Amino acid modulation of in vivo intestinal zinc absorption in freshwater rainbow trout

2002 ◽  
Vol 205 (1) ◽  
pp. 151-158 ◽  
Author(s):  
Chris N. Glover ◽  
Christer Hogstrand
Keyword(s):  
Amino Acids ◽  
Rainbow Trout ◽  
Amino Acid ◽  
Zinc Ion ◽  
Zinc Uptake ◽  
Intestinal Lumen ◽  
Zinc Absorption ◽  
Zinc Accumulation ◽  
Rainbow Trout Oncorhynchus Mykiss

SUMMARY The composition of the intestinal lumen is likely to have considerable influence upon the absorption, and consequently the nutrition and/or toxicity, of ingested zinc in aquatic environments, where zinc is both a nutrient and a toxicant of importance. The effects of amino acids upon intestinal zinc uptake in freshwater rainbow trout (Oncorhynchus mykiss) were studied using an in vivo perfusion technique. The presence of histidine, cysteine and taurine had distinct modifying actions upon quantitative and qualitative zinc absorption, compared to perfusion of zinc alone. Alterations in zinc transport were not correlated with changes in levels of free zinc ion. The chemical nature of the zinc–amino acid chelate, rather than the chelation itself, appeared to have the most important influence upon zinc absorption. l-histidine, despite a strong zinc-chelating effect, maintained quantitative zinc uptake at control (zinc alone) levels. This effect correlated with the formation of Zn(His)2 species. d-histidine at a luminal concentration of 100 mmol l–1 significantly enhanced subepithelial zinc accumulation, but reduced the fraction of zinc that was retained and absorbed by the fish. The possibility of a Zn(His)2-mediated pathway for intestinal uptake is discussed. l-cysteine specifically stimulated the accumulation of zinc post-intestinally, an effect attributed to enhanced zinc accumulation in the blood. Taurine increased subepithelial zinc accumulation, but decreased the passage of zinc to post-intestinal compartments. Amino acids are proposed to have important roles in modifying intestinal zinc uptake with potential implications for environmental toxicity as well as aquaculture.

In vivo characterisation of intestinal zinc uptake in freshwater rainbow trout

2002 ◽  
Vol 205 (1) ◽  
pp. 141-150 ◽  
Author(s):  
Chris N. Glover ◽  
Christer Hogstrand
Keyword(s):  
Rainbow Trout ◽  
High Capacity ◽  
Zinc Uptake ◽  
Ethylene Glycol Tetraacetic Acid ◽  
Intestinal Lumen ◽  
Zinc Absorption ◽  
Maximal Rate ◽  
Rainbow Trout Oncorhynchus Mykiss ◽  
Rate Of Accumulation

SUMMARY Knowledge of the uptake mechanisms and metabolism of metals is essential for understanding the factors governing metal toxicity, discerning means by which acclimation and homeostasis may be achieved and characterising interactions between the metal of interest and other environmental moieties. Zinc is both an important aquatic contaminant and a vital micronutrient. The physiological characterisation of dietary zinc absorption in fish has, therefore, important implications for environmental protection and aquaculture. The present study aimed to elucidate the mechanism of intestinal zinc uptake in freshwater rainbow trout (Oncorhynchus mykiss), using an in vivo cannulation technique. Only a saturable component of zinc uptake, with a concentration giving half-maximal rate of accumulation (K0.5) of 309 μmol l–1, and a maximal rate of accumulation (Jmax) of 933 nmol kg–1 h–1, was described. This characterised the intestine as a low-affinity, high-capacity zinc absorption pathway. Physiological mechanisms appear to regulate zinc uptake. Intestinal mucus was one important regulatory locus, promoting zinc uptake at low concentrations yet buffering the animal against high luminal zinc loads. Regulatory mechanisms also seemed to limit subepithelial zinc accumulation. Experiments using ethylene glycol tetraacetic acid (EGTA) to wash the intestinal lumen following zinc perfusion exhibited a higher proportion of loosely associated zinc at higher perfused concentrations. This was attributed to saturation of the uptake process or efflux from the subepithelium. Two distinct pathways for passage of zinc across the epithelium were discerned, with post-intestinal transfer possibly mediated by sulphydryl groups, as illustrated by N-ethylmaleimide perfusion experiments. Putative roles of zinc transporters and/or intracellular-binding proteins are discussed.

