RESUMO
This study investigates the structure of factors that influence consumer intentions to both try and to consume cultured proteins, and their intentions to substitute vegan, vegetarian and omnivore diets with these alternative protein sources. Comprehensive survey data (N = 3862) was collected from three Nordic countries (Denmark, Finland, and Norway) and analysed using confirmatory factor analysis and structural equation modelling. Theoretically, this article draws from behavioural models of environmental psychology, identity theory, and attitude theory. Results indicate that beliefs about the necessity of an industry producing cultured proteins and impacts of cultured proteins on the global economy are significant predictors of consumer intentions. Moreover, participants who exhibited high levels of general and food innovativeness were more likely to express positive intentions to consume cultured proteins. Social norms influenced consumer intentions: Individuals surrounded by positive attitudes and intentions toward cultured proteins within their social networks were more inclined to want to consume these products. The predictor variables in the final model accounted for between 39% and 66% of the variance in the different cultured proteins related intentions. Understanding consumer intentions better can inform targeted communication strategies aimed at promoting the advantages of cultured proteins and facilitating its adoption.
Assuntos
Comportamento do Consumidor , Intenção , Carne , Humanos , Masculino , Feminino , Adulto , Pessoa de Meia-Idade , Adulto Jovem , Preferências Alimentares/psicologia , Laticínios , Animais , Inquéritos e Questionários , Finlândia , Adolescente , Dieta Vegetariana/psicologia , Peixes , Idoso , Normas Sociais , Proteínas Alimentares , Alimentos Marinhos , Noruega , Conhecimentos, Atitudes e Prática em Saúde , Dieta/psicologia , Carne in vitroRESUMO
Genetic polymorphisms of bovine milk proteins affect the protein profile of the milk and, hence, certain technological properties, such as casein (CN) number and cheese yield. However, reports show that such polymorphisms may also affect the health-related properties of milk. Therefore, to gain insight into their digestion pattern and bioactive potential, ß-CN was purified from bovine milk originating from cows homozygous for the variants A(1), A(2), B, and I by a combination of cold storage, ultracentrifugation, and acid precipitation. The purity of the isolated ß-CN was determined by HPLC, variants were verified by mass spectrometry, and molar extinction coefficients at λ=280nm were determined. ß-Casein from each of the variants was subjected to in vitro digestion using pepsin and pancreatic enzymes. Antioxidant and angiotensin-converting enzyme (ACE) inhibitory capacities of the hydrolysates were assessed at 3 stages of digestion and related to that of the undigested samples. Neither molar extinction coefficients nor overall digestibility varied significantly between these 4 variants; however, clear differences in digestion pattern were indicated by gel electrophoresis. In particular, after 60min of pepsin followed by 5min of pancreatic enzyme digestion, one ≈4kDa peptide with the N-terminal sequence (106)H-K-E-M-P-F-P-K- was absent from ß-CN variant B. This is likely a result of the (122)Ser to (122)Arg substitution in variant B introducing a novel trypsin cleavage site, leading to the changed digestion pattern. All investigated ß-CN variants exhibited a significant increase in antioxidant capacity upon digestion, as measured by the Trolox-equivalent antioxidant capacity assay. After 60min of pepsin + 120min of pancreatic enzyme digestion, the accumulated increase in antioxidant capacity was ≈1.7-fold for the 4 ß-CN variants. The ACE inhibitory capacity was also significantly increased by digestion, with the B variant reaching the highest inhibitory capacity at the end of digestion (60min of pepsin + 120min of pancreatic enzymes), possibly because of the observed alternative digestion pattern. These results demonstrate that genetic polymorphisms affect the digestion pattern and bioactivity of milk proteins. Moreover, their capacity for radical scavenging and ACE inhibition is affected by digestion.
