Rhegmatogenous retinal detachment in uveitis

Abstract Background Retinal detachment is more common among uveitis patients than in the general population. Here, we aimed to assess the prevalence of rhegmatogenous retinal detachment (RRD) in a uveitis population. Methods We retrospectively studied 851 uveitis patients, recording characteristics such as uveitis duration, anatomical location, and cause; RRD occurrence; proliferative vitreoretinopathy (PVR) at presentation; surgical approach; reattachment rate; and initial and final visual acuity (VA). Results RRD occurred in 26 patients (3.1%; 29 affected eyes) and was significantly associated with posterior uveitis (p < 0.001), infectious uveitis (p < 0.001), and male gender (p = 0.012). Among cases of infectious uveitis, cytomegalovirus and varicella zoster virus were most commonly associated with RRD development. RRD in non-infectious uveitis was not found to be associated with any specific uveitis entity. The rate of single-operation reattachment was 48%, and the rate of final reattachment was 83%. Mean final VA was 20/125, with 41% of eyes ultimately having a VA of less than 20/200. Conclusion Uveitis is a risk factor for RRD development, which carries a poor prognosis

Tuning The Electrochemical Reduction Of Graphene Oxide: Structural Correlations Towards The Electrooxidation Of Nicotinamide Adenine Dinucleotide Hydride

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)This work demonstrates for the first time the effect of tuning the electrochemical reduction of graphene oxide (GO) on its electrocatalytic properties towards the electrooxidation of NADH. The investigations of differently tuned electrochemically reduced graphene oxide (ERGO) allowed the obtainment of clear evidences that groups containing C=O and/or C-O functionalities are responsible for this electrocatalytic response of the nanomaterial. The electrochemical reduction of GO was conducted by chronoamperometry. The ERGO-modified electrodes were characterised by Raman and X-ray photoelectron spectroscopy (XPS). The redox signals of the ERGO films in the presence of NADH have shown a completely different trend when compared to ferri/ferrocyanide, indicating that the electroactivity goes beyond electrical features of ERGO, with some oxygenated functional groups playing a vital role. We show that the presence of these groups depends on the manner in which the electrochemical reduction of GO was performed, and they are responsible for the electrocatalytic activity towards the electrooxidation of NADH. Our results show the influence of C-O/C=O containing functional groups, which are the same groups involved in the reaction between NADH and quinones. (C) 2015 Elsevier Ltd. All rights reserved.197194199Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)Conselho Nacional de Desenvolvimento Cientifico e Tecnologico (CNPq)Instituto Nacional de Ciencia e Tecnologia de Bioanalitica (INCTBio)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq

INHIBITORS of the MAJOR CYSTEINYL PROTEINASE (GP57/51) IMPAIR HOST-CELL INVASION and ARREST the INTRACELLULAR DEVELOPMENT of TRYPANOSOMA-CRUZI INVITRO

Peptidyl diazomethane (PDAM) derivatives, a class of irreversible inhibitors for cysteine proteinase, were screened for the ability to impair Trypanosoma cruzi invasion and intracellular development in primary cultures of heart muscle cells (HMC). T. cruzi GP57/51, a purified cysteinyl proteinase, and the substrate Z-Phe-Arg-NHMec were used to determine inhibition rate constants (k'+2) by continuous kinetic assays. the k'+2 values ranged from 25 400 to 2 800. the best inhibitors of GP57/51 had bulky hydrophobic residues in the P1 position (in addition to P2), the S1 sub-site specificity of the enzyme being thus similar to mammalian cathepsin L. the effects of these PDAM on parasite infectivity were then investigated. the ability to invade HMC was markedly impaired when trypomastigotes were briefly exposed to 10-mu-M of Z-(S-Bzl)Cys-Phe-CHN2. Striking effects were observed when PDAM were added to HMC cultures that had been previously infected with trypomastigotes: Z-(S-Bzl)Cys-Phe-CHN, with an IC50 of 0.4-mu-M, and less markedly Z-Phe-Phe-CHN, and Z-Tyr-Phe-CHN2 (or Z-Phe-Tyr-CHN2) blocked amastigote replication as well as their transformation into trypomastigotes, thereby arresting intracellular development. Bz-Phe-Gly-CHN2, in contrast, failed to display antiparasite activity. Direct characterization of the target cysteinyl proteinase was sought, by incubating viable amastigotes or infected HMC with Z-[I-125]Tyr-Phe-CHN2. Affinity labeling implicated GP57/51 as the major cysteinyl proteinase target for this probe. We propose that T. cruzi intracellular development is critically dependent on GP57/51 (cruzipain). Selective inhibitors for this cysteinyl proteinase may have therapeutic potential.UNIV FED RIO de JANEIRO,INST BIOFIS CARLOS CHAGAS FILHO,CCS CID UNIV,BR-21944 RIO de JANEIRO,BRAZILINST OSWALDO CRUZ,DEPT ULTRAESTRUT & BIOL CELULAR,RIO de JANEIRO,BRAZILINST BUTANTAN,SERV FARMACOL,São Paulo,BRAZILESCOLA PAULISTA MED SCH,INST BIOFIS,BR-04023 São Paulo,BRAZILESCOLA PAULISTA MED SCH,INST BIOFIS,BR-04023 São Paulo,BRAZILWeb of Scienc