DETERMINATION OF PROTEIN SYNTHESIS IN RAINBOW TROUT, ONCORHYNCHUS MYKISS, USING A STABLE ISOTOPE

1994 ◽  
Vol 189 (1) ◽  
pp. 279-284
Author(s):  
C Carter ◽  
S Owen ◽  
Z He ◽  
P Watt ◽  
C Scrimgeour ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Rainbow Trout ◽  
Amino Acid ◽  
Oncorhynchus Mykiss ◽  
Considerable Proportion ◽  
Published Data ◽  
Short Term ◽  
Terrestrial Mammals ◽  
Rainbow Trout Oncorhynchus Mykiss

It has been suggested (Houlihan, 1991) that the consumption of 1 g of protein in a variety of species of fish stimulates the synthesis of, approximately, an equal amount of protein. Although synthesis of protein may account for as much as 40 % of the whole-animal oxygen consumption (Lyndon et al. 1992), only about 30 % of the synthesized proteins are retained as growth (Houlihan et al. 1988; Carter et al. 1993a,b). Thus, one focus of attention is the potential advantage gained by fish in allocating a considerable proportion of assimilated energy to protein turnover in contrast to relatively low-cost, low-turnover protein growth (Houlihan et al. 1993). Rates of protein synthesis in several species of fish have been measured using radioactively labelled amino acids, frequently given as a flooding dose (reviewed by Fauconneau, 1985; Houlihan, 1991). These measurements cannot be made for longer than a few hours because of the decline in specific radioactivity in the amino acid free pool. However, as protein synthesis rates vary during the course of a day as a result of the post-prandial stimulation, and since radiolabelled amino acid methodology is invasive, short-term and terminal, it has been difficult to be certain of the relationship between protein growth measured in the long term and protein synthesis rates measured in the short term. This paper addresses these problems by developing a method using 15N in orally administered protein to measure protein synthesis rates in fish over relatively long periods, the aim being to use procedures that are as non-invasive and repeatable as possible. The use of stable isotopes to measure protein metabolism is well established in terrestrial mammals (see Rennie et al. 1991; Wolfe, 1992), but to our knowledge the only published data for aquatic ectotherms are on the blue mussel (Mytilus edulis L.) (Hawkins, 1985). In the present study, rates of protein synthesis of individual rainbow trout [Oncorhynchus mykiss (Walbaum)] were calculated from the enrichment of excreted ammonia with 15N over the 48 h following the feeding of a single meal (dose) containing protein uniformly labelled with 15N by use of an end-point stochastic model (Waterlow et al. 1978; Wolfe, 1992). Application of this type of modelling would appear to be ideal for measuring ammonotelic fish nitrogen metabolism since, unlike the situation in mammals, the catabolic flux of amino acids through urea is very small. Further, ammonia is excreted directly into the surrounding water via the gills and is not stored for any length of time, in contrast to the situation in mammals, so the rate of tracer appearance is easily measurable.

scholarly journals In vivo Determination of Amino Acid Bioavailability in Humans and Model Animals

2005 ◽  
Vol 88 (3) ◽  
pp. 923-934 ◽  
Author(s):  
Malcolm F Fuller ◽  
Daniel Tomé
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
The Body ◽  
Whole Body ◽  
Intestinal Lumen ◽  
Stable Isotope Labelling ◽  
Ileal Digestibility ◽  
Hydrolyzed Protein ◽  
Protein Free Diet