Assuntos
Inibidores da Enzima Conversora de Angiotensina/farmacologia , Antioxidantes/farmacologia , Caseínas/metabolismo , Caseínas/farmacologia , Digestão , Polimorfismo Genético , Sequência de Aminoácidos , Aminoácidos/análise , Animais , Caseínas/genética , Bovinos , Queijo/análise , Cromatografia Líquida de Alta Pressão , Feminino , Técnicas In Vitro , Leite/química , Proteínas do Leite/análise , Pepsina A/metabolismo , Peptídeos/química , Peptídeos/metabolismo , Peptidil Dipeptidase A , Relação Estrutura-Atividade , Tripsina/metabolismoRESUMO
AIMS: Caffeic acid, naringenin and quercetin are naturally occurring phenolic compounds (PCs) present in many plants as secondary metabolites. The aim of this study was to investigate their effect on glucose-stimulated insulin secretion (GSIS) in INS-1E cells and to explore their effect on expression of genes involved in ß-cell survival and function under normoglycaemic and glucotoxic conditions. METHODS: For acute studies, INS-1E cells were grown in 11 mM glucose (72 h) and then incubated with the PCs (1 h) with 3.3/16.7 mM glucose; whereas, for chronic studies, the cells were grown in 11 mM glucose (72 h) with/without the PCs, and then incubated with 3.3/16.7 mM glucose (1 h); thereafter, GSIS was measured. For GSIS and gene expression studies (GES) under glucotoxic conditions, two sets of cells were grown in 11/25 mM glucose with/without the PCs (72 h): one was used for GES, using real time RT-PCR, and the other was exposed to 3.3/16.7 mM glucose, followed by measurement of GSIS. RESULTS: The study demonstrated that the PCs can enhance GSIS under hyperglycaemic and glucotoxic conditions in INS-1E cells. Moreover, these compounds can differentially, yet distinctly change the expression profile of genes [Glut2 (glucose transporter 2), Gck (glucokinase), Ins1 (insulin 1), Ins2, Beta2 (neurogenic differentiation protein 1), Pdx1 (pancreatic and duodenal homeobox protein 1), Akt1 (RAC-α serine/threonine-protein kinase encoding gene), Akt2 (RAC-ß serine/threonine-protein kinase encoding gene), Irs1 (insulin receptor substrate 1), Acc1 (acetyl CoA carboxylase 1), Bcl2 (ß-cell lymphoma 2 protein), Bax (Bcl-2 associated X protein), Casp3 (Caspase 3), Hsp70 (heat shock protein 70), and Hsp90] involved in ß-cell stress, survival and function. CONCLUSION: The results indicate that the PCs tested enhance GSIS and glucose sensitivity in INS-1E cells. They also modulate gene expression profiles to improve ß-cell survival and function during glucotoxicity.
Assuntos
Ácidos Cafeicos/farmacologia , Flavanonas/farmacologia , Células Secretoras de Insulina/efeitos dos fármacos , Insulina/metabolismo , Preparações de Plantas/farmacologia , Quercetina/farmacologia , Animais , Transporte Biológico , Linhagem Celular , Sobrevivência Celular , Expressão Gênica/efeitos dos fármacos , Glucoquinase/metabolismo , Glucose/metabolismo , Secreção de Insulina , Células Secretoras de Insulina/metabolismo , Fitoterapia , RNA Mensageiro/metabolismo , Ratos , Via Secretória/efeitos dos fármacos , Transdução de Sinais/efeitos dos fármacosRESUMO
The aim of this study was to validate previously reported associations between microarray gene expression levels and pork quality traits using real-time PCR. Meat samples and meat quality data from 100 pigs were collected from a different pig breed to the one tested by microarray (Large White versus Pietrain) and a different country of origin (Denmark versus Germany). Ten genes (CARP, MB, CSRP3, TNNC1, VAPB, TNNI1, HSPB1, TNNT1, TIMP-1, RAD-like) were chosen from the original microarray study on the basis of the association between gene expression levels and the meat quality traits meat %, back fat, pH24, drip loss %, colour a*, colour b*, colour L*, WB-SF, SFA, MUFA, PUFA. Real-time PCR detection methods were developed for validation of all ten genes, confirming association with drip loss (two of two genes), ultimate pH (three of four genes), a* (redness) (two of six genes) and L*(lightness) (two of four genes). Furthermore, several new correlations for MUFA and PUFA were established due to additional meat quality trait information on fatty acid composition not available for the microarray study. Regression studies showed that the maximum explanation of the phenotypic variance of the meat quality traits was 50% for the ultimate pH trait using these ten genes only. Additional studies showed that the gene expression of several of the genes was correlated with each other. We conclude that the genes initially selected from the microarray study were robust, explaining variances of the genes for the meat quality traits.
