RESUMEN
Fontes alternativas de alimentos vem sendo estudadas em substituição à farinha de peixe na aquicultura, podendo acarretar diferença na incorporação de carbono e nitrogênio decorrentes da disponibilidade e do valor nutricional da fonte. Três experimentos tiveram o objetivo de quantificar a participação das diferentes fontes protéicas nos tecidos de juvenis e pós-larvas através da composição isotópica de C e N e sua influência no crescimento. Além disso, a digestibilidade aparente das dietas contendo mistura de plantas C3 e C4 foi estudada usando o 13C nas fezes como traçador. As dietas consistiram de quatro ingredientes protéicos. Farelo de soja FS, farelo de coco FC, farinha de vísceras de aves FVA e farinha de peixe FP que compuseram cinco combinações diferentes: FS100; FS60FC40; FS60FVA40; FS60FP40; FS19F10FP10FVA11. No primeiro experimento duzentos juvenis de tilápia com peso médio de 3,4 ± 0,20 g foram distribuídos em 20 gaiolas flutuantes e após serem alimentados com as dietas experimentais, foram coletados amostras aos 0, 22, 44, 66 e 88 dias para estimar a contribuição de C e N das dietas no tecido. Foi observada diferença significativa (P0,05).
Alternative sources of food have been studied in substitution for fishmeal in aquaculture, and it may result in a difference in incorporation of carbon and nitrogen, depending on the nutritional value and availability of the source. Two experiments were designed to quantify the participation of different protein sources in the muscle tissue in juvenile and post larvae through isotopic composition and its influence on growth and body composition. In addition, the apparent digestibility of feedingstuffs containing mixture of C3 and C4 plants has been studied using 13C as tracer. The experiments were conducted in a random design with five treatments and four repetitions. Diets consisted of by four sources of protein ingredients. soybean meal SBM, coconut meal CM, poultry product meal PPM, meal and fish meal FM, composed five different combinations of diets: SBM100 SBM60CM40 SBM60PPM40 SBM60FM40 SBM19CM10FM10PPM11. In the first experiment, it used 200 juveniles with an average weight of 3.4 ± 0.20 g, distributed in 20 vinyl cages. Fish collections were held after being fed the experimental diets for 0, 22, 28, 38, 44, 66 and 88 days. In this assay, it was observed significant difference (P<0.05) for final weight, weight gain, feed conversion, fillet yield, protein efficiency ratio and condition factorHowever, there was no difference between food consumption, weight and content of the fillet profile. For the experiment two, 300 post-larvae, 20 days old and with average weight starting at 0.07 ± 0.020g, were randomly distributed in the five treatments, making each experimental unit with twenty animals. Six fish collections were held at 0, 6, 12, 18, 24 and 30 days. This assay also showed significant difference (P<0.05) for final weight, weight gain, food intake, feed conversion and protein efficiency ratio.
Asunto(s)
Animales , Cíclidos/anatomía & histología , Cíclidos/metabolismo , Fenómenos Fisiológicos Nutricionales de los Animales/fisiología , Células Musculares/químicaRESUMEN
La sarcopenia, pérdida de masa y fuerza del músculo esqueléico, es una condición frecuente durante el envejecimiento. Conduce a incapacidad motora resultando en internación y mortalidad. Puesto que los niveles de estrógenos y/o testosterona disminuyen con la edad, la sarcopenia se ha asociado al déficit de estas hormonas. Aunque los mecanismos moleculares involucrados en esta patología no están totalmente dilucidados, existen evidencias indicando que la apoptosis es en parte responsable de la pérdida de miocitos en la adultez. Previamente demostramos que el 17ß-estradiol (E2) inhibe la apoptosis en la línea celular C2C12 de músculo esquelético a través de PI3K/Akt, MAPKs, HSP27 y receptores estrogénicos (ERs) con localización no clásica. Usando siRNAs específicos para silenciar las isoformas del ER, comprobamos que el E2 activa ERK involucrando a ERa, mientras que la activación de p38 MAPK es independiente de ERs. Confirmamos que el E2 puede inhibir la apoptosis a través de las MAPKs en cultivos primarios de músculo esquelético de ratón. Al igual que la E2, la testosterona bloquea la apoptosis. Las alteraciones morfológicas típicas de la apoptosis como fragmentación nuclear, desorganización del citoesqueleto, reorganización/disfunción mitocondrial y liberación de citocromo c, inducidos por H2O2 fueron suprimidas al preincubar las células con testosterona. Se requieren investigaciones adicionales para establecer un paralelismo entre los mecanismos de acción de ambas hormonas, que podrían estar implicados en patologías musculares asociadas a apoptosis. Los datos presentados en este estudio profundizan el conocimiento de las bases moleculares de la sarcopenia relacionada con estados de déficit de hormonas sexuales.
Asunto(s)
Humanos , Masculino , Femenino , Apoptosis , Factor Inductor de la Apoptosis , Células Musculares/química , Estradiol/metabolismo , Músculo Esquelético/anomalías , Músculo Esquelético/crecimiento & desarrollo , Testosterona/metabolismo , Debilidad MuscularRESUMEN
The muscle-specific intermediate filament protein desmin is expressed in mononucleated myoblasts and in differentiated myotubes. Desmin has been shown to associate with the sarcolemma in specific structures, such as neuromuscular junctions and the dystrophin-associated protein complex. Since these are specialized membrane regions, the study of a possible association between desmin and liquid-ordered membrane microdomains is of particular interest. We have carried out an analysis of the association between desmin and the muscle-specific protein caveolin-3, a major component of caveolar microdomains. Our results demonstrate that (1) desmin precisely co-localizes with caveolin-3 in myoblasts and multinucleated myotubes, (2) caveolin-3 is up-regulated during in vitro chick muscle development, (3) desmin is detectable in caveolae-enriched membrane fractions prepared from skeletal muscle, and (4) caveolin-3 co-immunoprecipitates with desmin. We have thus shown, for the first time, an association between the intermediate filament protein desmin and caveolin-3 in myogenic cells.