Immatures of Lamprosoma amethystinum Perty, 1832 (Chrysomelidae, Lamprosomatinae)

The genus Lamprosoma Kirby, 1818 includes 128 neotropical species and 54 of them are recorded from Brazil (Monros, 1960). The first species with a described larva was L. seraphinum Lacordaire. After that, larvae and pupae of three species were described: L. bicolor Kirby, 1818, L. chorisiae Monros, 1948 and L. azureum Germar, 1824. Fiebrig (1910) described the larva of L. seraphinum Lacordaire, collected on Teminalia hassleriana Chod. (Combretaceae) of Paraguay. Moreira (1913) described L. bicolor collected on Terminalia catappa L., in Rio de Janeiro. According to him, this tree was introduced from Molucas Islands, in Oceania. He also considered it probable that L. bicolor lived on one native species of Terminalia or on another species of Combretaceae and adaptated itself to live on Terminalia catappa. Monros (1949) described L. chorisiae collected on Chorisia speciosa and Ch. insignis [ Ceiba speciosa (A. St.-Hil., A. Juss. & Cambess.) Ravenna and Ceiba insignis (Kunth) P. E. Gibbs & J. Semir] (Bombacaceae) ("" palos borrachos"") in Tucuman. Caxambu and Almeida (1999) described L. azureum collected on Psidium cattleianum Sabine (Myrtaceae)(""araca""), in Parana state. Herein, the larva and pupa of L. amethystinum collected on Terminalia catappa amendoeira-da-praia"", "" chapeu-de-sol"") in Campinas, Sao Paulo state, are described and illustrated.

NEW RECORDS OF MOSQUITOES FROM NORTHWESTERN ARGENTINA

Eleven mosquito species, namely Aedes hastatus, Ae. fulvus, Coquillettidia albicosta, Cq. juxtamansonia, Culex aliciae, Cx. delpontei, Cx. oedipus, Cx. pedroi, Mansonia flaveola, Uranotaenia leucoptera, and Wyeomyia oblita, are recorded for the first time from northwestern Argentina. In addition, 3 species, Cx. brethesi, Limatus durhami, and Ur. nataliae, are reported for the first time from Salta Province. These records extend the geographical distribution of these 3 species to Salta Province. This study also extends the geographical distributions of Cq. nigricans, Cx. chidesteri, and Ma. humeralis to Jujuy Province and of Ae. meprai, Ae. milleri, Ae. oligopistus, Cx. brethesi, Cx. fernandezi, and Cx. tatoi to Tucuman Province.

Prediction with measurement errors in finite populations

We address the problem of selecting the best linear unbiased predictor (BLUP) of the latent value (e.g., serum glucose fasting level) of sample subjects with heteroskedastic measurement errors. Using a simple example, we compare the usual mixed model BLUP to a similar predictor based on a mixed model framed in a finite population (FPMM) setup with two sources of variability, the first of which corresponds to simple random sampling and the second, to heteroskedastic measurement errors. Under this last approach, we show that when measurement errors are subject-specific, the BLUP shrinkage constants are based on a pooled measurement error variance as opposed to the individual ones generally considered for the usual mixed model BLUP. In contrast, when the heteroskedastic measurement errors are measurement condition-specific, the FPMM BLUP involves different shrinkage constants. We also show that in this setup, when measurement errors are subject-specific, the usual mixed model predictor is biased but has a smaller mean squared error than the FPMM BLUP which points to some difficulties in the interpretation of such predictors. (C) 2011 Elsevier By. All rights reserved.

Characterization of Heparin-induced Glyceraldehyde-3-phosphate Dehydrogenase Early Amyloid-like Oligomers and Their Implication in alpha-Synuclein Aggregation

Lewy bodies and Lewy neurites, neuropathological hallmarks of several neurological diseases, are mainly made of filamentous assemblies of alpha-synuclein. However, other macromolecules including Tau, ubiquitin, glyceraldehyde-3-phosphate dehydrogenase, and glycosaminoglycans are routinely found associated with these amyloid deposits. Glyceraldehyde-3-phosphate dehydrogenase is a glycolytic enzyme that can form fibrillar aggregates in the presence of acidic membranes, but its role in Parkinson disease is still unknown. In this work, the ability of heparin to trigger the amyloid aggregation of this protein at physiological conditions of pH and temperature is demonstrated by infrared and fluorescence spectroscopy, dynamic light scattering, small angle x-ray scattering, circular dichroism, and fluorescence microscopy. Aggregation proceeds through the formation of short rod-like oligomers, which elongates in one dimension. Heparan sulfate was also capable of inducing glyceraldehyde-3-phosphate dehydrogenase aggregation, but chondroitin sulfates A, B, and C together with dextran sulfate had a negligible effect. Aided with molecular docking simulations, a putative binding site on the protein is proposed providing a rational explanation for the structural specificity of heparin and heparan sulfate. Finally, it is demonstrated that in vitro the early oligomers present in the glyceraldehyde-3-phosphate dehydrogenase fibrillation pathway promote alpha-synuclein aggregation. Taking into account the toxicity of alpha-synuclein prefibrillar species, the heparin-induced glyceraldehyde-3-phosphate dehydrogenase early oligomers might come in useful as a novel therapeutic strategy in Parkinson disease and other synucleinopathies.