Such resorbable biomaterial prostheses could serve as growth substrates together with specific siRNA

to foster neuronal regeneration. To the best of our knowledge, we are the first to biofunctionalize neuronal prostheses with siRNA. We analyzed neuronal and Schwann cell responses to scrambled siRNA coated polydioxanone polymer filaments designed to imitate pro-regenerative bands of Bfingner for oriented axonal regrowth. With a view to future clinical applications we were especially interested in potentially detrimental side effects. We employed a variety of in vitro methods, including a novel impedance electrode microchamber assay, fluorescence and scanning electron microscopy, metabolic labeling and RT-PCR. AZD1208 order We found that the application of chitosan/siRNA nanoparticles (1) did not affect glial cell motility or (2) axonal growth in contrast to other formulations, (3) only slightly reduced proliferation, and (4) did not induce inflammatory responses that might hamper axonal regeneration. The data suggest that chitosan/siRNA nanoparticle-coated polymer filaments are suitable for use in biohybrid implants with no significant side effects

on neuronal and glial cells. (C) 2011 Elsevier Ireland Ltd. All rights reserved.”
“We have recently demonstrated that human apolipoprotein E (apoE) is required for the infectivity and assembly of hepatitis C virus (HCV) (K.S. Chang, J. Jiang, Z. Cai, and G. Luo, J. Virol. 81:13783-13793, 2007; J. Jiang and G. Luo, J. Virol. 83:12680-12691, 2009). In the present study, we have determined the molecular basis underlying the importance of apoE in HCV assembly. Results derived from mammalian two-hybrid studies demonstrate FRAX597 datasheet a specific interaction between apoE and HCV nonstructural protein 5A (NS5A). The C-terminal third of apoE per se is sufficient for interaction with NS5A. Progressive deletion mutagenesis learn more analysis identified that the C-terminal alpha-helix domain of apoE is important for NS5A binding. The N-terminal receptor-binding domain and

the C-terminal 20 amino acids of apoE are dispensable for the apoE-NS5A interaction. The NS5A-binding domain of apoE was mapped to the middle of the C-terminal alpha-helix domain between amino acids 205 and 280. Likewise, deletion mutations disrupting the apoE-NS5A interaction resulted in blockade of HCV production. These findings demonstrate that the specific apoE-NS5A interaction is required for assembly of infectious HCV. Additionally, we have determined that using different major isoforms of apoE (E2, E3, and E4) made no significant difference in the apoE-NS5A interaction. Likewise, these three major isoforms of apoE are equally compatible with infectivity and assembly of infectious HCV, suggesting that apoE isoforms do not differentially modulate the infectivity and/or assembly of HCV in cell culture.”
“Acid-sensing ion channels (ASICs) in mammals monitor acid sensing and mechanoreception.