Using Geostatistical Analysis to Evaluate the Presence of Rotylenchulus reniformis in Cotton Crops in Brazil: Economic Implications.

In recent years, the productivity of cotton in Brazil has been progressively decreasing, often the result of the reniform nematode Rotylenchulus reniformis. This species can reduce crop productivity by up to 40%. Nematodes can be controlled by nematicides but, because of expense and toxicity, application of nematicides to large crop areas may be undesirable. In this work, a methodology using geostatistics for quantifying the risk of nematicide application to small crop areas is proposed. This risk, in economic terms, can be compared to nematicide cost to develop an optimal strategy for Precision Farming. Soil (300 cm(3)) was sampled in a regular network from a R. reniformis-infested area that was a cotton monoculture for 20 years. The number of nematodes in each sample was counted. The nematode number per volume of soil was characterized using geostatistics, and 100 conditional simulations were conducted. Based on the simulations, risk maps were plotted showing the areas where nematicide should be applied in a Precision Farming context. The methodology developed can be applied to farming in countries that are highly dependent on agriculture, with useful economic implications.

Administration of abciximab to patients receiving tirofiban or eptifibatide: effect on platelet function.

OBJECTIVES: The goal of this study was to evaluate platelet function and to preliminarily assess the clinical safety of sequential treatment with tirofiban or eptifibatide followed by abciximab in patients undergoing percutaneous coronary intervention (PCI). BACKGROUND: An increasing number of acute coronary syndrome (ACS) patients are treated early with tirofiban or eptifibatide. Some later require PCI and may benefit from switching to abciximab, for which long-term benefits have been reported. METHODS: Fifty ACS patients planned for PCI were enrolled. Twenty-five patients received tirofiban followed by abciximab. Ten patients received eptifibatide followed by abciximab. Fifteen patients received only abciximab. All patients had blood samples drawn six times during the therapeutic course. Platelet function was evaluated by ADP- and TRAP-induced aggregation, flow cytometry analysis of fibrinogen binding and the cone and plate(let) analyzer, which tests shear rate-dependent platelet activation. RESULTS: Administered after tirofiban, abciximab caused a significant further decline in platelet function, as evidenced by all methods. Administered after eptifibatide, abciximab caused a significant further reduction in platelet function, as assessed by the cone and plate(let) analyzer and fibrinogen binding methods. The platelet inhibition achieved by the combination therapy was always greater than or equal to that achieved by abciximab alone. There were no major bleeding or severe thrombocytopenia episodes. Three of the 35 combination therapy patients and one of the 15 who received abciximab alone had minor bleeding. CONCLUSIONS: This is the first in vivo study of combination intravenous platelet glycoprotein IIb/IIIa inhibitor therapy. Administration of abciximab immediately after tirofiban or eptifibatide therapy effectively inhibits platelet function and appears to be safe.

Isolation and sequence of the MIG1 homologue from the yeast Candida utilis.

The Mig1p repressor from the food yeast Candida utilis has been isolated using a homologous PCR hybridization probe. This probe was amplified with two sets of degenerate primers designed on the basis of highly conserved motifs in the DNA-binding region (zinc-finger domain) from yeast Mig1p and fungi CreA repressors. The cloned gene was sequenced and found to encode a polypeptide of 345 amino acids which shows significant identity with other yeast and fungus repressors in the DNA-binding domain and also with the yeast Mig1 proteins in the C-terminal region (effector domain). The MIG1 repressor gene from C. utilis was able to complement functionally the mig1 mutation of S. cerevisiae. The sequence presented here has been deposited in the EMBL data library under Accession No. AJ277830.

Purification, characterization and immobilization of proteinase inhibitors from Stichodactyla helianthus.

