1,902 research outputs found

    Geographic variation in adult survival and reproductive tactics of the mosquito Aedes albopictus

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    Climate differences across latitude can result in seasonal constraints and selection on life history characters. Since Aedes albopictus (Skuse) invaded North America in the mid-1980s, it has spread across a range of approximate to 14 degrees latitude and populations in the north experience complete adult mortality due to cold winter temperatures that are absent in the south. Life table experiments were conducted to test for differences in the adult survival and reproductive schedules of Ae. albopictus females from two populations from the northern (Bloomington, IN [BL] and Manassas, VA [VA]; approximate to 39 degrees N) and southern (Tampa, FL and Fort Myers, FL; approximate to 27-28 degrees N) extremes of the species distribution in North America. Regardless of population origin, age-specific hazard rate increased with reproductive output and decreased with number of bloodmeals. Larger females took fewer bloodmeals, and they had greater hazard rates than did smaller females. There were no consistent differences between northern versus southern populations in resource allocation between reproduction and maintenance, reproduction over time, and reproductive investment among offspring, suggesting that latitudinal variation in climate is probably not a main selective factor impinging on adult mortality and reproductive schedules. One possible effect of climate on geographic differences in life history was detected. BL had lower survivorship, lower lifetime reproductive output, and lower adult reproductive rate than did all other populations. This result may be an indirect result of lower egg survivorship due to the severity of winter in BL compared with other populations, including VA at approximately the same latitude. Such a scenario may make the BL population more prone to extinction, irregularly recolonized from more favorable sites, and thus more susceptible to founder effects, genetic drift, and inbreeding, resulting in lower mean values of fitness-related traits

    The role of Tyr(605) and Ala(607) of thimet oligopeptidase and Tyr(606) and Gly(608) of neurolysin in substrate hydrolysis and inhibitor binding

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    The physicochemical properties of TOP (thimet oligopeptidase) and NEL (neurolysin) and their hydrolytic activities towards the FRET (fluorescence resonance energy transfer) peptide series AbzGFSXFRQ-EDDnp [where Abz is o-aminobenzoyl; X = Ala, Ile, Leu, Phe, Tyr, Trp, Ser, Gln, Glu, His, Arg or Pro; and EDDnp is N-(2,4-dinitrophenyl)-ethylenediamine] were compared with those of site-mutated analogues. Mutations at Tyr(605) and Ala(607) in TOP and at Tyr(606) and Gly(608) in NEL did not affect the overall folding of the two peptidases, as indicated by their thermal stability, CD analysis and the pH-dependence of the intrinsic fluorescence of the protein. the kinetic parameters for the hydrolysis of substrates with systematic variations at position P-1 showed that Tyr(605) and Tyr(606) of TOP and NEL respectively, played a role in subsite S-1. Ala(607) of TOP and Gly(608) of NEL contributed to the flexibility of the loops formed by residues 600-612 (GHLAGGYDGQYYG; one-letter amino acid codes used) in NEL and 599-611 (GHLAGGYDAQYYG; one-letter amino acid codes used) in TOP contributing to the distinct substrate specificities, particularly with an isoleucine residue at P-1. TOP Y605A was inhibited less efficiently by JA-2 {N-[1-(R,S)-carboxy-3-phenylpropyl]Ala-Aib-Tyr-p-aminobenzoate}, which suggested that the aromatic ring of Ty,105 was an important anchor for its interaction with wild-type TOP. the hydroxy groups of Tyr 605 and Tyr.. did not contribute to the pH-activity profiles, since the pKs obtained in the assays of mutants TOP Y605F and NEL Y606F were similar to those of wild-type peptidases. However, the pH-k(cat)/K-m dependence curve of TOP Y605A differed from that of wild-type TOP and from TOP Y606F. These results provide insights into the residues involved in the substrate specificities of TOP and NEL and how they select cytosolic peptides for hydrolysis.Universidade Federal de São Paulo, Dept Biofis, BR-04044020 São Paulo, BrazilInst Butantan, Lab Especial Toxinol Aplicada, CAT, CEPID, BR-05467010 São Paulo, BrazilUniv São Paulo, Inst Ciencias Biomed, Dept Biol Celular & Desenvolvimento, Programa Biol Celular, BR-05508900 São Paulo, BrazilUniv São Paulo, Lab Neurociencias, BR-03071000 São Paulo, BrazilUniv Mogi das Cruzes, CIIB, BR-08780911 Mogi Das Cruzes, SP, BrazilUniversidade Federal de São Paulo, Dept Biofis, BR-04044020 São Paulo, BrazilWeb of Scienc

    Raf-1 Serine 338 Phosphorylation Plays a Key Role in Adhesion-Dependent Activation of Extracellular Signal-Regulated Kinase by Epidermal Growth Factor

