiv Gude1, Shubhada Kane3, Sorab N Dalal1 and Milind M Vaidya1*

Author Affiliations

1 Advanced Centre for Treatment Research and Education in Cancer Tata Memorial Centre (ACTREC), Kharghar, Navi Mumbai, India-410210

2 Oral Surgery, Head and Neck Unit, Tata Memorial Hospital, Parel, Mumbai, India-400012

3 Dept. of Pathology, Tata Memorial Hospital, Parel, Mumbai, India-400012

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BMC Cancer 2012, 12:32  doi:10.1186/1471-2407-12-32

Published: 20 January 2012

Additional files

Additional file 1:

Table S1. Clinico-pathological parameters of the OSCC patients.

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Additional file 2:

Figure S1. (A) Cell morphology (shape) of fascin-overexpressed and vector control clone analyzed by phase contrast microscopy. Scale bar: 100 μm. (B) Western blot analysis of fascin-overexpressed (AW-Fascin-1 and AW-Fascin-2) and vector control clones (AW-GFP-Cont) with antibody to vimentin. β-actin was used as a loading control. (C) Representative confocal images of b-catenin and E-cadherin staining in stable AW-Fascin-1, AW-Fascin-2 and AW-GFP-Cont clones. Scale bars: 10 μm. (D) Representative image of the size and number of colonies formed in soft agar of the indicated clones. Scale bar: 100 μm.

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Additional file 3:

Table S2. The Fascin overexpressed clones show a decrease in cell-cell adhesion. Cell adhesion was measured by the hanging drop assay as described. 2 × 104 cells of the indicated clones were resuspended in 35 μl of complete medium on the lid of a 24 well dish. 16 h later the cells were fixed and the number and area of aggregates in fifteen fields was measured. The numbers of aggregates of different sizes are shown.

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Additional file 4:

Figure S2. Representative images of haematoxylin and eosin along with immunohistochemical staining with antibodies against fascin, K8 and β4-integrin on paraffin embedded sections of human in oral tumors (A) and non malignant tissues (B). Sections were counter stained with eosin (Magnification: 200×).

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Additional file 5:

Figure 3. (A) Representative images of immunofluorescence staining with antibodies against β4-integrin and K1 of paraffin embedded sections of non malignant oral tissues. Sections were counter stained with DAPI. Scale bar: 50 μm. (B) Representative images of immunofluoroscence staining with antibodies against fascin, β4-integrin and K14 of paraffin embedded sections of human oral tumors and fascin IF stainging in non malignant oral tissues. Sections were counter stained with DAPI. Scale bar: 50 μm.

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Additional file 6:

Figure S4. Representative images of IHC staining with antibodies against fascin on paraffin embedded sections o f primary tumor and lymph node metastasized tumor of human OSCC tissues. Sections were counter stained with eosin (Magnification: 200×).

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Additional file 7:

Table S3. Correlations of fascin in combination with K8 and β4-integrin expression with clinico-pathological parameters of the OSCC patients.

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Additional file 8:

Figure R1. (A and B)Western blot analysis of fascin-overexpressed (AW-Fascin-1 and AW-Fascin-2) and vector control clones (AW-GFP-Cont) with antibodies to α6-integrin, β4-integrin and pFAK. β-actin and FAK were used as loading control respectively. Densitometric analysis for the quantification of level of α6-integrin, β4-integrin and pFAK obtained from western blot of the indicated clones. (C and D) Western blot analysis of fascin-overexpressed (AW-Fascin-1 and AW-Fascin-2) and vector control clones (AW-GFP-Cont) with antibodies to fascin. β-actin was used as a loading control. Quantification of levels of fascin in fascin-overexpressed (AW-Fascin-1 and AW-Fascin-2) and vector control (AW-GFP-Cont) clones using densitometric analysis.

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