Isolation of proteinase inhibitors from the sea anemone Stichodactyla helianthus was achieved by trichloroacetic acid treatment of the aqueous extract followed by affinity chromatography on trypsin-Sepharose and ion-exchange chromatography on CM-cellulose. The average molecular mass of the major inhibitor (ShPI-I) obtained by fast atom bombardment mass spectrometry (FAB-MS) was 6110.6 Da. The amino acid sequence was determined by FAB-MS combined with manual Edman degradation, digestions with endopeptidases and exopeptidases and automatic sequencing. The sequence of ShPI-I (55 amino acids) was compared with those reported in the SwissProt database for several proteinase inhibitors and significant similarity to inhibitors belonging to the Kunitz family was observed. ShPI-I exhibits a broad specificity for serine, cysteine and aspartic proteinases. The dissociation constants of the complexes formed with different enzymes were determined. The affinity-purified fraction (PI) was immobilized on Sepharose and used in the purification of different classes of proteinases.

Proteinase inhibitor from Stichodactyla helianthus: purification, characterization and immobilization.

A Kunitz type proteinase inhibitor was isolated from extracts of the sea anemone Stichodactyla helianthus. The purification procedure comprises treatment with trichloroacetic acid followed by affinity chromatography on trypsin-Sepharose and gel filtration on Sephadex G-50 or ion exchange chromatography on CM-cellulose. The major inhibitor (isoelectric point 8.4) is a small protein consisting of 55 amino acid residues lacking tryptophan and methionine, with a molecular weight of 6110 (FAB-MS). The amino acid sequence and the structure in solution (NMR) were determined. The inhibitor exhibits a broad specificity for serine, cysteine and aspartic proteinases. Reactors were prepared with immobilized inhibitor in different supports (Sepharose, cellulose, and silica gel) to be employed in the elimination of undesirable proteinases and the purification of different kinds of proteolytic enzymes.

The NMR solution structure of a Kunitz-type proteinase inhibitor from the sea anemone Stichodactyla helianthus.

The solution structure of a 55-amino-acid Kunitz-type proteinase inhibitor, ShPI, purified from the Caribbean sea anemone Stichodactyla helianthus, was determined by NMR spectroscopy. Nearly complete sequence-specific 1H-NMR assignments were obtained at pH 4.6 and 36 degrees C, and stereo-specific assignments were determined for 23 pairs of diastereotopic substituents. A data set of 666 upper distance limit constraints and 122 dihedral angle constraints collected on this basis was used as input for a structure calculation with the program DIANA. Following energy minimization with the program OPAL, the average root-mean-square diviation (RMSD) of the 20 DIANA conformers used to represent the solution structure relative to the mean structure is 61 pm for all backbone atoms N, C alpha and C', and 106 pm for all heavy atoms of residues 2-53. This high-quality solution structure of ShPI has a nearly identical molecular architecture as the bovine pancreatic trypsin inhibitor (BPTI), despite a mere 35% of sequence similarity between the two proteins. Exchange rates measured for 48 out of the 51 backbone amide protons showed that the positions of 20 slowly exchanging amide protons correlate well with hydrogen bonds involving these protons in the energy-minimized solution structure. The solution structure of ShPI is compared to the four homologous proteins for which the three-dimensional structure is also available.

[Measles and subcutaneous emphysema. Presentation of 3 cases]. / Sarampión y enfisema subcutáneo. Presentación de tres casos.

This is a three case study report of children with measles which later progressed to bronchopneumonia and subcutaneous emphysema. All three children were from farming families, and none had been previously vaccinate against measles. For a period of six months, 183 cases of measles were treated at our hospital of which only three worsened to subcutaneous emphysema, demonstrating an incidence rate of 1.6%; they also showed to have bronchopneumonia, with severe coughing episodes; which made us recall the possible physiopathology principle of the pressure gradient theory behind this complication proposed by Bloch in 1968. The factors related to our patients suggested a more severe and aggresive type of measles with a greater probability of having complications. The prognostic value of the severity of this type of measles in the presence of subcutaneous emphysema is limited and its management should be primarly focused on treating the added bronchial problem.