Homopolyatomic Bismuth Ions, Part 2 Electronic Excitations in Homopolyatomic Bismuth Cations: Spectroscopic Measurements in Molten Salts and an ab initio CI-Singles Study

Abstract: The electronic excitations of the low-valence bismuth cluster cations Bi 5 3 , Bi 8 2 , and Bi 9 5 have been studied with experimental and theoretical techniques. The UV-visible spectra of the bismuth ions were measured in acidic chloroaluminate melts (mixture of 1-methyl-3-benzyl imidazolium chloride and AlCl 3 ). The spectra of the Bi 5 3 and Bi 8 2 ions agree fairly well with previous reports, but also revealed additional low-energy absorptions. Ab initio methods were employed to assign the experimentally observed electronic transitions of these homopolyatomic bismuth cations. Structures were optimized at the RHF, MP2, and B3LYP levels of theory by using split-valence LANL2DZ basis sets that were augmented with one and two sets of pure d functions. The computed structures agree well with the results of neutron diffraction analyses of melts. Electronically excited states of the three clusters were treated by using the CI-Singles theory. The results of these calculations were used to explain the observed UV-visible spectra. The observed electronic excitations in the UV-visible range are all found to result from transitions involving the molecular orbitals formed by 6p-atomic-orbital overlap. This leads to the necessity of using basis sets that include d-type functions, which allow for an adequate description of the bonding that results from such p-orbital overlap. Spin-orbit coupling becomes increasingly important with increasing atomic number and its consideration is necessary when describing the electronic transitions in clusters of heavy atoms. The calculations show that singlet ± triplet transitions, which are made accessible by strong spin-orbit coupling, are responsible for some of the observed absorptions

Vaccination and Infection as Causative Factors in Japanese Patients With Rasmussen Syndrome: Molecular Mimicry and HLA Class I

Rasmussen syndrome is an intractable epilepsy with a putative causal relation with cellular and humoral autoimmunity. Almost half of the patients have some preceding causative factors, with infections found in 38.2%, vaccinations in 5.9% and head trauma in 8.9% of Japanese patients. In a patient with seizure onset after influenza A infections, cross-reaction of the patient's lymphocytes with GluRε2 and influenza vaccine components was demonstrated by lymphocyte stimulation test. Database analyses revealed that influenza A virus hemagglutinin and GluRε2 molecules contain peptides with the patient's HLA class I binding motif (HLA − A*0201). The relative risks of HLA class I genotypes for Rasmussen syndrome are 6.1 (A*2402), 6.4 (A*0201), 6.3 (A*2601) and 11.4 (B*4601). The relative risks of HLA class I-A and B haplotypes are infinity (A*2601+B*5401), 21.1 (A*2402+B*1501), 13.3 (A*2402+B*4801) and 5.1 (A*2402+B*5201). Some alleles and haplotypes of HLA class I may be the risk factors in Japanese patients. Cross-reactivity of cytotoxic T lymphocytes may contribute to the processes leading from infection to the involvement of CNS

Transparent Conductive Films Fabricated from Polythiophene Nanofibers Composited with Conventional Polymers

Transparent, conductive films were prepared by compositing poly(3-hexylthiophene) (P3HT) nanofibers with poly(methyl methacrylate) (PMMA). The transparency, conductivity, atmospheric stability, and mechanical strength of the resulting nanofiber composite films when doped with AuCl3 were evaluated and compared with those of P3HT nanofiber mats. The conductivity of the nanofiber composite films was 4.1 S∙cm−1, which is about seven times less than that which was previously reported for a nanofiber mat with the same optical transmittance (~80%) reported by Aronggaowa et al. The time dependence of the transmittance, however, showed that the doping state of the nanofiber composite films in air was more stable than that of the nanofiber mats. The fracture stress of the nanofiber composite film was determined to be 12.3 MPa at 3.8% strain

Identification of nuclear phosphoproteins as novel tobacco markers in mouse lung tissue following short-term exposure to tobacco smoke