Assuntos
Biomarcadores/metabolismo , Cruzamento/métodos , Regulação da Expressão Gênica/genética , Genes/genética , Carne/normas , Fenótipo , Sus scrofa/fisiologia , Animais , Primers do DNA/genética , Dinamarca , Ácidos Graxos Insaturados/metabolismo , Alemanha , Concentração de Íons de Hidrogênio , Análise em Microsséries , Reação em Cadeia da Polimerase em Tempo Real/veterinária , Análise de Regressão , Especificidade da Espécie , Sus scrofa/genéticaRESUMO
We have tested the ability of the c13 protein, which is a hybrid protein of the first 81 amino acids of the viral nonstructural protein (NS1) and the HA2 subunit of viral hemagglutination produced in E. coli, to render target cells susceptible to the lytic activity of influenza virus-specific cytotoxic T lymphocytes (CTL). The results showed that P815 cells coated with c13 protein were lysed by PR8 virus-induced secondary CTL derived from BALB/c mice. Cold-target inhibition tests clearly demonstrated that c13 protein-coated P815 cells were recognized by an H1 subtype-specific CTL population. Furthermore, PR8 virus-induced CTL derived from C3H mice did not lyse c13 protein-coated P815 cells, suggesting that c13 protein was recognized by CTL in conjunction with H-2d products. These findings suggest that this protein interacts with the cellular plasma membrane and makes target cells recognizable by H-2-restricted, influenza virus subtype-specific CTL.
Assuntos
Proteínas de Bactérias/genética , Escherichia coli/imunologia , Vírus da Influenza A/imunologia , Linfócitos T Citotóxicos/imunologia , Animais , Proteínas de Bactérias/imunologia , Citotoxicidade Imunológica , Escherichia coli/genética , Camundongos , Camundongos Endogâmicos , Plasmídeos , Especificidade da EspécieRESUMO
We have examined whether active immunization with c13 protein, a hybrid protein of the first 81 amino acids of the viral NS1 nonstructural protein and the HA2 subunit of A/PR/8 (H1N1) hemagglutinin, could protect BALB/c mice from challenge with A/PR/8 H1 subtype virus. Mice immunized with the c13 protein had a significant reduction of pulmonary virus titers with A/PR/8 (H1) virus, but failed to limit the replication of A/PC (H3) virus, which reflects the in vitro CTL activity of c13 immune spleen cells. We observed that the epitope recognized by HA2 specific CTL, which are induced by a derivative of c13 protein, is highly conserved among H1 and H2 subtype virus strains. This led us to test whether active immunization with c13 protein would also limit pulmonary virus replication in mice infected with the A/TW virus, a virus of the H1 subtype, which was isolated in 1986, and with a virus of the H2 subtype, A/Japan/305/57. Immunized mice had significantly lower lung virus titers than did control mice, and did not possess any neutralizing antibodies to the challenger viruses. These results indicate that active immunization with a fusion protein containing the cross-reactive CTL epitope protects mice from influenza infection by inducing CTL against influenza A H1 and H2 subtype virus strains, which markedly vary in their antibody binding sites on the HA1. The ability to induce active cross-reactive immunization with a fusion protein which contains a highly conserved CTL epitope offers a model for vaccine approaches against viruses which undergo significant variations in their antibody binding sites.
