Plasma levels of transthyretin and retinol-binding protein in child-a cirrhotic patients in relation to protein-calorie status and plasma amino acids, zinc, vitamin a and plasma thyroid hormones

Transthyretin and retinal-binding protein are sensitive markers of acute protein-calorie malnutrition both for early diagnosis and dietary evaluation. A preliminary study showed that retinal-binding protein is the most sensitive marker of protein-calorie malnutrition in cirrhotic patients, even those with the mild form of the disease (Child A). However, in addition to being affected by protein-calorie malnutrition, the levels of these short half-life-liver-produced proteins are also influenced by other factors of a nutritional (zinc, tryptophan, vitamin A, etc) and non-nutritional (sex, aging, hormones, renal and liver functions and inflammatory activity) nature. These interactions were investigated in 11 adult male patients (49.9 ± 9.2 years of age) with alcoholic cirrhosis (Child-Pugh grade A) and with normal renal function. Both transthyretin and retinol binding protein were reduced below normal levels in 55% of the patients, in close agreement with their plasma levels of retinal. In 67% of the patients (4/6), the reduced levels of transthyretin and retinal-binding protein were caused by altered liver function and in 50% (3/6) they were caused by protein-calorie malnutrition. Thus, the present data, taken as a whole, indicate that reduced transthyretin and retinal-binding protein levels in mild cirrhosis of the liver are mainly due to liver failure and/or vitamin A status rather than representing an isolated protein-calorie malnutrition indicator.

Spectroscopic study of the interaction of Nd3+ with amino acids: Phenomenological 4f-4f intensity parameters

We have studied the bevahior of the phenomenological 4f-4f intensity parameters in compounds of the Nd ion with glycine, L-aspartic acid, L-glutamic acid, L-histidine, DL-malic acid and Aspartame™ in aqueous solution, as a function of the pK values and partial charges on the oxygens of the carboxylate groups of these molecules. The results are discussed and qualitatively interpreted in terms of the forced electric dipole and dynamic coupling mechanisms of the 4f-4f intensities, thus indicating that the forced electric dipole mechanism is dominant.

Competition between humic substances and α-amino acids by metal species

The aim of the present work was to carry out experimental comparison between humic substances (HS) and representative α-amino acids (methionine, methionine sulfoxide and cysteine hydrochloride) in relation to the complexation of biologically active trace elements (Al, Cu, Pb, Mn, Zn, Cd and Ni). A mobile time-controlled tangential-flow UF technique was applied to differentiate between HS-metal and α-aminoacids-metal complexes. Metal determinations were conventionally carried out using a ICP-OES. The results showed that HS may be considered as a selective complexing agents with higher metal bonding capability in relation to Al, Cu and Pb, the fact that may be clinically important.

ZmPUMP encodes a fully functional monocot plant uncoupling mitochondrial protein whose affinity to fatty acid is increased with the introduction of a His pair at the second matrix loop

Uncoupling proteins (UCPs) are specialized mitochondrial transporter proteins that uncouple respiration from ATP synthesis. In this study, cDNA encoding maize uncoupling protein (ZmPUMP) was expressed in Escherichia coli and recombinant ZmPUMP reconstituted in liposomes. ZmPUMP activity was associated with a linoleic acid (LA)-mediated H+ efflux with Km of 56.36 ± 0.27 μM and Vmax of 66.9 μmol H+ min-1 (mg prot)-1. LA-mediated H+ fluxes were sensitive to ATP inhibition with Ki of 2.61 ± 0.36 mM (at pH 7.2), a value similar to those for dicot UCPs. ZmPUMP was also used to investigate the importance of a histidine pair present in the second matrix loop of mammalian UCP1 and absent in plant UCPs. ZmPUMP with introduced His pair (Lys155His and Ala157His) displayed a 1.55-fold increase in LA-affinity while its activity remained unchanged. Our data indicate conserved properties of plant UCPs and suggest an enhancing but not essential role of the histidine pair in proton transport mechanism. © 2006 Elsevier Inc. All rights reserved.