Smoking is a risk factor for lung diseases, including chronic obstructive pulmonary disease and lung cancer. However, the molecular mechanisms mediating the progression of these diseases remain unclear. Therefore, we sought to identify signaling pathways activated by tobacco-smoke exposure, by analyzing nuclear phosphoprotein expression using phosphoproteomic analysis of lung tissue from mice exposed to tobacco smoke. Sixteen mice were exposed to tobacco smoke for 1 or 7 days, and the expression of phosphorylated peptides was analyzed by mass spectrometry. A total of 253 phosphoproteins were identified, including FACT complex subunit SPT16 in the 1-day exposure group, keratin type 1 cytoskeletal 18 (K18), and adipocyte fatty acid-binding protein, in the 7-day exposure group, and peroxiredoxin-1 (OSF3) and spectrin β chain brain 1 (SPTBN1), in both groups. Semi-quantitative analysis of the identified phosphoproteins revealed that 33 proteins were significantly differentially expressed between the control and exposed groups. The identified phosphoproteins were classified according to their biological functions. We found that the identified proteins were related to inflammation, regeneration, repair, proliferation, differentiation, morphogenesis, and response to stress and nicotine. In conclusion, we identified proteins, including OSF3 and SPTBN1, as candidate tobacco smoke-exposure markers; our results provide insights into the mechanisms of tobacco smoke-induced diseases

Adiponectin Protein Exists in Aortic Endothelial Cells

<div><p>Aims</p><p>Inflammation is closely associated with the development of atherosclerosis and metabolic syndrome. Adiponectin, an adipose-derived secretory protein, possesses an anti-atherosclerotic property. The present study was undertaken to elucidate the presence and significance of adiponectin in vasculature.</p><p>Methods and Results</p><p>Immunofluorescence staining was performed in aorta of wild-type (WT) mice and demonstrated that adiponectin was co-stained with CD31. Thoracic aorta was cut through and then aortic intima was carefully shaved from aorta. Western blotting showed the existence of adiponectin protein in aortic intima, while there was no adiponectin mRNA expression. Adiponectin knockout (Adipo-KO) and WT mice were administered with a low-dose and short-term lipopolysaccharide (LPS) (1 mg/kg of LPS for 4 hours). The endothelium vascular adhesion molecule-1 (VCAM-1) and intercellular adhesion molecule-1 (ICAM-1) were highly increased in Adipo-KO mice compared to WT mice after LPS administration.</p><p>Conclusions</p><p>Adiponectin protein exists in aortic endothelium under steady state and may protect vasculature from the initiation of atherosclerosis.</p></div

Localization of adiponectin in aorta.

<p>A, Dual-immunofluorescence was performed in wild-type (WT) and adiponectin knockout (Adipo-KO) mice as described in Materials and Methods. B, High magnification images of aortic intima using confocal laser microscope were obtained from WT mice. Green, adiponectin; blue, DAPI; red, CD31.</p

Effect of LPS on endothelial adhesion molecules in aortic intima.

<p>Aortic intima of wild-type (WT) or adiponectin knockout (Adipo-KO) mice were removed at 4 hours after LPS administration and were subjected to RT-PCR (A) and western blotting (B). Values are mean ± SEM; n = 6 for each group. * <i>P</i><0.05, compared with the values of WT mice with saline treatment; ‡ <i>P</i><0.05, compared with the values of WT mice with LPS administration group.</p

Existence of adiponectin protein in aortic intima.

<p>Mice were perfused with cold saline to eliminate the contamination of circulating adiponectin. After removing perivascular fat, thoracic aorta was cut through and then intima was carefully shaved from the aorta. A, Western blotting with antibodies against adiponectin, perilipin A, and CD31 in aortic intima. B, Multimeric complexes of adiponectin protein in aortic intima. C, The mRNA level of adiponectin in fat tissue and aortic intima. WT, wild-type mice; KO, adiponectin knockout mice; N.D., not detected.</p