Genes differentially expressed in MBP-1 depleted HFF.

<p>Genes differentially expressed in MBP-1 depleted HFF.</p

Knockdown of MBP-1 in human foreskin fibroblasts induces cell proliferation.

<p>Panel A: Normal human foreskin fibroblasts were transfected with MBP-1 specific shRNA or control scrambled shRNA and selected with neomycin for 3 weeks. Colonies were pooled and examined for endogenous expression of MBP-1 by Western blot analysis using a specific antibody to MBP-1. Densitometric analysis of MBP-1/tubulin was performed using Image Quant Software (Amersham, ME). Panel B: Knockdown of MBP-1 inhibits HFF proliferation. Cells were plated after selection, and counted at different time points by trypan blue exclusion method. Panel C: MBP-1 knockdown in HFF results in accumulation of HFF at the G1 phase. Asynchronized HFF-control and HFF-MBPsi-4 were harvested fixed and stained with propidium iodide. DNA content was analyzed by flow cytometry. Results are represented as percent of cell population in G1, S, and G2/M phases of the cell cycle. Results are presented together with standard errors from three independent experiments.</p

PODs accumulate during premature senescence in MBP-1 knockdown HFF.

<p>PML localization in HFF-control (Panel A) or HFF-MBPsi-4 (Panel B) was determined by indirect immunofluorescence using the PML monoclonal antibody.</p

MBP-1 knockdown in HFF modulates expression of cyclins.

<p>Panel A: Expression of cyclins in control and MBP-1 knockdown HFF. Lysates prepared from cells were subjected to Western blot analysis using indicated antibodies. Knockdown of MBP-1 enhanced cyclin D1 expression and cyclin E and reduced cyclin A expression in HFF-control. Panel B: Time-dependent elevation of cyclin D1 expression in MBP-1 knockdown HFF as compared to control HFF. Cells were synchronized by serum-starvation and lysates were prepared at different time points as indicated following serum stimulation. Cell lysates were examined for the expression of cyclin D1 by Western blot analysis using specific antibody. Protein load was normalized and determined level of cyclin D1 by densitometric analysis. Arbitrary unit was chosen to represent relative cyclin D1 expression. Results are presented together with standard errors from three independent experiments.</p

MBP-1 knockdown results in activation of p53 and p21.

<p>Lysates from HFF-control and HFF-MBPsi-4 were subjected to Western blot analysis by probing with antibodies against MBP-1, phosphorylated (Ser15), acetylated p53(Lys382), p53 (DO1), p21 and actin.</p

Knockdown of MBP-1 in HFF altered morphology and exhibited senescence-associated β-galactosidase expression.

<p>Panel A: HFF-MBPsi-4 (panel a) and HFF-control (panel b) were grown to near confluency and stained with H & E. MBP-1 knockdown fibroblasts displayed an irregular, enlarged cellular morphology as compared to the control siRNA transfected cells. Panel B: HFF-MBPsi-4 cells and control-HFF were grown in plates and senescence-associated β-galactosidase assay was performed. MBP-1 knockdown HFF displayed a significantly higher senescence associated β-galactosidase activity (panel a), unlike in control HFF (panel b).</p

The role of endoscopist adenoma detection rate in in sex differences in colonoscopy findings: cross-sectional analysis of the SCREESCO randomized controlled trial

Fewer adenomas are detected at colonoscopy in women compared to men and failure to detect adenomas and sessile serrated polyps is associated with an increased risk of post-colonoscopy colorectal cancer. The aim of this study was to investigate whether this was in part due to the greater difficulty of conducting colonoscopy in women, with the difference being more apparent in colonoscopies conducted by less skilled endoscopists. Cross-sectional exploratory analysis of data on 16,551 individuals undergoing a primary colonoscopy (PCOL group) or colonoscopy after positive faecal immunochemical test (FIT group) within the randomized controlled trial SCREESCO. Endoscopist adenoma detection rate (ADR; low or high) was determined based on each endoscopist’s colonoscopies performed in SCREESCO. In each study group, the relationship between the sex difference in colonoscopy outcome and endoscopist ADR was assessed using multiplicative interaction tests. Endoscopists performed equally many colonoscopies in men and women (median 52% men). There were no signs of effect modification of the risk ratio of any finding (men vs women) by endoscopist ADR in the PCOL group (p = 0.33) or the FIT group (p = 0.30). The proportion of incomplete index colonoscopies was lower in men than in women in both groups and there was no effect modification by endoscopist ADR in either the PCOL group (p = 0.41) or the FIT group (p = 0.96). This study provides no evidence that endoscopist skill measured by ADR underlies the sex difference in adenoma detection at colonoscopy. This study has trial number NCT02078804 and is registered with ClinicalTrials.gov.</p

Supplementary data for Xu et al., 2024., G-cubed

Supplementary data for manuscript A rapid, simple, and low-blank pumped ion-exchange column chromatography technique for boron purification from carbonate and seawater matrices, Xu et al., 2024., G-cubed</p

BME treatment in HNSCC cells inhibits proliferation.

<p>(A). HNSCC cells were treated with BME for 24 h, and MTS assay was performed. (B). Cal27 cells were treated with BME for different time points. Cell proliferation was measured in control and BME treated Cal27 cells by Trypan blue exclusion method. The results are presented as means of three different experiments with standard errors. (**, p<0.001).</p

Modulation of cell cycle regulatory molecules following BME treatment in HNSCC cells.

<p>(A). Gene expression profiling from RNA of mock or BME treated Cal27 cells was performed using SABiosciences cell cycle pathway qRT-PCR arrays. BME treated cells display a pattern of modulated cell proliferation markers (e.g., ATM, CCND1, MCM2 and BIRC5). (B). Cal27 and JHU-22 cells were treated with BME and cell lysates were analyzed for certain cell cycle molecules for verification. The expression of CyclinD1, p21, p27 and survivin was examined by Western blot using specific antibodies. The blots were reprobed with an antibody to GAPDH for comparison of protein load.</p