Childbearing May Increase the Risk of Nondiabetic Cataract in Chinese Women’s Old Age

Backgrounds. Ocular changes may arise during pregnancy and after childbirth, but very few studies have reported the association between childbearing and cataract among older adults. Methods. 14,292 individuals aged 60+ years were recruited in Xiamen, China, in 2013. Physician-diagnosed cataract and diabetes status were assessed by a self-reported questionnaire. Childbearing status was measured by number of children (NOC). Structural equation modeling (SEM) analysis was conducted to examine the relationships among NOC, diabetes, and cataract. Gender-specific logistic models regressing nondiabetic cataract on NOC were performed by adjusting some covariates. Results. 14,119 participants had complete data, of whom 5.01% suffered from cataract, with higher prevalence in women than men (6.41% versus 3.51%). Estimates of SEM models for women suggested that both NOC and diabetes were risk factors for cataract and that no correlation existed between NOC and diabetes. Women who had one or more children faced roughly 2–4 times higher risk of nondiabetic cataract than their childless counterparts (OR [95% CI] = 3.88 [1.24, 17.71], 3.21 [1.04, 14.52], 4.32 [1.42, 19.44], 4.41 [1.46, 19.74], and 3.98 [1.28, 18.10] for having 1, 2, 3, 4-5, and 6 or more children, resp.). Conclusions. Childbearing may increase the risk of nondiabetic cataract in Chinese women’s older age

Fast T-Type Photochromism of Colloidal Cu-Doped ZnS Nanocrystals

This paper reports on durable and nearly temperature-independent (at 298–328 K) T-type photochromism of colloidal Cu-doped ZnS nanocrystals (NCs). The color of Cu-doped ZnS NC powder changes from pale yellow to dark gray by UV light irradiation, and the color changes back to pale yellow on a time scale of several tens of seconds to minutes after stopping the light irradiation, while the decoloration reaction is accelerated to submillisecond in solutions. This decoloration reaction is much faster than those of conventional inorganic photochromic materials. The origin of the reversible photoinduced coloration is revealed to be a strong optical transition involving a delocalized surface hole which survives over a minute after escaping from intraparticle carrier recombination due to electron-hopping dissociation. ZnS NCs can be easily prepared in a water-mediated one-pot synthesis and are less toxic. Therefore, they are promising for large-scale photochromic applications such as windows and building materials in addition to conventional photochromic applications. Moreover, the present study demonstrates the importance of excited carrier dynamics and trap depths, resulting in coloration over minutes not only for photochromic nanomaterials but also for various advanced photofunctional materials, such as long persistent luminescent materials and photocatalytic nanomaterials

Inversionless gain in a three-level system driven by a strong field and collisions

Inversionless gain in a three-level system driven by a strong external field and by collisions with a buffer gas is investigated. The mechanism of populating of the upper laser level contributed by the collision transfer as well as by relaxation caused by a buffer gas is discussed in detail. Explicit formulae for analysis of optimal conditions are derived. The mechanism developed here for the incoherent pump could be generalized to other systems.Comment: RevTeX, 9 pages, 4 eps figure

Antiinflammatory and Antioxidant Flavonoids and Phenols from Cardiospermum halicacabum (倒地鈴 Dào Dì Líng)

ABSTRACTSeventeen compounds, quercetin-3-O-α-l-rhamnoside (1), kaempferol-3-O-α-l-rhamnoside (2), apigenin-7-O-β-d-glucuronide (3), apigenin 7-O-β-d-glucuronide methyl ester (4), apigenin 7-O-β-d-glucuronide ethyl ester (5), chrysoeriol (6), apigenin (7), kaempferol (8), luteolin (9), quercetin (10), methyl 3,4-dihydroxybenzoate (11), p-coumaric acid (12), 4-hydroxybenzoic acid (13), hydroquinone (14), protocathehuic acid (15), gallic acid (16), and indole-3-carboxylic acid (17), were isolated from the ethanol extract of Taiwanese Cardiospermum halicabum. All chemical structures were determined by physical and extensive spectroscopic analyses such as 1H Nuclear Magnetic Resonance spectroscopy (NMR), 13C NMR, 1H-1H Correlation spectroscopy (1H-1H COSY), Heteronuclear Multiple Quantum Coherence spectroscopy (HMQC), Heteronuclear Multiple-bond Correlation spectroscopy (HMBC), and Nuclear Overhauser Effect spectroscopy (NOESY), as well as comparison with literature values. Furthermore, the High-Performance Liquid Chromatography-Photodiode Array Detector (HPLC-DAD) fingerprint profile was established for the determination of major constituents in the EtOAc extract and retention times of the isolated compounds. All isolated compounds were also evaluated for antiinflammatory and antioxidant activities

