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Abstract: A complementary electrochromic device (ECD) based on Prussian blue (PB) and poly(3,3-diethyl-3,4-dihydro-2H-thieno-[3,4-b][1,4]dioxepine) (PProDOT-Et2) has been systematically investigated. PB is regarded as an anodic coloring material with high electrochemical stability, while PProDOT-Et2 is a cathodic coloring polymer with high contrast and high coloration efficiency (η). The electro-optical properties of the two electrochromic (EC) materials are characterized separately in a 0.1M LiClO4 in propylene carbonate (PC). A complementary ECD is assembled based on the two EC materials. The maximum transmittance of the ECD at 590nm can be changed reversibly from 11.3% to 70.6% at the applied voltages of 1.2 and −1.3V, and achieved a high coloration efficiency of 1214cm2/C. Moreover, this ECD still remains at 98% of its maximum transmittance window (ΔT max) even after 1,200 cycles, namely, the ΔT value decreases from 59% to 58%. [Copyright &y& Elsevier]

Mitosis is a complicated process by which eukaryotic cells segregate duplicated genomes into two daughter cells. To achieve the goal, numerous regulators have been revealed to control mitosis. The oncogenic Aurora-A is a versatile kinase responsible for the regulation of mitosis including chromosome condensation, spindle assembly, and centrosome maturation through phosphorylating a range of substrates. However, overexpression of Aurora-A bypasses cytokinesis, thereby generating multiple nuclei by unknown the mechanisms. To explore the underlying mechanisms, we found that SLAN, a potential tumor suppressor, served as a substrate of Aurora-A and knockdown of SLAN induced immature cytokinesis. Aurora-A phosphorylates SLAN at T573 under the help of the scaffold protein 14-3-3η. The SLAN phosphorylation-mimicking mutants T573D or T573E, in contrast to the phosphorylation-deficiency mutant T573A, induced higher level of multinucleated cells, and the endogenous SLAN p573 resided at spindle midzone and midbody with the help of the microtubule motor MKLP1. The Aurora-A- or SLAN-induced multiple nuclei was prevented by the knockdown of 14-3-3η or Aurora-A respectively, thereby revealing a 14-3-3η/Aurora-A/SLAN cascade negatively controlling cytokinesis. Intriguingly, SLAN T573D or T573E inactivated and T573A activated the key cytokinesis regulator RhoA. RhoA interacted with SLAN np573, i.e., the nonphosphorylated form of SLAN at T573, which localized to the spindle midzone dictated by RhoA and ECT2. Therefore, we report here that SLAN mediates the Aurora-A-triggered cytokinesis bypass and SLAN plays dual roles in that process depending on its phosphorylation status.

Lung resistance-related protein (LRP) is a human major vault protein (MVP) implicated in drug resistance of cancer cells in a cell-type dependent manner. The primary goal of the study was to understand the role(s) of LRP in doxorubicin (DOX) resistance of non-small cell lung cancer (NSCLC) cells and the underlying working mechanisms. In the study, the roles of LRP in the regulation of DOX dynamics, nuclear import of minor vault proteins (vault poly (ADP-ribose) polymerase, vPARP and telomerase associated protein-1, TEP-1) and DOX-mediated cytotoxicity were examined in CH27 and H460 cells. Our results were the first to show that the CH27 cells with higher LRP expression levels were more resistant to DOX-induced cytotoxicity as shown in apoptosis experiments. LRP at the nuclear membrane could regulate DOX efflux from the nucleus to the cytosol, and also the reverse vPARP/TEP1 influx from the cytosol, to protect NSCLC cells from DOX-induced apoptosis. Cytosolic LRP could bind to DOX, vPARP and TEP1 to clear DOX away from the nucleus and promote the assembly of vaults for cell protection again. Based on the data obtained, the molecular mechanisms responsible for DOX resistance of NSCLC were delineated to demonstrate that LRP, vPARP and TEP1 were potential targets for NSCLC therapy. Inhibitors of these proteins, including small interfering LRP (siLRP), wheat-germ agglutenin (WGA) (WGA), 3-aminobenzamide (3-AB) and 3,6,9-trisubstituted acridine 9-[4-(N,N-dimethylamino) phenylamino]-3,6-bis(3-pyrrolodinopropionamido) acridine (BRACO-19), break down the DOX resistance of NSCLC cells, particularly in CH27 cells, and may have therapeutic values in the control of NSCLC.

Background: Lung cancer with lung to lung metastasis is common. The objective of this study was to investigate the association among the distribution of contralateral lung metastases versus primary lung tumor location, clinical characteristics, and epidermal growth factor receptor (EGFR) mutations status., Methods: The study included treatment-naïve stage IV lung adenocarcinoma with contralateral lung metastases from 2012 through 2013., Results: In total, 103 patients were enrolled after excluding lung cancer with histology other than adenocarcinoma, synchronous multiple primary lung cancers, or other active malignancy. The median age was 65 years (range, 28-93 years); 47 male patients (45.6%); 69 non-smoker (NS) patients (67.0%); 68 Eastern Cooperative Oncology Group performance status (ECOG PS) 0-1 patients (66.0%); 38 M1a patients (38.9%); and 60 EGFR mutation patients (58.3%). There were 51 cases (49.5%) with primary lung cancer located over upper lobes. Among them, 36 (70.6%) had contralateral upper lung predominance metastasis, 9 (17.6%) had lower lung predominance, and 6 (11.8%) had equal distribution. Among the 52 lower lobe tumors, 17 (32.7%), 19 (36.5%), and 16 (30.8%) had upper, lower lung predominance, and equal distribution metastasis, respectively. Univariate analysis showed only male gender and primary tumor location over upper lobes were significantly associated with contralateral upper lung predominance metastases. After multivariate analysis, only primary tumor location over upper lobes was significantly associated with contralateral upper lung predominance metastases (adjusted OR 5.49, 95% CI, 2.15-14.03, P<0.001)., Conclusions: Upper lobe lung adenocarcinoma was significantly associated with contralateral upper lung predominance metastases. Further research is needed to elucidate the mechanisms underlying this phenomenon.

Purpose: Although existence of humoral immunity has been previously shown in malignant pleural effusions, only a limited number of immunogenic tumor-associated antigens (TAA) have been identified and associated with lung cancer. In this study, we intended to identify more TAAs in pleural effusion-derived tumor cells., Experimental Design: Using morphologically normal lung tissues as a control lysate in Western blotting analyses, 54 tumor samples were screened with autologous effusion antibodies. Biochemical purification and mass spectrometric identification of TAAs were done using established effusion tumor cell lines as antigen sources. We identified a p48 antigen as alpha-enolase (ENO1). Semiquantitative immunohistochemistry was used to evaluate expression status of ENO1 in the tissue samples of 80 patients with non-small cell lung cancer (NSCLC) and then correlated with clinical variables., Results: Using ENO1-specifc antiserum, up-regulation of ENO1 expression in effusion tumor cells from 11 of 17 patients was clearly observed compared with human normal lung primary epithelial and non-cancer-associated effusion cells. Immunohistochemical studies consistently showed high level of ENO1 expression in all the tumors we have examined thus far. Log-rank and Cox's analyses of ENO1 expression status revealed that its expression level in primary tumors was a key factor contributing to overall- and progression-free survivals of patients (P < 0.05). The same result was also obtained in the early stage of NSCLC patients, showing that tumors expressing relatively higher ENO1 level were tightly correlated with poorer survival outcomes., Conclusions: Our data strongly support a prognostic role of ENO1 in determining tumor malignancy of patients with NSCLC.