Morphogenesis of galls induced by Baccharopelma dracunculifoliae (Hemiptera: Psyllidae) on Baccharis dracunculifolia (Asteraceae) leaves

The commonest insect gall on Baccharis dracunculifolia (Asteraceae) leaves is induced by Baccharopelma dracunculifoliae (Hemiptera, Psyllidae). The gall-inducing insect attacks young leaves in both the unfolded and the fully expanded stages. Four developmental phases were observed in this type of gall: 1) A folding phase, during which the leaf lamina folded upward alongside the midrib and the edges of the upper portion of the leaf approached each other, forming a longitudinal slit. A single chamber was formed on the adaxial surface of the leaf; 2) A swelling phase, in which the folded leaf tissues thickened and the edges of the leaf drew closer together, narrowing the slit. In this phase the gall matured, turning succulent, fusiform and pale green. The single nymphal chamber was lined with white wax and was able to house from one to several nymphs; 3) A dehiscence phase, characterized by the opening of the slit to release inducers; and 4) A senescence phase, when the gall turned dark and dry. The dermal system of the mature gall was composed of a single-layered epidermis. The mesophyll was swollen, and the swelling was due mainly to hyperplasia of the parenchyma. The vascular tissues along the midrib vein were conspicuous and the perivascular fibers resembled parenchymal cells. The hypertrophied secretory cavities contained low lipophylic content. This gall does not form nutritive tissue, but salivary sheaths left by the inducers were observed near the parenchyma, vascular bundles and secretory cavities. This study complements our current knowledge of gall biology and sheds further light on the plasticity of plant tissues stimulated by biotic factors

Contribuições para a adaptação de inventários de ciclo de vida de madeira serrada utilizada em estrutura de telhados no estado de São Paulo

Este trabalho teve como objetivo desenvolver o inventário de ciclo de vida para madeira empregada na estrutura de telhado de edificações populares do Estado de São Paulo, com base na adaptação de inventários existentes na base de dados ecoinvent (versão 3.1) para a realidade da produção madeireira no Brasil. Considerou-se como sistema de produto a produção de 1m3 de madeira serrada de cambará proveniente de manejo florestal sustentável na Amazônia, desde a extração das toras até a peça de madeira serrada estocada em São Paulo. As informações nacionais foram obtidas da literatura. A despeito das semelhanças entre o sistema de produto da base ecoinvent e a realidade nacional na extração das toras na floresta, há diferenças referentes ao transporte até a serraria, ao desdobro das toras e à geração e destinação de resíduos: no Brasil, todas as etapas são executadas próximas à região de exploração, resultando em alterações no modelo de transporte, máquinas empregadas e resíduos gerados. Além disso, os valores de consumo de diesel e eletricidade apresentaram ordens de grandeza diferentes dos ICVs de referência. Com base nessa análise, conclui-se que a estrutura de dados dos ICVs existentes na base ecoinvent auxilia a construção de inventários nacionais e que a adaptação dos inventários é imprescindível para a realização de estudos de avaliação do ciclo de vida condizentes com as condições do Brasil. Entretanto, considerando as diferenças observadas, é recomendada a apuração dos índices de consumo nacionais por meio de verificação e coleta de dados inloc

N- and C-terminal modifications of nociceptin/orphanin FQ generate highly potent NOP receptor ligands