Spatio-temporal distribution of fatty acid-binding protein 6 (fabp6) gene transcripts in the developing and adult zebrafish (Danio rerio)

We have determined the structure of the fatty acid-binding protein 6 (fabp6) gene and the tissue-specific distribution of its transcripts in embryos, larvae and adult zebrafish (Danio rerio). Like most members of the vertebrate FABP multigene family, the zebrafish fabp6 gene contains four exons separated by three introns. The coding region of the gene and expressed sequence tags code for a polypeptide of 131 amino acids (14 kDa, pI 6.59). The putative zebrafish Fabp6 protein shared greatest sequence identity with human FABP6 (55.3%) compared to other orthologous mammalian FABPs and paralogous zebrafish Fabps. Phylogenetic analysis showed that the zebrafish Fabp6 formed a distinct clade with the mammalian FABP6s. The zebrafish fabp6 gene was assigned to linkage group (chromosome) 21 by radiation hybrid mapping. Conserved gene synteny was evident between the zebrafish fabp6 gene on chromosome 21 and the FABP6/Fabp6 genes on human chromosome 5, rat chromosome 10 and mouse chromosome 11. Zebrafish fabp6 transcripts were first detected in the distal region of the intestine of embryos at 72 h postfertilization. This spatial distribution remained constant to 7-day-old larvae, the last stage assayed during larval development. In adult zebrafish, fabp6 transcripts were detected by RT-PCR in RNA extracted from liver, heart, intestine, ovary and kidney (most likely adrenal tissue), but not in RNA from skin, brain, gill, eye or muscle. In situ hybridization of a fabp6 riboprobe to adult zebrafish sections revealed intense hybridization signals in the adrenal homolog of the kidney and the distal region of the intestine, and to a lesser extent in ovary and liver, a transcript distribution that is similar, but not identical, to that seen for the mammalian FABP6/Fabp6 gene. © 2008 The Authors.

Light emission from tryptophan oxidation by hypobromous acid

The emission of ultraweak light from cells is a phenomenon associated with the oxidation of biomolecules by reactive oxygen species. The indole moiety present in tryptophan, serotonin and melatonin is frequently associated with the emission of light during the oxidation of these metabolites. This study presents results for hypobromous acid (HOBr) oxidation of tryptophan as a putative endogenous source of ultraweak light emission. We found that chemiluminescence elicited by the oxidation of tryptophan by HOBr was significantly higher than by hypochlorous acid (HOCl). This difference was related to secondary oxidation reactions, which were more intense using HOBr. The products identified during oxidation by HOCl, but depleted by using HOBr, were N-formylkynurenine, kynurenine, 1,2,3,3a,8,8a-hexahydro-3a-hydroxypyrrolo[2,3-b]-indole-2-carboxylic acid, oxindolylalanine and dioxindolylalanine. The emission of light is dependent on the free α-amino group of tryptophan, and hence, the indole of serotonin and melatonin, although efficiently oxidized, did not produce chemiluminescence. The emission of light was even greater using taurine monobromamine and dibromamine as the oxidant compared to HOBr. A mechanism based on bromine radical intermediates is suggested for the higher efficiency in light emission. Altogether, the experimental evidence described in the present study indicates that the oxidation of free tryptophan or tryptophan residues in proteins is an important source of ultraweak cellular emission of light. This light emission is increased in the presence of taurine, an amino acid present in large amounts in leukocytes, where this putative source of ultraweak light emission is even more relevant.

Free Amino Acids in Pacu, Piaractus mesopotamicus, Eggs and Larvae

Free amino acids (FAA) are used principally as substrate in protein synthesis and the source of energy in aerobic catabolism. In marine fish, embryo and larvae FAA are used to maintain body fluid osmolality during fish early development. However, there is essentially no information about FAA concentrations in early ontogeny of freshwater neotropical species in comparison to marine fishes. Therefore, the aim of this study was to evaluate the FAA concentrations in pacu, Piaractus mesopotamicus, eggs and larvae. Broodstock fish were induced to spawn and ovulated females were stripped of their eggs and immediately sampled for analysis. Larvae were sampled right after hatching (HL) and after the completion of the yolk-sac absorption (YSA). The wet weight of the HL and YSA larvae amounted to 0.5±0.1mg and 1.1±0.3mg, respectively. HL larvae showed higher levels of most of the indispensable amino acids (IAA) in comparison to eggs and YSA larvae. Exceptions were observed with His and Trp that showed higher or similar levels, respectively, in YSA larvae. The FAA Orn, Tau, Glu, Gln, Gly, and Tyr increased concentrations in both larval stages while that of Tau was found in higher concentration in all analyzed stages. Also, the concentrations of Asn, Ala, Pro, Ser, and Asp were higher in HL larvae. Both larval stages displayed a rise in total free IAA/total free DAA (dispensable amino acids) ratio. The authors conclude that the highest level of FAA in HL pacu larvae is indicative of active proteolysis of yolk reserves and a probable catabolism regulation of some FAA through spare-effect. In addition, Tau is one of the major FAA occurring during pacu ontogeny and may be performing regulation on body fluid osmolality regulation. © Copyright by the World Aquaculture Society 2013.

