Additional file 1: of Anxiety after Sympathectomy in patients with primary palmar hyperhidrosis may prolong the duration of compensatory hyperhidrosis

Table S1. Post-operative self-assessment questionnaire. (DOCX 13 kb

BCAR1, phospho-BCAR1, p38 and phospho-p38 expression in NSCLC tissues and cells.

<p>A: Immunoblotting indicated either BCAR1 or phospho-p38(Thr180/Tyr182) levels in three NSCLC tissues (C) were significantly higher than in the adjacent normal tissues (N). But phospho-BCAR1 (Tyr410) and p38 levels in NSCLC and the adjacent normal tissues were similar. BCAR1, phospho-BCAR1, p38 and phospho-p38 expressions were also detected in A549 and Calu-3 NSCLC cell line by using Immunoblotting assay. BCAR1 knockdown causes the appreciable reduction of phospho-BCAR1 and phospho-p38 levels in A549 cells. B: Gray scales analysis of immunoblotting also suggested BCAR1 and phospho-p38(Thr180/Tyr182) levels were significantly higher in NSCLC than in the normal adjacent tissue (48.18±24.7 vs 10.97±9.8,<i>P</i><0.001; 16.03±5.8 vs 28.82±8.0, <i>P</i><0.001). However, phospho-BCAR1 (Tyr410) and p38 had not the trend (20.72±6.4 vs 24.37±7.5, <i>P</i> = 0.22; 25.3±11.2 vs 27.8±15.2, <i>P</i> = 0.476). C: IHC suggested the expressions of BCAR1 (either in the nucleus, the cytoplasm), phospho- BCAR1 (prone to locate in the cytoplasm), phospho-p38 (prone to locate in the nucleus), p38 (prone to locate in the cytoplasm) and apoptotic bodies. Note: N (adjacent normal tissue); C (NSCLC tissue); ** (<i>P</i><0.001); # (<i>P</i>>0.05).</p

High levels of BCAR1 predict poorer prognosis, and are correlated to activation of p38.

<p>A: The survival rate of BCAR1 high-expressed group was significantly lower than of low-expressed group (<i>P</i> = 0.001). B: Phospho-p38 positive cells was significantly and positively correlated with percentages of BCAR1 positive cells, in the 182 NSCLC tissues (Spearman's rho, correlation coefficient = 0.811, p<0.001). And percentages of phospho-p38 positive cells in BCAR1 high-expressed tissues were significantly higher than in low-expressed tissues (Mann-whitney U test z = −3.689 <i>P</i><0.001). C: The sequential sections were stained for BCAR1, phospho-BCAR1, phospho-p38 and p38, which demonstrated that the cells over-expressing BCAR1 also have a higher level of phospho-p38 (×200). Either phospho-BCAR1 or p38 was slightly positive.</p

In A549 cells, BCAR1 knockdown caused cell growth arrest, cell migration inhibition, cell cycle arrest, but not apoptosis.

<p>A: At least an 80% reduction in mRNA of BCAR1 in A549-BCAR1-RNAi cells was confirmed by real-time RT-PCR. B: Colony forming units of A549-BCAR1-RNAi were detectably less than of A549-negative control cells, eleven days after plating. C: Cell migration assay suggested BCAR1 knockout prevented cell migration of A549-BCAR1-RNAi cells. D: Flow cytometry indicated BCAR1 knockout also caused cell cycle arrest of A549-BCAR1-RNAi cells. E: Flow cytometry indicated BCAR1 knockout did not increase apoptosis rate following either transient (39.1% vs 42.1%) or stable transfection (0.33% vs 0.4%) in A549 cells.</p

Multivariate regression analysis in predicting the overall survival of NSCLC patients.

<p>Multivariate regression analysis in predicting the overall survival of NSCLC patients.</p

The patients’ clinical and pathological characteristics according to BCAR1 and p-p38 expression in NSCLC.

<p>Note:</p>#<p>: <i>X</i>² test for the positive rate of staining (NSCLC vs Normal adjacent tissue);</p>*<p>: Mann-whitney U test;</p>▵<p>: Kruskal-Wallis test.</p

Discovery of Pyrrole−Indoline-2-ones as Aurora Kinase Inhibitors with a Different Inhibition Profile

A series of pyrrole−indolin-2-ones were synthesized, and their inhibition profile for Aurora kinases was studied. The potent compound 33 with phenylsulfonamido at the C-5 position and a carboxyethyl group at the C-3′ position selectively inhibited Aurora A over Aurora B with IC50 values of 12 and 156 nM, respectively. Replacement of the carboxyl group with an amino group led to compound 47, which retained the activity for Aurora B and lost activity for Aurora A (IC50 = 2.19 μM). Computation modeling was used to address the different inhibition profiles of 33 and 47. Compounds 47 and 36 (the ethyl ester analogue of 33) inhibited the proliferation of HCT-116 and HT-29 cells and suppressed levels of the phosphorylated substrates of Aurora A and Aurora B in the Western blots