Contextualização da pesca mundial de lagostas e características de comercialização de Scyllarides spp. E Panulirus spp. na Baixada Santista, estado de São Paulo, Brasil

This study aimed to contextualize the world's lobster fishing and identify the characteristics of their trades in Santos region (SP). For this purpose, were realized surveys about the captures of 56 years referring the families traded in the world through the informations supplied by the FAO (Food and Agriculture Organization). To State of São Paulo, consults were made in the data base Propesq (Fishing Institute) about the fishing and prices. Besides interviews in fishmonger, businessmen of fishing and restaurant, we observed the trade and the economical potential compared the lobsters Scyllarides spp. and Panulirus spp. The worldwide the family Nephropidae is the one that has been presenting bigger growth in the captures from 1950 and the one that has the biggest observed captures, the Palinuridae showed a little growth of the captures up to the 80' years, and leaving from there it is oscillating without many expressive changes; Scyllarides began to stand out as fisheries only 70' in Asia, precisely where the other two Families had low catches proportional. In the State of São Paulo, two types of lobsters are sold in Baixada Santista, with conspicuous differences in prices between them. There is also a difference in the flow of trade in relation to active fishing gear. Traders notice a decrease in both abundance and size of individuals of both genders and a clear preference to sell the slippers lobsters (Scyllarides spp.) both for the quality of meat as the lowest price.

Characterization of small-scale fisheries in the Camamu-Almada basin, southeast state of Bahia, Brazil

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Structure and biological activities of eumenine mastoparan-AF (EMP-AF), a new mast cell degranulating peptide in the venom of the solitary wasp (Anterhynchium flavomarginatum micado)

A new mast cell degranulating peptide, eumenine mastoparan-AF (EMP-AF), was isolated from the venom of the solitary wasp Anterhynchium flavomarginatum micado, the most common eumenine wasp found in Japan. The structure was analyzed by FAB-MS/MS together with Edman degradation, which was corroborated by solid-phase synthesis. The sequence of EMP-AF, Ile-Asn-Leu-Leu-Lys-Ile-Ala-Lys-Gly-Ile-lle-Lys-Ser-Leu-NH(2), was similar to that of mastoparan, a mast cell degranulating peptide from a hornet venom; tetradecapeptide with C-terminus amidated and rich in hydrophobic and basic amino acids. In fact, EMP-AF exhibited similar activity to mastoparan in stimulating degranulation from rat peritoneal mast cells and RBL-2H3 cells. It also showed significant hemolytic activity in human erythrocytes. Therefore, this is the first example that a mast cell degranulating peptide is found in the solitary wasp venom. Besides the degranulation and hemolytic activity, EMP-AF also affects on neuromuscular transmission in the lobster walking leg preparation. Three analogs EMP-AF-1 similar to 3 were snythesized and biologically tested together with EMP-AF, resulting in the importance of the C-terminal amide structure for biological activities. (C) 2000 Elsevier B.V. Ltd. All rights reserved.

Molecular determinants of binding of a wasp toxin (PMTXs) and its analogs in the Na+ channels proteins

The structural specificity of alpha-PMTX, a novel peptide toxin derived from wasp venom has been studied on the neuromuscular synapse in the walking leg of the lobster. alpha-PMTX is known to induce repetitive action potentials in the presynaptic axon due to sodium channel inactivation. We synthesized 29 analogs of alpha-PMTX by substituting one or two amino acids and compared threshold concentrations of these mutant toxins for inducing repetitive action potentials. In 13 amino acid residues of alpha-PMTX, Arg-1, Lys-3 and Lys-12 regulate the toxic activity because substitution of these basic amino acid residues with other amino acid residues greatly changed the potency. Determining the structure-activity relationships of PMTXs will help clarifying the molecular mechanism of sodium channel inactivation. (C) 2000 Elsevier B.V. Ireland Ltd. All rights reserved.

A new class of neurotoxin from wasp venom slows inactivation of sodium current

The effects of alpha-pompilidotoxin (alpha-PMTX), a new neurotoxin isolated from the venom of a solitary wasp, were studied on the neuromuscular synapses in lobster walking leg and the rat trigeminal ganglion (TG) neurons. Paired intracellular recordings from the presynaptic axon terminals and the innervating lobster leg muscles revealed that alpha-PMTX induced long bursts of action potentials in the presynaptic axon, which resulted in facilitated excitatory and inhibitory synaptic transmission. The action or alpha-PMTX was distinct from that of other known facilitatory presynaptic toxins, including sea anemone toxins and alpha-scorpion toxins, which modify the fast inactivation of Na+ current. We further characterized the action of alpha-PMTX on Na+ channels by whole-cell recordings from rat trigeminal neurons. We found that alpha-PMTX stowed the Na+ channels inactivation process without changing the peak current-voltage relationship or the activation time course of tetrodotoxin (TTX)-sensitive Na+ currents, and that alpha-PMTX had voltage-dependent effects on the rate of recovery from Na+ current inactivation and deactivating tail currents. The results suggest that alpha-PMTX slows or blocks conformational changes required for fast inactivation of the Na+ channels on the extracellular surface. The simple structure of alpha-PMTX, consisting of 13 amino acids, would be advantageous for understanding the functional architecture of Na+ channel protein.

Novel wasp toxin discriminates between neuronal and cardiac sodium channels

Pompilidotoxins (PMTXs), derived from the venom of solitary wasp has been known to facilitate synaptic transmission in the lobster neuromuscular junction, and a recent further study from rat trigeminal neurons revealed that the toxin slows Na+ channel inactivation without modifying activation process. Here we report that beta -PMTX modifies rat brain type II Na+ channel alpha -subunit (rBII) expressed in human embryonic kidney cells but fails to act on the rat heart alpha -subunit (rH1) at similar concentrations. We constructed a series of chimeric mutants of rBII and rH1 Na+ channels and compared modification of the steady-state Na+ currents by beta -PMTX. We found that a difference in a single amino acid between Glu-1616 in rBII and Gln-1615 in rH1 at the extracellular loop of D4S3-S4 is crucial for the action of beta -PMTX. PMTXs, which are small peptides with 13 amino acids, would be a potential tool for exploring a new functional moiety of Na+ channels.

Força de reação do solo (vertical) de indivíduos realizando exercício de hidroginástica em ambiente terrestre e aquático

Pós-graduação em Engenharia Mecânica - FEG

Outra banda: lugar de quem?

Pós-graduação em Geografia - IGCE

Taxonomia e distribuição das lagostas (Crustacea: Decapoda: Achelata e Polychelida) no Oceano Atlântico

Pós-graduação em Ciências Biológicas (Zoologia) - IBRC

Slipper lobsters (Scyllaridae) off the southeastern coast of Brazil: relative growth, population structure, and reproductive biology

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)