.Previous structure-activity studies on nociceptin/orphanin FQ (N/OFQ) identified [Phe1\ube(CH2- NH)Gly2]N/OFQ(1-13)-NH2 and [Nphe1]N/OFQ(1-13)-NH2 as a N/OFQ peptide receptor (NOP) partial agonist and pure antagonist, respectively. The addition of fluorine to the Phe4 or the insertion of a further pair of basic amino acids Arg14-Lys15 generate potent agonists. On the basis of these findings, we combined in the N/OFQ-NH2 template the chemical modifications Arg14-Lys15 and (pF)Phe4 that increase the agonist potency with those conferring partial agonist (Phe1\ube(CH2NH)Gly2) or pure antagonist (Nphe1) properties. Twelve peptides were synthesized and pharmacologically evaluated in Chinese hamster ovary cells expressing the human recombinant NOP and in electrically stimulated mouse vas deferens and guinea pig ileum assays. All peptides behaved as NOP ligands; the chemical modifications Arg14-Lys15 and (pF)- Phe4 increased ligand affinity/potency. Peptides with the normal Phe1-Gly2 peptide bond behaved as full agonists, and those with the Phe1\ube(CH2NH)Gly2 modification behaved as partial agonists, while those with the Nphe1 modification behaved as partial agonists or pure antagonists depending on the presence or absence of the (pF)Phe4 modification, respectively. The full agonist [(pF)Phe4,Arg14,Lys15]N/OFQ-NH2, the partial agonist [Phe1\ube(CH2NH)- Gly2,(pF)Phe4,Arg14,Lys15]N/OFQ-NH2, and the pure antagonist [Nphe1,Arg14,Lys15]N/OFQ-NH2 represent the most potent peptide ligands for NOP

N- and C-terminal modifications of nociceptin/orphanin FQ generate highly potent NOP receptor ligands

Previous structure-activity studies on nociceptin/orphanin FQ (N/OFQ) identified [Phe1¾(CH2- NH)Gly2]N/OFQ(1-13)-NH2 and [Nphe1]N/OFQ(1-13)-NH2 as a N/OFQ peptide receptor (NOP) partial agonist and pure antagonist, respectively. The addition of fluorine to the Phe4 or the insertion of a further pair of basic amino acids Arg14-Lys15 generate potent agonists. On the basis of these findings, we combined in the N/OFQ-NH2 template the chemical modifications Arg14-Lys15 and (pF)Phe4 that increase the agonist potency with those conferring partial agonist (Phe1¾(CH2NH)Gly2) or pure antagonist (Nphe1) properties. Twelve peptides were synthesized and pharmacologically evaluated in Chinese hamster ovary cells expressing the human recombinant NOP and in electrically stimulated mouse vas deferens and guinea pig ileum assays. All peptides behaved as NOP ligands; the chemical modifications Arg14-Lys15 and (pF)- Phe4 increased ligand affinity/potency. Peptides with the normal Phe1-Gly2 peptide bond behaved as full agonists, and those with the Phe1¾(CH2NH)Gly2 modification behaved as partial agonists, while those with the Nphe1 modification behaved as partial agonists or pure antagonists depending on the presence or absence of the (pF)Phe4 modification, respectively. The full agonist [(pF)Phe4,Arg14,Lys15]N/OFQ-NH2, the partial agonist [Phe1¾(CH2NH)- Gly2,(pF)Phe4,Arg14,Lys15]N/OFQ-NH2, and the pure antagonist [Nphe1,Arg14,Lys15]N/OFQ-NH2 represent the most potent peptide ligands for NOP

Structure-activity studies on neuropeptide S - Identification of the amino acid residues crucial for receptor activation

Neuropeptide S (NPS) has been recently recognized as the endogenous ligand for the previous orphan G-protein-coupled receptor GPR154, now referred to as the NPS receptor (NPSR). The NPS-NPSR receptor system regulates important biological functions such as sleeping/wakening, locomotion, anxiety, and food intake. To collect information on the mechanisms of interaction between NPS and its receptor, a classical structure-activity relationship study was performed. Human (h) NPS derivatives obtained by Ala and D-scan and N- and C-terminal truncation were assessed for their ability to stimulate calcium release in HEK293 cells expressing the human recombinant NPSR. The results of this study indicate that (i) the effect of hNPS is mimicked by the fragment hNPS- (1-10); (ii) Phe2, Arg3, and Asn4 are crucial for biological activity; (iii) the sequence Thr8-Gly9-Met10 is important for receptor activation, although with non-stringent chemical requirements; and (iv) the sequence Val6-Gly7 acts as a hinge region between the two above-mentioned domains. However, the stimulatory effect of hNPS given intracerebroventricularly on mouse locomotor activity was not fully mimicked by hNPS-(1-10), suggesting that the C-terminal region of the peptide maintains importance for in vivo activity. In conclusion, this study identified the amino acid residues of this peptide most important for receptor activation