Sensory structures of the antennae of Nannotrigona testaceicornis (Apidae : Meliponinae)

The total number and distribution per antennal flagellomere of sensilla placodea (olfactory disks), sensilla coeloconica, sensilla ampullacea and sensilla campaniformia were determined in workers of Nannotrigona testaceicornis Lepeletier a stingless bee species quite common in Brazil. The distribution of the sensilla was uniform, with the largest number occurring in flagellomere 10 and gradually decreasing in the direction of the basal flagellomeres in a way similar to that observed in Scaptotrigona postica Latreille.Nannotrigona testaceicornis had a larger number of sensilla ampullacea and a smaller number of sensilla coeloconica and sensilla campaniformia than Scaptotrigona postica. Although Nan notrigona testaceicornis does not communicate through the formation of pheromone trails, this species presents a larger quantity of sensilla placodea (relative to the length of the flagellum) than Scaptotrigona postica.

Integrability vs supersymmetry: Poisson structures of the pohlmeyer reduction

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Structures of the noncovalent complexes of human and bovine prothrombin fragment 2 with human PPACK-thrombin

Both human and bovine prothrombin fragment 2 (the second kringle) have been cocrystallized separately with human PPACK (D-Phe-Pro-Arg)-thrombin, and the structures of these noncovalent complexes have been determined and refined (R = 0.155 and 0.157, respectively) at 3.3-Å resolution using X-ray crystallographic methods. The kringles interact with thrombin at a site that has previously been proposed to be the heparin binding region. The latter is a highly electropositive surface near the C-terminal helix of thrombin abundant in arginine and lysine residues. These form salt bridges with acidic side chains of kringle 2. Somewhat unexpectedly, the negative groups of the kringle correspond to an enlarged anionic center of the lysine binding site of lysine binding kringles such as plasminogens K1 and K4 and TPA K2. The anionic motif is DGDEE in prothrombin kringle 2. The corresponding cationic center of the lysine binding site region has an unfavorable Arg70Asp substitution, but Lys35 is conserved. However, the folding of fragment 2 is different from that of prothrombin kringle 1 and other kringles: the second outer loop possesses a distorted two-turn helix, and the hairpin β-turn of the second inner loop pivots at Val64 and Asp70 by 60°. Lys35 is located on a turn of the helix, which causes it to project into solvent space in the fragment 2-thrombin complex, thereby devastating any vestige of the cationic center of the lysine binding site. Since fragment 2 has not been reported to bind lysine, it most likely has a different inherent folding conformation for the second outer loop, as has also been observed to be the case with TPA K2 and the urokinase kringle. The movement of the Val64-Asp70 β-turn is most likely a conformational change accompanying complexation, which reveals a new heretofore unsuspected flexibility in kringles. The fragment 2-thrombin complex is only the second cassette module-catalytic domain structure to be determined for a multidomain blood protein and only the third domain-domain interaction to be described among such proteins, the others being factor Xa without a Gla domain and Ca2+ prothrombin fragment 1 with a Gla domain and a kringle. © 1993 American Chemical Society.

Synthesis, characterization and molecular structures of the pyridinium trans-bis(pyridine)tetrachlororuthenate(III) and pyridinium trans-(carbonyl)(pyridine)tetrachlororuthenate(III)

The pyH[trans-RuCl4(py)2](1) and pyH[trans-RuCl4(CO)(py)](2) complexes were synthesized and found to crystallize in space group P21/n, Z = 4 with a = 8.080(7), b = 22.503(7), c = 10.125(6) Å, β = 93.19(6)° for (1) and a = 7.821(1), b = 10.337(3), c = 19.763(3) Å, β = 93.07(1)° for (2). The structures were solved by Patterson and difference Fourier techniques and refined to R = 0.062 for (1) and R = 0.038 for (2). In both cases the Ru(III) ion is octahedrally coordinated to four co-planar chlorine atoms, the nitrogen of the pyridine rings or carbon from the carbon monoxide. Another protonated pyridine group, which forms the counter-cation completes the crystal structures. The UV-Vis absorption spectra show three bands: (1) 360 (ε = 1180 M-1 cm-1), 441 (ε = 3200 M-1 cm-1) and 532 nm (ε = 400 M-1 cm-1); (2) 315(ε = 1150 M-1 cm-1), 442 (ε = 3170 M-1 cm-1) and 530 nm (ε = 390 M-1 cm-1). The two higher energy bands were associated with ligand-to-metal charge transfer transitions and a third band at lower energy was assigned to a d-d transition. Low temperature EPR data confirmed the presence of the paramagnetically active Ru(III) and it is consistent with axial symmetry of the complexes. The position of the stretching CO band in complex (2) is discussed in terms of metal-CO backbonding.