Nanopartículas de sílica e ácido p-amino benzóico: um estudo de associação para protetores solares

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

Síntese e caracterização de amino ácidos e ésteres n-(aminoalquil)-lactâmicos derivados do paba com potencial atividade biológica

Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)

Sequence characterization of coding regions of the myostatin gene (GDF8) from Brazilian Murrah buffaloes (Bubalus bubalis) and comparison with the Bos taurus sequence

Within about 30 years the Brazilian buffalo (Bubalus bubalis) herd will reach approximately 50 million head as a result of the great adaptive capacity of these animals to tropical climates, together with the good productive and reproductive potential which make these animals an important animal protein source for poor and developing countries. The myostatin gene (GDF8) is important in the physiology of stock animals because its product produces a direct effect on muscle development and consequently also on meat production. The myostatin sequence is known in several mammalian species and shows a high degree of amino acid sequence conservation, although the presence of non-silent and silent changes in the coding sequences and several alterations in the introns and untranslated regions have been identified. The objective of our work was to characterize the myostatin coding regions of B. bubalis (Murrah breed) and to compare them with the Bos taurus regions looking for variations in nucleotide and protein sequences. In this way, we were able to identify 12 variations at DNA level and five alterations on the presumed myostatin protein sequence as compared to non double-muscled bovine sequences.

Chemical composition and fatty acid contents in farmed freshwater prawns

The objective of this work was to evaluate the chemical composition and fatty acid contents of Amazonian and giant river prawns. After four-month farming, with the same diet for both species, palmitic and stearic acids were the main saturated fatty acids. Oleic acid was the main monounsatured fatty acid, and the eicosapentaenoic and docosahexaenoic acids were the most abundant polyunsaturated acids. Amazonian prawn has higher levels of protein and polyunsaturated fatty acids than those of the giant river prawn, which shows its potential for aquaculture.

Swimming Exercise Changes Hemodynamic Responses Evoked by Blockade of Excitatory Amino Receptors in the Rostral Ventrolateral Medulla in Spontaneously Hypertensive Rats

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

Transport of amino acids from milk whey by Caco-2 cell monolayer after hydrolytic action of gastrointestinal enzymes

The bioavailability of amino adds from milk whey protein hydrolysates was evaluated using diffusion of the substances through semi-permeable membranes (dialyzability) and transport by Caco-2 cell cultures. The hydrolysates with low degree of hydrolysis (LDH) and high degree of hydrolysis (HDH) were obtained after 120 min of reaction time at 50 degrees C after the initial addition of pepsin, followed by the addition of trypsin, chymotrypsin and carboxypeptidase-A. The proteins and hydrolysates were further subjected to in vitro digestion with pepsin plus pancreatin. HPLC was used to determine the concentrations of dialyzable amino adds (48.4% of the non-hydrolyzed proteins, 63.2% of the LDH sample and 58.3% of the HDH sample), demonstrating the greater dialyzability of the hydrolysates. The LDH and HDH whey protein hydrolysates prepared with pepsin, trypsin, chymotrypsin and carboxypeptidase-A showed only 14.7% and 20.8% of dialyzable small peptides and amino acids, respectively. The efficiency of absorption was demonstrated by the preferential transport of Ile, Lou and Arg through a layer of cells. In the LDH hydrolysate, Tyr was also transported. Prior high- and low-degree hydrolysis of the whey provided transport by 5.7% and 6.6%, respectively, in comparison with 23% for non-hydrolyzed proteins, considering the total amount of these amino adds that was applied to the cells. (C) 2014 Elsevier Ltd. All rights reserved.

Nicotine-enhanced oxidation of low-density lipoprotein and its components by myeloperoxidase/H2O2/Cl- system

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

Chemical and Fatty acid composition of different cuts cooked or uncooked from yearling bulls fed oil sources

This study evaluated the chemical and lipid composition of uncooked or cooked loin (Longissimus thoracis) and rump (Biceps femoris) in samples of 2.54 cm thick from 35 carcasses of Nellore young bulls finished in feedlot for 96 days and slaughtered at an average weight of 532.17 ± 30.25 kg and 24 months of age. The rump had the lowest level of protein and ash (18.57 and 0.90%, respectively) and the highest level of ether extract compared to loin (3.37 and 1.90%, respectively). Higher levels of cholesterol were found in rump compared to loin (40.91 e 30.93 mg 100 g-1, respectively). The uncooked loin showed lower content of saturated fatty acids and higher content of polyunsaturated fatty acids. The best values for the omega-6: omega-3 ratio was observed in the uncooked beef. In the present study, the loin was healthier due to the higher amount of polyunsaturated fatty acids compared to rump. Cooking the meat decreases the levels of polyunsaturated fatty acids, omega-3, omega-6 and the omega-6: omega-3 ratio.