Assuntos
Hemaglutininas Virais/imunologia , Vírus da Influenza A/imunologia , Proteínas Recombinantes de Fusão/imunologia , Proteínas Recombinantes/imunologia , Linfócitos T Citotóxicos/imunologia , Animais , Capsídeo/imunologia , Reações Cruzadas , Epitopos , Imunidade Celular , Imunização Passiva , Pulmão/microbiologia , Camundongos , Proteínas do Core Viral/imunologia , Proteínas não Estruturais ViraisRESUMO
We have tested the abilities of various polypeptides of A/PR/8/34 (H1N1) virus, constructed by recombinant DNA techniques, to induce influenza virus-specific secondary cytotoxic T lymphocyte (CTL) responses. A hybrid protein (c13 protein), consisting of the first 81 amino acids of viral nonstructural protein (NS1) and the HA2 subunit of viral hemagglutinin (HA), induced H-2-restricted, influenza virus subtype-specific secondary CTL in vitro, although other peptides did not. Using a recombinant virus, the viral determinant responsible for recognition was mapped to the HA2 portion of c13 protein. Immunization of mice with c13 protein induced the generation of memory CTL in vivo. The CTL precursor frequencies of A/PR/8/34 virus- and c13 protein-immune mice were estimated as one in 8,047 and 50,312, respectively. These results indicate that c13 protein primed recipient mice, even though the level of precursor frequency was below that observed in virus-immune mice.
Assuntos
Capsídeo/imunologia , Hemaglutininas Virais/imunologia , Vírus da Influenza A/imunologia , Linfócitos T Citotóxicos/imunologia , Proteínas Virais/imunologia , Animais , Antígenos Virais/genética , Antígenos Virais/imunologia , Capsídeo/genética , Clonagem Molecular , Citotoxicidade Imunológica , Escherichia coli/genética , Glicoproteínas de Hemaglutininação de Vírus da Influenza , Hemaglutininas Virais/genética , Imunização , Memória Imunológica , Técnicas In Vitro , Camundongos , Camundongos Endogâmicos BALB C , Proteínas não Estruturais Virais , Proteínas Virais/genéticaRESUMO
The current vaccine against tuberculosis, Mycobacterium bovis strain bacille Calmette-Guerin (BCG), offers potential advantages as a live, innately immunogenic vaccine vehicle for the expression and delivery of protective recombinant antigens (Stover, C.K., V.F. de la Cruz, T.R. Fuerst, J.E. Burlein, L.A. Benson, L.T. Bennett, G.P. Bansal, J.F. Young, M.H. Lee, G.F. Hatfull et al. 1991. Nature [Lond]. 351:456; Jacobs, W.R., Jr., S.B. Snapper, L. Lugosi and B.R. Bloom. 1990. Curr. Top. Microbiol. Immunol. 155:153; Jacobs, W.R., M. Tuckman, and B.R. Bloom. 1987. Nature [Lond.]. 327:532); but as an attenuated intracellular bacterium residing in macrophages, BCG would seem to be best suited for eliciting cellular responses and not humoral responses. Since bacterial lipoproteins are often among the most immunogenic of bacterial antigens, we tested whether BCG expression of a target antigen as a membrane-associated lipoprotein could enhance the potential for a recombinant BCG vaccine to elicit high-titered protective antibody responses to target antigens. Immunization of mice with recombinant BCG vaccines expressing the outer surface protein A (OspA) antigen of Borrelia burgdorferi as a membrane-associated lipoprotein resulted in protective antibody responses that were 100-1,000-fold higher than responses elicited by immunization with recombinant BCG expressing OspA cytoplasmically or as a secreted fusion protein. Furthermore, these improved antibody responses were observed in heterogeneous mouse strains that vary in their immune responsiveness to OspA and sensitivity to BCG growth. Thus, expression of protective antigens as chimeric membrane-associated lipoproteins on recombinant BCG may result in the generation of new candidate vaccines against Lyme borreliosis and other human or veterinary diseases where humoral immunity is the protective response.
