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A, c ?200; b, d ?Quadri et al. BMC Cancer (2017) 17:Page 5 ofFig. 3 Photomicrographs of pancreatic cancer tissue microarray (TMA) cores of p-ERK immunohistochemical staining: a no staining for p-ERK (score 0); b weak p-ERK (score 1+) staining; c moderate p-ERK (score 2+) staining; d strong p-ERK (score 3+) staining. Magnification: a-d: ?70 cases as 2+ (58.3 ), and 16 cases as 3+ (13.3 ) (Fig. 5a).
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Ss microarray chip platforms when hybridizing the same sample RNA [32]. Additionally,Toussaint et al. Molecular Cancer 2012, 11:32 http://www.molecular-cancer.com/content/11/1/Page 8 ofFigure 4 (A) Galectin-1 transfection does not alter U87MG attachment to fibronectin. Attachment to fibronectin-coated 96-well plates was quantitated with an MTT assay with and without a media change in the middle of
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Rbance values of the other wells. Average corrected absorbance was compared between transfectant and parental cells, using a t-test.ECM attachment assaysThe U87MG human glioma cell line was kept in tissue culture in DMEM (Cellgro Mediatech, Inc.), with 10 fetal bovine serum, and penicillin/streptomycin. For transfection, 2.5x106 cells were plated overnight on a 100 mm round dish. Cells were trans
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Galectin-1 transfectants. A population of GFP-sorted cells (the "Gal-1" bars in Figure 4A) was compared to its parental counterpart. The number of metabolically-active cells attached to fibronectin was no different between the two lines at eight hours. Changing the media at four hours reduced the number of cells left for labeling, but the effect was equal in both groups, suggesting a similar rate
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Ase) makes it a resource for identification, as well as preclinical targeting, of novel mediators of glioma invasion. Galectin-1 was identified in this manner, and has proven in vitro and in vivo to be important in the migration and invasion of glioblastoma cells. Previous work suggests an even greater role of galectin-1 in GBM neoangiogenesis, chemo- and radioresistence, and immune privilege. Tar

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