Journal: Cancer Research and Treatment : Official Journal of Korean Cancer Association

Article Title: Long Non-coding RNA HOXA11 Antisense Promotes Cell Proliferation and Invasion and Predicts Patient Prognosis in Serous Ovarian Cancer

doi: 10.4143/crt.2016.263

Figure Lengend Snippet: Knockdown of HOXA11 antisense ( HOXA11as ) inhibits serous ovarian cancer cell proliferation. (A) Expression of HOXA11as in human ovarian surface epithelial cell line (HOSE) and six ovarian cancer cell lines determined by quantitative real time polymerase chain reaction (qRT-PCR). (B) Knockdown efficiency was determined by qRT-PCR analysis in OVCA429 and SKOV3 cells. Cells were transfected with HOXA11as -specific siRNA (siHOXA11as) and negative control siRNA (siNC). (C, D) Knockdown of HOXA11as significantly reduced cell proliferation in OVCA429 and SKOV3 cells as determined by 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay. Bars indicate mean±standard deviation of three independent experiments performed in triplicate. * p < 0.05 vs. siNC. siHOXA11as, HOXA11as -specific siRNA.

Article Snippet: Normal human ovarian surface epithelial (HOSE) cells were purchased from ScienCell Research Laboratories (San Diego, CA).

Techniques: Knockdown, Expressing, Real-time Polymerase Chain Reaction, Quantitative RT-PCR, Transfection, Negative Control, MTT Assay, Standard Deviation

Journal: BMC Cancer

Article Title: N-glycosylation of ICAM-2 is required for ICAM-2-mediated complete suppression of metastatic potential of SK-N-AS neuroblastoma cells

doi: 10.1186/1471-2407-13-261

Figure Lengend Snippet: ICAM-2 WT and variants co-precipitated with α-actinin. A ) IP/IB experiments with control cell lines demonstrate the expected association of ICAM-2, α-actinin and actin in lysates from SK-N-ASpIRES.ICAM-2 cells (labeled as WT), but not SK-N-ASpIRESneo cells (neo). Results for these control cell lines were published previously . B ) ICAM-2 glycosylation site variants associated simultaneously with α-actinin and actin. Immunoprecipitations (IP) were performed using whole cell lysates and a mouse monoclonal antibody to α-actinin (MAB1682, Millipore). Following protein separation by electrophoresis, immunoblots (IB) were performed with antibodies to α-actinin (sc-7454, Santa Cruz Biotech), ICAM-2 (AF244, R&D Systems), or actin (4968, Cell Signaling). The presence of ICAM-2 WT and variants in each preparation was confirmed by immunoblot analysis of input preparations (a representative blot is shown in Figure C) and also by immunoblot analysis of the proteins remaining in the supernatant following precipitation (not shown), to confirm the presence of sufficient/excess ICAM-2 protein or variant in each preparation used for immunoprecipitation experiments.

Article Snippet: Antibodies used for immunoblots (IB) for ICAM-2, α-actinin, and actin were AF244 (R&D Systems, Minneapolis, MN) and sc-1512 (Santa Cruz Biotech, Santa Cruz, CA), 4968 (Cell Signaling Technology, Danvers, MA), and A5316 (Sigma-Aldrich, St. Louis, MO), respectively.

Techniques: Control, Labeling, Glycoproteomics, Electrophoresis, Western Blot, Variant Assay, Immunoprecipitation