Assuntos
Antígenos de Superfície/imunologia , Vacina BCG/imunologia , Proteínas da Membrana Bacteriana Externa/imunologia , Vacinas Bacterianas/imunologia , Grupo Borrelia Burgdorferi/imunologia , Lipoproteínas/imunologia , Animais , Feminino , Doença de Lyme/prevenção & controle , Camundongos , Camundongos Endogâmicos BALB C , Camundongos Endogâmicos C3H , Proteínas Recombinantes de Fusão/análise , Vacinação , Vacinas Sintéticas/imunologiaRESUMO
Influenza is caused by highly variable RNA viruses belonging to the orthomyxovirus group. These viruses are capable of constantly changing the genes coding for their surface proteins as well as for their nonsurface proteins. The mechanisms responsible for these changes in type A influenza viruses include recombination (reassortment) of genes among strains, deletions and insertions in genes, and, frequently, point mutations. In addition, old strains may reappear in the population. Influenza viruses of types B and C appear to vary to a lesser degree. The mechanisms responsible for changes in these viruses are not well characterized.
Assuntos
Orthomyxoviridae/genética , Variação Genética , Hemaglutininas Virais/genética , Mutação , Neuraminidase/genética , Proteínas Virais/genéticaRESUMO
Transfer RNA (tRNA) suppression of nonsense mutations in prokaryotic systems has been widely used to study the structure and function of different prokaryotic genes. Through genetic engineering techniques, it is now possible to introduce suppressor (Su+) tRNA molecules into mammalian cells. A quantitative assay of the suppressor tRNA activity in these mammalian cells is described; it is based on the amount of tRNA-mediated readthrough of a terminating codon in the influenza virus NS1 gene after the cells are infected with virus. Suppressor activity in L cells continuously expressing Su+ (tRNAtyr) was 3.5 percent and that in CV-1 cells infected with an SV40- Su+ (tRNAtyr) recombinant was 22.5 percent.
Assuntos
RNA de Transferência/genética , Supressão Genética , Animais , Células Cultivadas , Células Eucarióticas/fisiologia , Genes Virais , Camundongos , Orthomyxoviridae/genética , Terminação Traducional da Cadeia Peptídica , Biossíntese de Proteínas , Vírus 40 dos Símios/genéticaRESUMO
The circumsporozoite (CS) protein of the human malaria parasite Plasmodium falciparum may be the most promising target for the development of a malaria vaccine. In this study, proteins composed of 16, 32, or 48 tandem copies of a tetrapeptide repeating sequence found in the CS protein were efficiently expressed in the bacterium Escherichia coli. When injected into mice, these recombinant products resulted in the production of high titers of antibodies that reacted with the authentic CS protein on live sporozoites and blocked sporozoite invasion of human hepatoma cells in vitro. These CS protein derivatives are therefore candidates for a human malaria vaccine.
Assuntos
Formação de Anticorpos , Antígenos de Superfície/imunologia , Malária/prevenção & controle , Plasmodium falciparum/imunologia , Proteínas de Protozoários , Vacinas/imunologia , Animais , Antígenos de Superfície/genética , Carcinoma Hepatocelular , Linhagem Celular , Clonagem Molecular , Reações Cruzadas , DNA Recombinante , Escherichia coli/genética , Humanos , Neoplasias Hepáticas , Camundongos , Plasmodium/imunologia , Plasmodium falciparum/genética , Plasmodium falciparum/fisiologiaRESUMO
Immunization with radiation-attenuated malaria sporozoites induces potent cellular immune responses, but the target antigens are unknown and have not previously been elicited by subunit vaccines prepared from the circumsporozoite (CS) protein. A method is described here for inducing protective cell-mediated immunity to sporozoites by immunization with attenuated Salmonella typhimurium transformed with the Plasmodium berghei CS gene. These transformants constitutively express CS antigens and, when used to immunize mice orally, colonize the liver, induce antigen-specific cell-mediated immunity, and protect mice against sporozoite challenge in the absence of antisporozoite antibodies. These data indicate that the CS protein contains T cell epitopes capable of inducing protective cell-mediated immunity, and emphasize the importance of proper antigen presentation in generating this response. Analogous, orally administered vaccines against human malaria might be feasible.
