4.6 Article

Metabolism of Seriola lalandi during Starvation as Revealed by Fatty Acid Analysis and Compound-Specific Analysis of Stable Isotopes within Amino Acids

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PLOS ONE
卷 12, 期 1, 页码 -

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PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0170124

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资金

  1. Consejo Nacional de Ciencia y Tecnologia [CB-2014-237204]
  2. Universidad Autonoma de Baja California [18a-630]
  3. CONACYT [CB-2014-237204, 630]

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Fish starvation is defined as food deprivation for a long period of time, such that physiological processes become confined to basal metabolism. Starvation provides insights in physiological processes without interference from unknown factors in digestion and nutrient absorption occurring in fed state. Juveniles of amberjack Seriola lalandi were isotopically equilibrated to a formulated diet for 60 days. One treatment consisted of fish that continued to be fed and fish in the other treatment were not fed for 35 days. The isotopic signatures prior to the beginning of and after the starvation period, for fish in the starvation and control treatments, were analysed for lipid content, fatty acid composition and isotopic analysis of bulk (EA-IRMS) and of amino acids (compound specific isotope analysis, CSIA). There were three replicates for the starvation group. Fatty acid content in muscle and liver tissue before and after starvation was determined to calculate percent change. Results showed that crude lipid was the most used source of energy in most cases; the PUFAs and LC-PUFAs were highly conserved. According to the protein signature in bulk (delta N-15) and per amino acid (delta C-13 and delta N-15), in muscle tissue, protein synthesis did not appear to occur substantially during starvation, whereas in liver, increases in delta C-13 and delta N-15 indicate that protein turnover occurred, probably for metabolic routing to energy-yielding processes. As a result, isotopic values of delta N-15 in muscle tissue do not change, whereas CSIA net change occurred in the liver tissue. During the study period of 35 days, muscle protein was largely conserved, being neither replenished from amino acid pools in the plasma and liver nor catabolized.

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