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    Activation of the extracellular signal-regulated kinase (ERK) 1/2 cascade by polypeptide growth factors is tightly coupled to adhesion to extracellular matrix in nontransformed cells. Raf-1, the initial kinase in this cascade, is intricately regulated by phosphorylation, localization, and molecular interactions. We investigated the complex interactions between Raf-1, protein kinase A (PKA), and p21-activated kinase (PAK) to determine their roles in the adhesion dependence of signaling from epidermal growth factor (EGF) to ERK. We conclude that Raf-1 phosphorylation on serine 338 (S338) is a critical step that is inhibited in suspended cells. Restoration of phosphorylation at S338, either by expression of highly active PAK or by expression of an S338 phospho-mimetic Raf-1 mutation, led to a partial rescue of ERK activation in suspended cells. Raf-1 inhibition in suspension was not due to excessive negative regulation on inhibitory sites S43 and S259, as these serines were largely dephosphorylated in suspended cells. Finally, strong phosphorylation of Raf-1 S338 provided resistance to PKA-mediated inhibition of ERK activation. Phosphorylation at Raf-1 S43 and S259 by PKA only weakly inhibited EGF activation of Raf-1 and ERK when cells maintained high Raf-1 S338 phosphorylation

    Eficácia da imunoterapia no tratamento de pitiose facial em equino.

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    Pythiosis in horses is a proliferative and ulcerative disease that primarily affects the skin and subcutaneous tissue of limbs, thoracic-abdominal region and head. This disease sometimes can also affect limb bones or cause tumoral masses in abdomen. Usually, the cutaneous cases are confused with habronemiasis. The disease is more common in marshy areas, places with formation of slow drainage ponds and aquatic vegetation under high temperatures. The aim of this study was to describe the development of facial lesions in a horse caused by pythiosis in Cuiaba, Mato Grosso, and, additionally to discuss relevant issues regarding the diagnosis, clinical course and response to immunotherapy treatment.Publicação 955. Hospital Forum

    Retro-1-oligonucleotide conjugates. Synthesis and biological evaluation

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    Addition of small molecule Retro-1 has been described to enhance antisense and splice switching oligonucleotides. With the aim of assessing the effect of covalently linking Retro-1 to the biologically active oligonucleotide, three different derivatives of Retro-1 were prepared that incorporated a phosphoramidite group, a thiol or a 1,3-diene, respectively. Retro-1-oligonucleotide conjugates were assembled both on-resin (coupling of the phosphoramidite) and from reactions in solution (Michael-type thiol-maleimide reaction and Diels-Alder cycloaddition). Splice switching assays with the resulting conjugates showed that they were active but that they provided little advantage over the unconjugated oligonucleotide in the well-known HeLa Luc705 reporter system

    Viable black hole solution in Bopp-Podolsky electrodynamics

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    Following a recent approach in which the gravitational field equations in curved spacetimes were presented in the Bopp-Podolsky electrodynamics, we obtained an approximate and spherically symmetric black hole solution in this context. The calculations were carried out up to the linear approximation in both the spacetime geometry and the radial electric field. The solution presents a new parameter, that comes from the Lagrangian of the model, but even so it is in agreement with the the no-hair conjecture. Moreover, the black hole presented here is viable when its shadow is compared to the Sagittarius A* shadow, recently revealed by the Event Horizon Telescope Collaboration.Comment: 9 pages, 3 figures, 1 table. V2 with minor change

    Integrins Regulate the Linkage between Upstream and Downstream Events in G Protein-coupled Receptor Signaling to Mitogen-activated Protein Kinase

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    Receptor tyrosine kinases (RTKs) and G protein-coupled receptors (GPCRs) can both activate mitogen-activated protein kinase (MAPK), a critical intermediate in the transduction of proliferative signals. Numerous observations have demonstrated that integrin-mediated cell anchorage can regulate the efficiency of signaling from RTKs to MAPK. Recently, a relationship between integrins and GPCR signaling has also emerged; however, little is understood concerning the mechanisms involved. Here, we investigate integrin regulation of GPCR signaling to MAPK, focusing on the P2Y class of GPCRs that function through activation of phospholipase Cbeta. P2Y receptor signaling to the downstream components mitogen-activated protein kinase kinase and MAPK is highly dependent on integrin-mediated cell anchorage. However, activation of upstream events, including inositol phosphate production and generation of calcium transients, is completely independent of cell anchorage. This indicates that integrins regulate the linkage between upstream and downstream events in this GPCR pathway, just as they do in some aspects of RTK signaling. However, the P2Y pathway does not involve cross-activation of a RTK, nor a role for Shc or c-Raf; thus, it is quite distinct from the classical RTK-Ras-Raf-MAPK cascade. Rather, integrin-modulated P2Y receptor stimulation of MAPK depends on calcium and on the activation of protein kinase C

    Avaliação da prevenção e controle da anemia infecciosa equina no Pantanal.

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