Assuntos
Antígenos de Superfície/imunologia , Vacinas Bacterianas/imunologia , Malária/imunologia , Plasmodium berghei/imunologia , Proteínas de Protozoários , Salmonella typhimurium/imunologia , Animais , Feminino , Fígado/microbiologia , Malária/prevenção & controle , Camundongos , Camundongos Endogâmicos BALB C , Plasmídeos , Salmonella typhimurium/genéticaRESUMO
One factor affecting meat quality is pre-slaughter stress. We investigated the effects of exercise stress on drip loss and toughness in relation to resting times of 0, 1 or 3h following exercise on a treadmill. This exercise stress was regarded as combined physical and physiological stress. Exercise stress increased the muscle temperature, reduced the creatine phosphate, ATP and glycogen content of pigs slaughtered immediately after stress exposure. These conditions lead to a reduced pH early post mortem and an increased drip loss, while only 1h of rest after exercise stress normalised these effects. However, an overshooting effect was noted when pigs were rested for 1-3h before slaughter, emphasising the importance of critical control of the resting period when studying exercise stress-induced effects on meat quality. Furthermore, meat from exercise stressed pigs, irrespective of resting, had increased toughness compared to controls, indicating that the toughness was not related to drip loss in meat from exercise stressed pigs.
RESUMO
Many longitudinal studies have investigated whether self-esteem predicts depressive symptoms (vulnerability model) or the other way around (scar model) in adolescents. The most common method of analysis has been the Cross-lagged Panel Model (CLPM). The CLPM does not separate between-person effects from within-person effects, making it unclear whether the results from previous studies actually reflect the within-person effects, or whether they reflect differences between people. We investigated the associations between self-esteem and depressive symptoms at the within-person level, using Random Intercept Cross-Lagged Panel Models (RI-CLPM). To get an impression of the magnitude of possible differences between the RI-CLPM and CLPM, we compared the results of both models. We used data from three longitudinal adolescent samples (age range 7-18; Study 1: N=1,948; Study 2: N=1,455; Study 3: N=316). Intervals between the measurements were 1-1.5 years. Single-paper meta-analyses showed support for small within-person associations from self-esteem to depressive symptoms, but not the other way around, thus only providing some support for the vulnerability model. The cross-lagged associations in the aggregated RI-CLPM and CLPM showed similar effect sizes. Overall, our results show that over 1-1.5 year time intervals, low self-esteem may negatively influence depressive symptoms over time within adolescents, but only weakly so.
RESUMO
Creatine content in the muscle may delay postmortem lactate formation and postpone the pH decline, hence potentially improving the water-holding capacity (WHC) as shown in a previous study including purebred Duroc pigs, although the same study did not find any effect on meat from purebred Landrace pigs. In the present study Danish D(LY) crossbreeds were supplemented with 0 or 50g creatine monohydrate (CMH)/d for five days prior to the slaughter. CMH supplementation had no effect on meat quality indicators (pH and temperature), meat quality attributes (WHC and colour) or eating quality (juiciness and tenderness) of meat from the D(LY) crossbred pigs. As a consequence the D(LY) crossbreed was classified as a non-responder to CMH supplementation.
RESUMO
Duroc and Landrace pigs as well as primary myotubes from these breeds were used to investigate mechanisms behind differences in their response to creatine monohydrate (CMH). Pigs were supplemented with 0, 12.5, 25 or 50g CMH/d for 5 days (n=10 per treatment and breed). Plasma levels of creatine increased dose-dependently in both breeds, while muscle-creatine phosphate content increased only in the Duroc pigs. (1)H NMR metabolic profiling showed a tendency towards clustering according to CMH supplementation only among Duroc pigs, revealing a stronger response compared to Landrace pigs. The abundance of insulin-like growth factor I and myostatin mRNA was decreased by CMH supplementation while that of type 1 IGF-receptor and creatine transporter was unaffected. Protein synthesis, increased in the myotubes from both breeds, indicating protein accretion, but no effect was observed on the mRNA abundance of IGF-I, type 1 IGF-receptor, myostatin or the creatine transporter in myotubes.
