In elderly patients with optimally treated CHF, meditation reduced NE, improved quality of life, and reduced the VE/VCO(2) slope. Our results support the possible role of meditation as a new hope in the treatment of CHF.

Abstract. The diagnosis of strongyloidiasis relies upon the identification of the parasite in stool samples. In 1981, a serologic assay was developed, which was useful in the diagnosis of strongyloidiasis in the immunocompetent host. In the present study, we evaluated the enzyme-linked immunosorbent assay (ELISA) in patients with hematologic malignancies. Between April 1995 and December 1998, sera from 164 consecutive patients were tested for the presence of IgG antibody to Strongyloides stercoralis. Patient was considered uninfected after at least three negative stool examinations. The prevalence of strongyloidiasis was 13%. The underlying diseases were acute leukemia in 21% and lymphoma in 52% of the patients. The majority of the patients were receiving chemotherapy (93%) and steroids (76%). The sensitivity, specificity, and positive and negative predictive values were 68%, 89%, 48%, and 95%, respectively. The ELISA may be an excellent assay to rule out the diagnosis of strongyloidiasis in patients with hematologic malignancies.

Hymenoptera venoms are complex mixtures containing simple organic molecules, proteins, peptides, and other bioactive elements. Several of these components have been isolated and characterized, and their primary structures determined by biochemical techniques. These compounds are responsible for many toxic or allergic reactions in different organisms, such as local pain, inflammation, itching, irritation, and moderate or severe allergic reactions. The most extensively characterized Hymenoptera venoms are bee venoms, mainly from the Apis genus and also from social wasps and ant species. However, there is little information about other Hymenoptera groups. The Apis venom presents high molecular weight molecules - enzymes with a molecular weight higher than 10.0 kDa - and peptides. The best studied enzymes are phospholipase A2, responsible for cleaving the membrane phospholipids, hyaluronidase, which degrades the matrix component hyaluronic acid into non-viscous segments and acid phosphatase acting on organic phosphates. The main peptide compounds of bee venom are lytic peptide melittin, apamin (neurotoxic), and mastocyte degranulating peptide (MCD)

Lysine-ketoglutarate reductase catalyzes the first step of lysine catabolism in maize (Zea mays L.) endosperm. The enzyme condenses L-lysine and a-ketoglutarate into saccharopine using NADPH as cofactor. It is endosperm-specific and has a temporal pattern of activity, increasing with the onset of kernel development, reaching a peak 20 to 25 days after pollination, and thereafter decreasing as the kernel approaches maturity. The enzyme was extracted from the developing maize endosperm and partially purified by ammonium-sulfate precipitation, anion-exchange chromatography on DEAE-cellulose, and affinity chromatography on Blue-Sepharose CL-6B. The preparation obtained from affinity chromatography was enriched 275-fold and had a specific activity of 411 by the opaque-2 mutation may explain, at least in part, the elevated concentration of lysine found in the opaque-2 endosperm.There is little information on lysine catabolism in higher plants. Most of the available data were obtained in studies on the incorporation and metabolism of radiolabeled precursors by plant tissues. Feeding experiments with ["4C]lysine demonstrated the incorporation of radioactivity into a-amino adipic acid and glutamic acid in wheat (18) and into saccharopine and diaminopimelic acid in maize and barley (16,26). In developing endosperm of maize and barley, radiolabeled lysine is incorporated primarily into glutamic acid and proline (4, 26). These findings indicate that lysine is catabolized in plants via the saccharopine pathway.The first enzymatic evidence for the operation of the saccharopine pathway for lysine catabolism in plants was obtained with the demonstration of LKR3 activity in immature endosperm of maize (3). LKR (EC 1.5.1.8) condenses lysine and a-ketoglutarate into saccharopine using NADPH as cofactor.An understanding of the pathways for lysine biosynthesis and degradation in plants has enormous importance because of the limiting concentration of this essential amino acid in major food sources such as cereals. Valuable information can be obtained by the elucidation of the properties of enzymes involved in the biosynthesis and catabolism of lysine and by the use of mutants in which the activities of the enzymes are altered.Since the discovery of the superior nutritive value of the high lysine maize mutant opaque-2 (15), there have been many studies on the effects of this mutant gene on protein and amino acid metabolism in maize endosperm. The opaque-2 gene is located on the short arm of chromosome 7 and its major effect is the reduction of the maize storage protein zein. This is a complex of polypeptides coded by a multigenic family located on chromosomes 4 and 7 (23). The opaque-2 gene in the homozygous form reduces the zein content of the endosperm by up to 70% (6). The reduction is