Structure and antimycobacterial activity of the novel organometallic [Pd(C-bzan)(SCN)(dppp)] compound

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Evolution of representation of the hands in plastic arts

A interação entre arte e ciência foi intensa durante o Renascimento, sofrendo declínio nos anos posteriores com retomada significativa no século XX, principalmente com o uso de técnicas de identificação, datação de obras de arte e o desenvolvimento de novos materiais. O relacionamento entre artes plásticas e Cirurgia da Mão mantêm-se intenso , sendo freqüente o uso de reproduções artísticas da mão nas ilustrações de textos científicos. Objetivando compreender o papel da mão nas artes plásticas, reproduções de obras de artes (esculturas e pinturas) representativas de vários estilos ou períodos da história da arte foram analisadas com enfoque no estudo das mãos. Detalhes anatômicos, relacionamento com outras estruturas do corpo humano, papel na composição e aspectos simbólicos das mãos foram estudados no contexto histórico e artístico de obras de arte do período paleolítico (pré-história) até o século XX. A representação da mão nas artes plásticas está diretamente relacionada ao estilo ou período da obra e à capacidade individual de interpretação e execução do artista.

Role of flanking sequences and phosphorylation in the recognition of the simian-virus-40 large T-antigen nuclear localization sequences by importin-alpha

The nuclear import of simian-virus-40 large T-antigen (tumour antigen) is enhanced via phosphorylation by the protein kinase CK2 at Ser(112) in the vicinity of the NLS (nuclear localization sequence). To determine the structural basis of the effect of the sequences flanking the basic cluster KKKRK, and the effect of phosphorylation on the recognition of the NLS by the nuclear import factor importin-alpha (Impalpha), we co-crystallized non-autoinhibited Impalpha with peptides corresponding to the phosphorylated and non-phosphorylated forms of the NLS, and determined the crystal structures of the complexes. The structures show that the amino acids N-terminally flanking the basic cluster make specific contacts with the receptor that are distinct from the interactions between bipartite NLSs and Impalpha. We confirm the important role of flanking sequences using binding assays. Unexpectedly, the regions of the peptides containing the phosphorylation site do not make specific contacts with the receptor. Binding assays confirm that phosphorylation does not increase the affinity of the T-antigen NLS to Impalpha. We conclude that the sequences flanking the basic clusters in NLSs play a crucial role in nuclear import by modulating the recognition of the NLS by Impalpha, whereas phosphorylation of the T-antigen enhances nuclear import by a mechanism that does not involve a direct interaction of the phosphorylated residue with Impalpha.

Evaluation of the beta-glucanolytic enzyme complex of Trichoderma harzianum Rifai for the production of gluco-oligosaccharide fragments by enzymatic hydrolysis of 1,3;1,6-beta-D-glucans

Botryosphaeran, a new exopolysaccharide from the endophytic fungus Botryosphaeria rhodina MAMB-05, and algal laminarin were hydrolyzed by partially-fractionated enzymes of the beta-glucanolytic complex from Trichoderma harzianum Rifai. beta-Glucanase fractions (F-I and F-II) separated by gel permeation chromatography presented different modes of attack on botryosphaeran and laminarin. Botryosphaeran was hydrolyzed to the extent of 66% (F-I) and 98% (F-II) within 30 min, and its main hydrolysis products were gluco-oligosaccharides of DP >= 4, with lesser amounts of glucose, di- and tri-saccharides. The action of enzyme fractions I and II on laminarin resulted in 15% conversion to glucose, while the percentage of saccharification was radically different (70% for F-I and 25% for F-II). The different product arrays within the polysaccharide hydrolysates can be explained by the difference in the enzymes' specificities within each enzyme fraction, and the molecular structures of the polysaccharides and their complexity.

Acetylcholinesterase Inhibitory Pyridine Alkaloids of the Leaves of Senna multijuga

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

Morphology of the walls of the cavernous sinus of Cebus apella (tufted capuchin monkey)

The morphology of the dura mater and its relationship with the structures of the cavernous sinus were analyzed in five tufted capuchin monkeys (Cebus apella) using histological sections, showing that the walls of the cavernous sinus of this species are similar to those of other primates, including man. Except for the medial wall of the cavernous sinus, the remaining walls consist of two distinct dura mater layers. The deep layer of the lateral wall of the cavernous sinus is contiguous to the sheath of the oculomotor, trochlear and ophthalmic nerves. Arterioles, venules, venous spaces, neuronal bodies and nervous fiber bundles are found on this lateral wall.