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Lameness and impaired walking ability in rapidly growing meat-type broiler chickens are major welfare issues that cause economic losses. This study analyzed the prevalence of impaired walking and its associations with production data, abattoir registrations, and postmortem tibia measurements in Norwegian broiler chickens. Gait score (GS) was used to assess walking ability in 59 different commercial broiler flocks (Ross 308) close to the slaughter d, 5,900 broilers in total, in 3 different geographical regions. In each flock, 100 arbitrary broilers were gait scored and 10 random broilers were culled to harvest tibias. Abattoir registrations on flock level were collected after slaughter. A total of 24.6% of the broilers had moderate to severe gait impairment. The broilers were sampled in 2 stages, first slaughterhouse/region, and then owner/flock. The final models showed that impaired gait is associated with first-week mortality (P < 0.05), region (P < 0.001), height of tibias mid-shaft (P < 0.05), and calcium content in the tibia ash (P < 0.05), and negatively associated with DOA (P < 0.05). The prevalence of impaired gait indicates that this is a common problem in the broiler industry in Norway, although the mean slaughter age is only 31 d and the maximum allowed animal density is relatively low. Impaired walking ability could not be predicted by the welfare indicators footpad lesion score, total on-farm mortality, and decreasing DOA prevalence. Further studies are needed to explore the relationship between first-week mortality and gait score.
Assuntos
Matadouros/estatística & dados numéricos , Galinhas , Marcha , Doenças das Aves Domésticas/epidemiologia , Tíbia/anatomia & histologia , Criação de Animais Domésticos/estatística & dados numéricos , Bem-Estar do Animal/estatística & dados numéricos , Animais , Densidade Óssea , Cálcio/análise , Estudos Transversais , Mortalidade , Noruega/epidemiologia , Tíbia/química , CaminhadaRESUMO
The energy status of the chicken at slaughter has a large impact on the development of pH postmortem and thus on color and water-holding capacity (WHC). Supplementation of creatine monohydrate and glucose (CMH+GLU) may increase the creatine content in the muscles before slaughter, thereby delaying the formation of lactic acid and postponing the pH decline. The objective of this study was to examine the impact of supplementing CMH+GLU in the drinking water within the last 48 h before slaughter on the pH decline, meat color, and WHC in the pectoralis major from 2 strains of Ross chickens. Forty Ross 308 (fast-growing) female chickens and 40 Ross 1972 (slow-growing) female chickens had free access to drinking water either supplemented with CMH (15 g/ L) and glucose (50 g/L) within the last 48 h before slaughter or without supplementation. All chickens were slaughtered at 42 or 43 d of age irrespective of weight. Temperature and pH were measured at 1 and 30 min and at 1, 3, 8, and 24 h postmortem. Also, WHC measured as drip loss and color were determined postmortem. The CMH+GLU supplementation decreased pH (P < 0.05) at all time points between 1 min and 8 h postmortem in both strains, whereas at 24 h postmortem only pH in Ross 308 chickens were decreased significantly upon supplementation. Lightness was significantly increased in the meat from Ross 308 but not from Ross 1972 chickens upon supplementation. This interaction was significant (P < 0.05). The redness of the meat was decreased upon supplementation (P < 0.05), although only significantly in Ross 1972. The pH was lower for Ross 1972 chickens at the early time points (P < 0.01) and also a higher drip loss (P < 0.05), lightness (P < 0.01), and redness (P < 0.001) were observed. Thus, there seems to be no beneficial effect of CMH+GLU supplementation on chicken meat quality on the basis of results from this experiment.