Inactivation of the particulate methane monooxygenase (pMMO) in Methylococcus capsulatus (Bath) by acetylene

Acetylene (HCCH) has a long history as a mechanism-based enzyme inhibitor and is considered an active-site probe of the particulate methane monooxygenase (pMMO). Here, we report how HCCH inactivates pMMO in Methylococcus capsulatus (Bath) by using high-resolution mass spectrometry and computational simulation. High-resolution MALDI-TOF MS of intact pMMO complexes has allowed us to confirm that the enzyme oxidizes HCCH to the ketene (C_2H_2O) intermediate, which then forms an acetylation adduct with the transmembrane PmoC subunit. LC-MS/MS analysis of the peptides derived from in-gel proteolytic digestion of the protein subunit identifies K196 of PmoC as the site of acetylation. No evidence is obtained for chemical modification of the PmoA or PmoB subunit. The inactivation of pMMO by a single adduct in the transmembrane PmoC domain is intriguing given the complexity of the structural fold of this large membrane-protein complex as well as the complicated roles played by the various metal cofactors in the enzyme catalysis. Computational studies suggest that the entry of hydrophobic substrates to, and migration of products from, the catalytic site of pMMO is controlled tightly within the transmembrane domain. Support of these conclusions is provided by parallel experiments with two related alkynes: propyne (CH3CCH) and trifluoropropyne (CF_3CCH). Finally, we discuss the implication of these findings to the location of the catalytic site in pMMO

Simulations of small-scale turbulent dynamo

We report an extensive numerical study of the small-scale turbulent dynamo at large magnetic Prandtl numbers Pm. A Pm scan is given for the model case of low-Reynolds-number turbulence. We concentrate on three topics: magnetic-energy spectra and saturation levels, the structure of the field lines, and the field-strength distribution. The main results are (1) the folded structure (direction reversals at the resistive scale, field lines curved at the scale of the flow) persists from the kinematic to the nonlinear regime; (2) the field distribution is self-similar and appears to be lognormal during the kinematic regime and exponential in the saturated state; and (3) the bulk of the magnetic energy is at the resistive scale in the kinematic regime and remains there after saturation, although the spectrum becomes much shallower. We propose an analytical model of saturation based on the idea of partial two-dimensionalization of the velocity gradients with respect to the local direction of the magnetic folds. The model-predicted spectra are in excellent agreement with numerical results. Comparisons with large-Re, moderate-Pm runs are carried out to confirm the relevance of these results. New features at large Re are elongation of the folds in the nonlinear regime from the viscous scale to the box scale and the presence of an intermediate nonlinear stage of slower-than-exponential magnetic-energy growth accompanied by an increase of the resistive scale and partial suppression of the kinetic-energy spectrum in the inertial range. Numerical results for the saturated state do not support scale-by-scale equipartition between magnetic and kinetic energies, with a definite excess of magnetic energy at small scales. A physical picture of the saturated state is proposed.Comment: aastex using emulateapj; 32 pages, final published version; a pdf file (4Mb) of the paper containing better-quality versions of figs. 5, 8, 12, 15, 17 is available from http://www.damtp.cam.ac.uk/user/as629 or by email upon request

Azbel-Hofstadter model on triangular lattice revisited

In the present paper, the mean of Lyapunov exponents for the Azbel-Hofstadter model on the triangular lattice is calculated. It is recently proposed that [Phys. Rev. Lett. {\bf 85}, 4920 (2000)], for the case of the square lattice, this quantity can be related to the logarithm of the partition function of the two dimensional Ising model and has a connection to the asymptotic bandwidth. We find that the correspondence of this quantity to the logarithm of the partition function of the two dimensional Ising model is not complete for the triangular lattice. Moreover, the detailed connection between this quantity and the asymptotic bandwidth is not valid. Thus the conclusions for the mean of Lyapunov exponents suggested previously depend on the lattice geometry.Comment: RevTeX, 4 page, no figur