Abstract Because the digestion of many dietary proteins is incomplete, and because there is a continuous (but variable) entry into the intestinal lumen of endogenous protein and amino acid nitrogen that is also subject to digestion, the fluxes of nitrogen, amino acids, and protein in the gut exhibit a rather complicated pattern. Methods to distinguish and quantitate the endogenous and dietary components of nitrogen and amino acids in ileal chyme or feces include the use of a protein-free diet, the enzyme-hydrolyzed protein method, different levels of protein intake, multiple regression methods, and stable-isotope labelling of endogenous or exogenous amino acids. Assessment of bioavailability can be made, with varying degrees of difficulty, in man directly but, for routine evaluation of foods, the use of model animals is attractive for several reasons, the main ones being cost and time. Various animals and birds have been proposed as models for man but, in determining their suitability as a model, their physiological, enzymological, and microbiological differences must be considered. Fecal or ileal digestibility measurements, as well as apparent and true nitrogen and amino acid digestibility measurements, have very different nutritional significance and can, thus, be used for different objectives. Measurements at the ileal level are critical for determining amino acid losses of both dietary and endogenous origin, whereas measurements at the fecal level are critical in assessing whole-body nitrogen losses. A complementary and still unresolved aspect is to take into account the recycling of intestinal nitrogen and bacterial amino acids to the body.

Amino acids in the rat intestinal lumen regulate their own absorption from a distant intestinal site

2009 ◽  
Vol 297 (2) ◽  
pp. G292-G298 ◽  
Author(s):  
Fadi H. Mourad ◽  
Kassem A. Barada ◽  
Carmen Khoury ◽  
Tamim Hamdi ◽  
Nayef E. Saadé ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Inhibitory Effect ◽  
Intestinal Lumen ◽  
Jejunal Segment ◽  
Subdiaphragmatic Vagotomy ◽  
Regulatory Loop ◽  
Dependent Transport

Intestinal nutrient transport is altered in response to changes in dietary conditions and luminal substrate level. It is not clear, however, whether an amino acid in the intestinal lumen can acutely affect its own absorption from a distant site. Our aim is to study the effect of an amino acid present in rat small intestinal segment on its own absorption from a proximal or distal site and elucidate the underlying mechanisms. The effect of instillation of alanine (Ala) in either jejunum or ileum on its own absorption at ileal or jejunal level was examined in vivo. The modulation of this intestinal regulatory loop by the following interventions was studied: tetrodotoxin (TTX) added to Ala, subdiaphragmatic vagotomy, chemical ablation of capsaicin-sensitive primary afferent (CSPA) fibers, and IV administration of calcitonin gene-related peptide (CGRP) antagonist. In addition, the kinetics of jejunal Ala absorption and the importance of Na+-dependent transport were studied in vitro after instilling Ala in the ileum. Basal jejunal Ala absorption [0.198 ± 0.018 μmol·cm−1·20 min−1 (means ± SD)] was significantly decreased with the instillation of 20 mM Ala in the ileum or in an adjacent distal jejunal segment (0.12 ± 0.015; P < 0.0001 and 0.138 ± 0.014; P < 0.002, respectively). Comparable inhibition was observed in the presence of proline in the ileum. Moreover, basal Ala absorption from the ileum (0.169 ± 0.025) was significantly decreased by the presence of 20 mM Ala in the jejunum (0.103 ± 0.027; P < 0.01). The inhibitory effect on jejunal Ala absorption was abolished by TTX, subdiaphragmatic vagotomy, neonatal capsaicin treatment, and CGRP antagonism. In vitro studies showed that Ala in the ileum affects Na+-mediated transport and increases Km without affecting Vmax. Intraluminal amino acids control their own absorption from a distant part of the intestine, by affecting the affinity of the Na+-mediated Ala transporter, through a neuronal mechanism that involves CSPA and CGRP.

Disulphide bonds and cross‐linked amino acids may affect amino acid utilization in feather meal fed to rainbow trout (Oncorhynchus mykiss)

2019 ◽  
Vol 50 (8) ◽  
pp. 2081-2095 ◽  
Author(s):  
Guillaume Pfeuti ◽  
James Longstaffe ◽  
Leonid S. Brown ◽  
Anna K. Shoveller ◽  
Carol M. Taylor ◽  
...  
Keyword(s):  
Amino Acids ◽  
Rainbow Trout ◽  
Amino Acid ◽  
Oncorhynchus Mykiss ◽  
Feather Meal ◽  
Rainbow Trout Oncorhynchus Mykiss ◽  
Disulphide Bonds ◽  
Amino Acid Utilization
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