Final stages of the Brasiliano Orogenesis in SE Brazil: U-Pb and 40Ar/39Ar evidence for overprinting of the Brasília Belt by the Ribeira Belt Tectonics

Around the southern margins of the São Francisco Craton, there is a zone of tectonic interference between the Brasília belt to the west and the younger Ribeira belt to the east. U-Pb monazite and 40Ar/39Ar cooling age determinations carried out in the area reveal the cooling histories of these belts and the timing of tectonic overprint, unraveling the final stages of Brasiliano Orogeny in SE Brazil. The U-Pb monazite data from migmatized paragneisses and late-stage pegmatites in the Socorro-Guaxupé Nappe System of the southern Brasília belt show that migmatization peaked between ca. 613±1 and 607±3 Ma. 40Ar/39Ar biotite and muscovite ages of paragneisses and schists in this area indicate that the northern high-grade core of the Nappe System (Guaxupé Domain) was uplifted and cooled through the 350°C isotherm between 599±1 and 587±1 Ma. In contrast, samples from the southern high-grade core of the Nappe System, the Socorro Domain, south of the Jacutinga shear zone, yields a broader and younger spectrum of 40Ar/39Ar biotite ages between 571±1 and 562±1 Ma, attributed to a later uplift and cooling of the crust. The cooling ages can be assigned to local resetting of the 40Ar/39Ar system during transpressive tectonic overprint due to reactivation as a result of collision of the Ribeira belt. A younger group of 40Ar/39Ar mica ages (537±1 to 521±1Ma) in schists of the Socorro Domain, are associated with transpressional structures of the Ribeira belt. Rock samples from the Jacutinga and Três Corações shear zones, yield 40Ar/39Ar biotite-muscovite ages around 520 Ma. These are typical cooling ages of the Ribeira belt, and are interpreted to mark the western limit of the Ribeira belt transpressional regime within the Brasília belt. The youngest biotite-muscovite cooling ages in schists of the Socorro Domain, between 510±2 and 491±1 Ma, mark the final cooling and exhumation of that part of the Brasília belt.

Influence of arginine vasopressin receptor and nitric oxide on the water, sodium intake and arterial blood pressure induce by angiotensin injected into third ventricle of the brain

As several structures of the central nervous system are involved in the control of hydromineral and cardiovascular balance we investigated whether the natriorhexigenic and pressor response induced by the injection of ANG II into the 3rd V could be mediated by vasopressinergic and nitrergic system. Male Holtzman rats weighing 200-250 g with cannulae implanted into the 3rd V were used. The drugs were injected in 0.5 μL over 30-60 sec. Controls were injected with a similar volume of 0.15 M NaCl. ANGII increased the water intake vs control. AVPA injected into 3rd V prior to ANGII decreased the dipsogenic effect of ANGII. L-arginine also decreased the water intake induced by ANGII. AVPA plus L-arginine inhibit the water intake induced by ANGII. 7NIT injected prior to ANGII potentiated the dipsogenic effect of ANGII. Pre-treatment with ANGII increased the sodium ingestion vs control. AVPA decreased the ANGII effect in sodium intake. L-arginine also decreased the natriorhexigenic effect of ANGII. The combination of L-arginine and AVPA inhibit the sodium intake induced by ANGII. 7NIT injected prior to ANGII potentiated the sodium intake induced by ANGII. ANGII induced an increase in Mean Arterial Pressure (MAP) vs control. AVPA and L-arginine induced a decreased in the pressor effect of ANGII. The combination of L-arginine and AVPA inhibit the pressor effect of ANGII. 7NIT injected prior to ANGII into 3rd V potentiated the pressor effect of ANGII. These data suggest that arginine vasopressin V 1 receptors and Nitric Oxide (NO) within the circumventricular structures may be involved in sodium intake and pressor response induced by the activation of ANGII receptors within the circumventricular neurons. These studies revealed the involvement of sodium appetite by utilizing the angiotensinergic, vasopressinergic and nitrergic system in the central regulation of blood pressure. © 2006 Asian Network for Scientific Information.

Chemical Composition of the Bark of Tetrapterys mucronata and Identification of Acetylcholinesterase Inhibitory Constituents

Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)