VEGF is a chemoattractant for FGF-2–stimulated neural progenitors

Mmigration of undifferentiated neural progenitors is critical for the development and repair of the nervous system. However, the mechanisms and factors that regulate migration are not well understood. Here, we show that vascular endothelial growth factor (VEGF)-A, a major angiogenic factor, guides the directed migration of neural progenitors that do not display antigenic markers for neuron- or glia-restricted precursor cells. We demonstrate that progenitor cells express both VEGF receptor (VEGFR) 1 and VEGFR2, but signaling through VEGFR2 specifically mediates the chemotactic effect of VEGF. The expression of VEGFRs and the chemotaxis of progenitors in response to VEGF require the presence of fibroblast growth factor 2. These results demonstrate that VEGF is an attractive guidance cue for the migration of undifferentiated neural progenitors and offer a mechanistic link between neurogenesis and angiogenesis in the nervous system

Phytoremediation Potential of Three Species of Macrophytes for Nitrate in Contaminated Water

Abstrac

Modelling human choices: MADeM and decision‑making

Research supported by FAPESP 2015/50122-0 and DFG-GRTK 1740/2. RP and AR are also part of the Research, Innovation and Dissemination Center for Neuromathematics FAPESP grant (2013/07699-0). RP is supported by a FAPESP scholarship (2013/25667-8). ACR is partially supported by a CNPq fellowship (grant 306251/2014-0)

Synthesis and crystal structures of <i>N</i>-(2,3,4,6<i>-</i>Tetra-<i>O</i>-acetyl-<i>β</i>-<i>D</i>-glycosyl)thiocarbamoyl <span style="font-size:12.0pt;line-height:115%;font-family:"Times New Roman"; mso-fareast-font-family:"Times New Roman";mso-ansi-language:NL;mso-fareast-language: EN-IN;mso-bidi-language:HI" lang="NL">methylene diamine</span>

1072-1075The structure of N-(2,3,4,6-Tetra-O-acetyl-β-D-glycosyl)thiocarbamoyl methylene diamine, C16H25N3O9S has been determined by X-ray diffraction method. It crystallizes in the monoclinic system, space group P2l, with lattice parameters a = 7.6560(2), b = 10.3113(3), c = 14.1813(1)Å, β = 100.879 (2)o, and Z = 2. The hexapyranosyl ring adopts a chair conformation. All the ring substituents are in the equatorial position. The acetoxylmethyl group is in the gauche- gauche conformation. The S atom is in synperiplanar conformation, while the N-C-N-C linkage is antiperiplanar. The N-H...O intermolecular hydrogen bonds link the molecules into infinite chains and these are connected by C-H...O interaction

Deciphering the Effect of Lysine Acetylation on the Misfolding and Aggregation of Human Tau Fragment 171IPAKTPPAPK180 Using Molecular Dynamic Simulation and the Markov State Model

The formation of neurofibrillary tangles (NFT) with &beta;-sheet-rich structure caused by abnormal aggregation of misfolded microtubule-associated protein Tau is a hallmark of tauopathies, including Alzheimer&rsquo;s Disease. It has been reported that acetylation, especially K174 located in the proline-rich region, can largely promote Tau aggregation. So far, the mechanism of the abnormal acetylation of Tau that affects its misfolding and aggregation is still unclear. Therefore, revealing the effect of acetylation on Tau aggregation could help elucidate the pathogenic mechanism of tauopathies. In this study, molecular dynamics simulation combined with multiple computational analytical methods were performed to reveal the effect of K174 acetylation on the spontaneous aggregation of Tau peptide 171IPAKTPPAPK180, and the dimerization mechanism as an early stage of the spontaneous aggregation was further specifically analyzed by Markov state model (MSM) analysis. The results showed that both the actual acetylation and the mutation mimicking the acetylated state at K174 induced the aggregation of the studied Tau fragment; however, the effect of actual acetylation on the aggregation was more pronounced. In addition, acetylated K174 plays a major contributing role in forming and stabilizing the antiparallel &beta;-sheet dimer by forming several hydrogen bonds and side chain van der Waals interactions with residues I171, P172, A173 and T175 of the corresponding chain. In brief, this study uncovered the underlying mechanism of Tau peptide aggregation in response to the lysine K174 acetylation, which can deepen our understanding on the pathogenesis of tauopathies