The Echinococcus canadensis (G7) genome: A key knowledge of parasitic platyhelminth human diseases

Background: The parasite Echinococcus canadensis (G7) (phylum Platyhelminthes, class Cestoda) is one of the causative agents of echinococcosis. Echinococcosis is a worldwide chronic zoonosis affecting humans as well as domestic and wild mammals, which has been reported as a prioritized neglected disease by the World Health Organisation. No genomic data, comparative genomic analyses or efficient therapeutic and diagnostic tools are available for this severe disease. The information presented in this study will help to understand the peculiar biological characters and to design species-specific control tools. Results: We sequenced, assembled and annotated the 115-Mb genome of E. canadensis (G7). Comparative genomic analyses using whole genome data of three Echinococcus species not only confirmed the status of E. canadensis (G7) as a separate species but also demonstrated a high nucleotide sequences divergence in relation to E. granulosus (G1). The E. canadensis (G7) genome contains 11,449 genes with a core set of 881 orthologs shared among five cestode species. Comparative genomics revealed that there are more single nucleotide polymorphisms (SNPs) between E. canadensis (G7) and E. granulosus (G1) than between E. canadensis (G7) and E. multilocularis. This result was unexpected since E. canadensis (G7) and E. granulosus (G1) were considered to belong to the species complex E. granulosus sensu lato. We described SNPs in known drug targets and metabolism genes in the E. canadensis (G7) genome. Regarding gene regulation, we analysed three particular features: CpG island distribution along the three Echinococcus genomes, DNA methylation system and small RNA pathway. The results suggest the occurrence of yet unknown gene regulation mechanisms in Echinococcus. Conclusions: This is the first work that addresses Echinococcus comparative genomics. The resources presented here will promote the study of mechanisms of parasite development as well as new tools for drug discovery. The availability of a high-quality genome assembly is critical for fully exploring the biology of a pathogenic organism. The E. canadensis (G7) genome presented in this study provides a unique opportunity to address the genetic diversity among the genus Echinococcus and its particular developmental features. At present, there is no unequivocal taxonomic classification of Echinococcus species; however, the genome-wide SNPs analysis performed here revealed the phylogenetic distance among these three Echinococcus species. Additional cestode genomes need to be sequenced to be able to resolve their phylogeny.Fil: Maldonado, Lucas Luciano. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones en Microbiología y Parasitología Médica. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones en Microbiología y Parasitología Médica; ArgentinaFil: Assis, Juliana. Fundación Oswaldo Cruz; BrasilFil: Gomes Araújo, Flávio M.. Fundación Oswaldo Cruz; BrasilFil: Salim, Anna C. M.. Fundación Oswaldo Cruz; BrasilFil: Macchiaroli, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones en Microbiología y Parasitología Médica. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones en Microbiología y Parasitología Médica; ArgentinaFil: Cucher, Marcela Alejandra. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones en Microbiología y Parasitología Médica. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones en Microbiología y Parasitología Médica; ArgentinaFil: Camicia, Federico. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones en Microbiología y Parasitología Médica. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones en Microbiología y Parasitología Médica; ArgentinaFil: Fox, Adolfo. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones en Microbiología y Parasitología Médica. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones en Microbiología y Parasitología Médica; ArgentinaFil: Rosenzvit, Mara Cecilia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones en Microbiología y Parasitología Médica. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones en Microbiología y Parasitología Médica; ArgentinaFil: Oliveira, Guilherme. Instituto Tecnológico Vale; Brasil. Fundación Oswaldo Cruz; BrasilFil: Kamenetzky, Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Investigaciones en Microbiología y Parasitología Médica. Universidad de Buenos Aires. Facultad de Medicina. Instituto de Investigaciones en Microbiología y Parasitología Médica; Argentin