Assuntos
Galinhas/crescimento & desenvolvimento , Creatina/análogos & derivados , Creatina/administração & dosagem , Suplementos Nutricionais , Glucose/administração & dosagem , Músculo Esquelético/química , Mudanças Depois da Morte , Animais , Peso Corporal , Cor , Creatina/análise , Ingestão de Líquidos , Ingestão de Alimentos , Feminino , Tecnologia de Alimentos , Concentração de Íons de Hidrogênio , Temperatura , Água/análiseRESUMO
The human urinary bladder carcinogen, 4-aminobiphenyl (ABP), is known to undergo hepatic metabolism to an N-hydroxy arylamine and its corresponding N-glucuronide. It has been proposed that these metabolites are both transported through the blood via renal filtration to the urinary bladder lumen where acidic pH can facilitate the hydrolysis of the N-glucuronide and enhance the conversion of N-hydroxy-4-aminobiphenyl (N-OH-ABP) to a reactive electrophile that will form covalent adducts with urothelial DNA. Blood ABP-hemoglobin adducts, which have been used to monitor human exposure to ABP, are believed to be formed by reactions within the erythrocyte involving N-OH-ABP that has entered the circulation from the liver or from reabsorption across the urothelium. To test these hypotheses directly, experimental data were obtained from female beagles given [3H]ABP (p.o., i.v., or intraurethrally). [3H]N-OH-ABP (i.v. or intraurethrally), or [3H]N-OH-ABP N-glucuronide (i.v.). Analyses included determinations of total ABP in whole blood and plasma, ABP-hemoglobin adducts in blood erythrocytes, ABP and N-OH-ABP levels (free and N-glucuronide) in urine, urine pH, frequency of urination (controlled by urethral catheter), rates of reabsorption of ABP and N-OH-ABP across the urothelium, and apparent volumes of distribution in the blood/tissue compartment. The major ABP-DNA adduct, N-(guan-8-yl)-4-aminobiphenyl, was also measured in urothelial and liver DNA using a sensitive immunochemical method. An analog/digital hybrid computer was then utilized to construct a multicompartmental pharmacokinetic model for ABP and its metabolites that separates: (a) absorption; (b) hepatic metabolism and distribution in blood and tissues; (c) ABP-hemoglobin adduct formation; (d) hydrolysis and reabsorption in the urinary bladder lumen; and (e) excretion. Using this model, cumulative exposure of the urothelium to free N-OH-ABP was simulated from the experimental data and used to predict ABP-DNA adduct formation in the urothelium. The results indicated that exposure to N-OH-ABP and subsequent ABP-DNA adduct formation are directly dependent on voiding frequency and to a lesser extent on urine pH. This was primarily due to the finding that, after p.o. dosing of ABP to dogs, the major portion of the total N-OH-ABP entering the bladder lumen was free N-OH-ABP (0.7% of the dose), with much lower amounts as the acid-labile N-glucuronide (0.3% of the dose).(ABSTRACT TRUNCATED AT 400 WORDS)
Assuntos
Compostos de Aminobifenil/metabolismo , Carcinógenos/metabolismo , DNA/metabolismo , Hemoglobinas/metabolismo , Fígado/metabolismo , Bexiga Urinária/metabolismo , Micção , Compostos de Aminobifenil/sangue , Compostos de Aminobifenil/farmacocinética , Compostos de Aminobifenil/urina , Animais , Cães , Feminino , Cinética , Modelos Biológicos , Fatores de Tempo , Distribuição TecidualRESUMO
Increased creatine content in the muscle may delay post mortem lactate formation and postpone the pH decline, hence potentially improving the water-holding capacity (WHC). Duroc and Landrace pigs were supplemented with 0, 12.5, 25 or 50g creatine monohydrate (CMH)/d for 5 days prior to slaughter. Meat from Longissimus dorsi (LD) of Duroc pigs had a higher WHC and pH at all times, lower colour determinants; a* (redness), b* (yellowness), L* (lightness) and was more juicy compared to that of Landrace pigs. Furthermore, higher pH(2h), pH(24h) and decreased colour determinants were observed in carcass sides exposed to a faster cooling profile. Dietary supplementation with CMH increased the body weight gain of both breeds. However, only meat from Duroc pigs had higher pH(30min) and pH(45min) (at 50g CMH/d) and WHC, but reduced redness (reduced in both breeds) and juiciness when supplemented with CMH compared to non-supplemented controls.