In this study, we describe the cDNA cloning, sequencing, and 3-D structure of the allergen hyaluronidase from Polybia paulista venom (Pp-Hyal). Using a proteomic approach, the native form of Pp-Hyal was purified to homogeneity and used to produce a Pp-specific polyclonal antibody. The results revealed that Pp-Hyal can be classified as a glycosyl hydrolase and that the full-length Pp-Hyal cDNA (1315 bp; GI: 302201582) is similar (80-90%) to hyaluronidase from the venoms of endemic Northern wasp species. The isolated mature protein is comprised of 338 amino acids, with a theoretical pI of 8.77 and a molecular mass of 39,648.8 Da versus a pI of 8.13 and 43,277.0 Da indicated by MS. The Pp-Hyal 3D-structural model revealed a central core (α/β)(7) barrel, two sulfide bonds (Cys 19-308 and Cys 185-197), and three putative glycosylation sites (Asn79, Asn187, and Asn325), two of which are also found in the rVes v 2 protein. Based on the model, residues Ser299, Asp107, and Glu109 interact with the substrate and potential epitopes (five conformational and seven linear) located at surface-exposed regions of the structure. Purified native Pp-Hyal showed high similarity (97%) with hyaluronidase from Polistes annularis venom (Q9U6V9). Immunoblotting analysis confirmed the specificity of the Pp-Hyal-specific antibody as it recognized the Pp-Hyal protein in both the purified fraction and P. paulista crude venom. No reaction was observed with the venoms of Apis mellifera, Solenopsis invicta, Agelaia pallipes pallipes, and Polistes lanio lanio, with the exception of immune cross-reactivity with venoms of the genus Polybia (sericea and ignobilis). Our results demonstrate cross-reactivity only between wasp venoms from the genus Polybia. The absence of cross-reactivity between the venoms of wasps and bees observed here is important because it allows identification of the insect responsible for sensitization, or at least of the phylogenetically closest insect, in order to facilitate effective immunotherapy in allergic patients.

Fireflies emit flashes in the green-yellow region of the spectrum for the purpose of sexual attraction. The bioluminescence color is determined by the luciferases. It is well known that the in vitro bioluminescence color of firefly luciferases can be shifted toward the red by lower pH and higher temperature; for this reason they are classified as pH-sensitive luciferases. However, the mechanism and structural origin of pH sensitivity in fireflies remains unknown. Here we report the cloning of a new luciferase from the Brazilian twilight active firefly Macrolampis sp2, which displays an unusual bimodal spectrum. The recombinant luciferase displays a sensitive spectrum with the peak at 569 nm and a shoulder in the red region. Comparison of the bioluminescence spectra of Macrolampis, Photinus and Cratomorphus firefly luciferases shows that the distinct colors are determined by the ratio between green and red emitters under luciferase influence. Comparison of Macrolampis luciferase with the highly similar North American Photinus pyralis luciferase (91%) showed few substitutions potentially involved with the higher spectral sensitivity in Macrolampis luciferase. Site-directed mutagenesis showed that the natural substitution E354N determines the appearance of the shoulder in the red region of Macrolampis luciferase bioluminescence spectrum, helping to identify important interactions and residues involved in the pH-sensing mechanism in firefly luciferases.

Polybia paulista (Hymenoptera: Vespidae) is a neotropical social wasp from southeast Brazil. As most social Hymenoptera, venom from P. paulista comprises a complex mixture of bioactive toxins ranging from low molecular weight compounds to peptides and proteins. Several efforts have been made to elucidate the molecular composition of the P. paulista venom. Data derived from proteomic, peptidomic and allergomic analyses has enhanced our understanding of the whole envenoming process caused by the insect sting. The combined use of bioinformatics, -omics- and molecular biology tools have allowed the identification, characterization, in vitro synthesis and recombinant expression of several wasp venom toxins. Some of these P. paulista - derived bioactive compounds have been evaluated for the rational design of antivenoms and the improvement of allergy specific diagnosis and immunotherapy. Molecular characterization of crude venom extract has enabled the description and isolation of novel toxins with potential biotechnological applications. Here, we review the different approaches that have been used to unravel the venom composition of P. paulista. We also describe the main groups of P. paulista - venom toxins currently identified and analyze their potential in the development of component-resolved diagnosis of allergy, and in the rational design of antivenoms and novel bioactive drugs.

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