Expression of Msx1 and Dlx1 during Dumbo rat head development: Correlation with morphological features

The Dumbo rat possesses some characteristics that evoke several human syndromes, such as Treacher-Collins: shortness of the maxillary, zygomatic and mandibular bones, and low position of the ears. Knowing that many homeobox genes are candidates in craniofacial development, we investigated the involvement of the Msx1 and Dlx1 genes in the Dumbo phenotype with the aim of understanding their possible role in abnormal craniofacial morphogenesis and examining the possibility of using Dumbo rat as an experimental model for understanding abnormal craniofacial development. We studied the expression of these genes during craniofacial morphogenesis by RT-PCR method. We used Dumbo embryos at E12 and E14 and included the Wistar strain as a control. Semi-quantitative PCR analysis demonstrated that Msx1 and Dlx1 are expressed differently between Dumbo and Wistar rats, indicating that their low expression may underly the Dumbo phenotype

Pathogens, parasites, and parasitoids associated with bumble bees (Bombus spp.) from Uruguay

As elsewhere in the world, bumble bees play a vital role as pollinators in Uruguay, but knowledge on their health status is still limited. Between September 2012 and May 2013, 403 adult individuals of the two speciesof Bombus known for the country (Bombus atratus , Bombus bellicosus ) were collected in six localities.We found that 177 (119 B. atratus, 58 B. bellicosus ) were harboring one or two types of pathogens, parasites, or parasitoids.Identification of these natural enemies carried out by morphological or molecular procedures revealed the presence of two species of Microsporidia [Nosema ceranae (prevalence: 18.2 % in B. atratus; 44.9 % in B. bellicosus ),Tubulinosema pampeana (prevalence: 13 % in B. atratus )], two species of Nematoda [Sphaerularia bombi (prevalence: 40.4 % in B. atratus; 40% in B. bellicosus ) and an unidentified Mermithidae (prevalence: 0.8 % inB. bellicosus )], and one species of Diptera parasitoid (prevalence: 3.2 % in B. atratus ; 4.2 % in B. bellicosus ). Except N. ceranae , none of the other species have been previously reported in Uruguay.Fil: Plischuk, Santiago. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Estudios Parasitológicos y de Vectores. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. Centro de Estudios Parasitológicos y de Vectores; ArgentinaFil: Salvarrey, Sheena. Universidad de la República. Facultad de Ciencias; UruguayFil: Arbulo, Natalia. Universidad de la República; UruguayFil: Santos, Estela. Universidad de la República. Facultad de Ciencias; UruguayFil: Skevington, Jeffrey H.. Canadian National Collection of Insects; CanadáFil: Kelso, Scott. Canadian National Collection of Insects; CanadáFil: Revainera, Pablo Damian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina. Universidad Nacional de Mar del Plata; ArgentinaFil: Maggi, Matías Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata; Argentina. Universidad Nacional de Mar del Plata; ArgentinaFil: Invernizzi, Ciro. Universidad de la República. Facultad de Ciencias; UruguayFil: Lange, Carlos Ernesto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Estudios Parasitológicos y de Vectores. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo. Centro de Estudios Parasitológicos y de Vectores; Argentina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas; Argentin

Crystal structure of the catalytic portion of human HMG-CoA reductase: insights into regulation of activity and catalysis

3-hydroxy-3-methylglutaryl-CoA reductase (HMGR) catalyzes the formation of mevalonate, the committed step in the biosynthesis of sterols and isoprenoids. The activity of HMGR is controlled through synthesis, degradation and phosphorylation to maintain the concentration of mevalonate-derived products. In addition to the physiological regulation of HMGR, the human enzyme has been targeted successfully by drugs in the clinical treatment of high serum cholesterol levels. Three crystal structures of the catalytic portion of human HMGR in complexes with HMG-CoA, with HMG and CoA, and with HMG, CoA and NADP(+), provide a detailed view of the enzyme active site. Catalytic portions of human HMGR form tight tetramers. The crystal structure explains the influence of the enzyme's oligomeric state on the activity and suggests a mechanism for cholesterol sensing. The active site architecture of human HMGR is different from that of bacterial HMGR; this may explain why binding of HMGR inhibitors to bacterial HMGRs has not been reported