Liver uptake of amino acids and carbohydrates during a single circulatory passage

1975 ◽  
Vol 228 (4) ◽  
pp. 1155-1161 ◽  
Author(s):  
WM Pardridge ◽  
LS Jefferson
Keyword(s):  
Amino Acids ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Amino Acid Uptake ◽  
Ringer Solution ◽  
Transport Systems ◽  
Test Substance ◽  
Acid Uptake ◽  
Liver Uptake ◽  
Rapid Injection

The uptake of 14C-labeled amino acids and carbohydrates by liver following rapid injection into the portal vein was measured relative to a simultaneously injected highly diffusible reference, tritium-labeled water, (3HOH). A 0.25-ml bolus of buffered Ringer solution containing 1-2 muCi of the 14C-labeled test substance and 3-6 muCi of 3HOH was administered by rabid portal injection in anesthetized rats. Circulation was terminated after a single passage of the bolus through the hepatic microvasculature and the tissue was immediately macerated, solubilized, and subjected to liquid scintillation counting. Liver uptake indices (LUI) were calculated from the ratio of 14C to 3H in liver tissue relative to the same ratio in the injection mixture. LUI's of five carbohydrates were measured: sucrose (24.3 percent), inulin (27.7 percent), D-mannitol (80.2 percent), D-glucose (96.8 percent) and L-glucose (26.7 percent). The LUI for cholic acid was 127.1 percent. Among 18 amino acids tested, the LUI's were the highest for the acidic ones (L-aspartic acid, 100.0 percent and L-glutamic acid, 86.4 percent) and lowest for the basic ones (L-arginine, 37.4 percent and L-lysine, 31.4 percent). Stereospecificity for glucose and alanine uptake, saturation kinetics for glutamic acid (Km equal to 4.8 mM) and aspartic acid (Km equal to 2.7 mM), and cross-inhibition among uptake of the acidic amino acids were observed. These findings confirmed the applicability of a technique which was originally developed for studies of amino acid uptake in brain to characterization of transport systems in liver.

The uptake of amino acids by mouse cells (strain LS) during growth in batch culture and chemostat culture: the influence of cell growth rate

1967 ◽  
Vol 168 (1013) ◽  
pp. 421-438 ◽  
Keyword(s):  
Amino Acids ◽  
Growth Rate ◽  
Amino Acid ◽  
Cell Growth ◽  
Glutamic Acid ◽  
Batch Culture ◽  
Amino Acid Uptake ◽  
Essential Amino Acids ◽  
Growth Yields ◽  
Acid Uptake

The uptake of thirteen essential amino acids by mouse LS cells in suspension culture was determined by bacteriological assay methods. Chemostat continuous-flow cultures were used to determine the effect of different cell growth rates on the quantitative amino acid requirements for growth. The growth yields of the cells ( Y = g cell dry weight produced/g amino acid utilized) were calculated for each of the essential amino acids. A mixture of the non-essential amino acids, serine, alanine and glycine increased the cell yield from the essential amino acids. The growth yields from nearly all the essential amino acids in batch culture were increased when glutamic acid was substituted for the glutamine in the medium. The growth yields from the amino acids in batch culture were much less at the beginning than at the end of the culture. The highest efficiencies of conversion of amino acids to cell material were obtained by chemostat culture. When glutamic acid largely replaced the glutamine in the medium the conversion of amino acid nitrogen to cell nitrogen was 100 % efficient (that is, the theoretical yield was obtained) at the optimum growth rate (cell doubling time, 43 h). The maximum population density a given amino acid mixture will support can be calculated from the data. It is concluded that in several routinely used tissue culture media the cell growth is limited by the amino acid supply. In batch culture glutamine was wasted by (1) its spontaneous decomposition to pyrrolidone carboxylic acid and ammonia, and (2) its enzymic breakdown to glutamic acid and ammonia, but also glutamine was used less efficiently than glutamic acid. Study of the influence of cell growth rate on amino acid uptake rates per unit mass of cells indicated that a marked change in amino acid metabolism occurred at a specific growth rate of 0.4 day -1 (cell doubling time, 43 h). With decrease in specific growth rate below 0.4 day -1 there was a marked stimulation of amino acid uptake rate per cell and essential amino acids were consumed increasingly for functions other than synthesis of cell material.

Amino acid uptake systems in Bacteroides ruminicola

1979 ◽  
Vol 25 (10) ◽  
pp. 1161-1168 ◽  
Author(s):  
Roselynn M. W. Stevenson
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Nitrogen Sources ◽  
Amino Acid Uptake ◽  
Defined Medium ◽  
High Rate ◽  
Transport Systems ◽  
Acid Uptake ◽  
Chemical Structures ◽  
Kinetic Inhibition

Uptake of amino acids by Bacteroides ruminicola was observed in cells grown in a complete defined medium, containing ammonia as the nitrogen source. A high rate of uptake occurred only in fresh medium, as an inhibitory substance, possibly acetate, apparently accumulated during growth. All amino acids except proline were taken up and incorporated into cold trichloroacetic acid precipitable material. Different patterns of incorporation and different responses to 2,4-dinitrophenol and potassium ferricyanide indicated multiple uptake systems were involved. Kinetic inhibition patterns suggested six distinct systems were present for amino acid uptake, with specificities related to the chemical structures of the amino acids. Thus, the failure of free amino acids to act as sole nitrogen sources for growth of B. ruminicola is not due to the absence of transport systems for these compounds.

In vivo muscle amino acid transport involves two distinct processes

2004 ◽  
Vol 287 (1) ◽  
pp. E136-E141 ◽  
Author(s):  
Sharon Miller ◽  
David Chinkes ◽  
David A. MacLean ◽  
Dennis Gore ◽  
Robert R. Wolfe
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Transport ◽  
Interstitial Fluid ◽  
Muscle Blood Flow ◽  
Amino Acid Uptake ◽  
Transport Systems ◽  
Acid Uptake ◽  
Acid Transport ◽  
Rate Limiting

We have tested the hypothesis that transit through the interstitial fluid, rather than across cell membranes, is rate limiting for amino acid uptake from blood into muscle in human subjects. To quantify muscle transmembrane transport of naturally occurring amino acids, we developed a novel 4-pool model that distinguishes between the interstitial and intracellular fluid compartments. Transport kinetics of phenylalanine, leucine, lysine, and alanine were quantified using tracers labeled with stable isotopes. The results indicate that interstitial fluid is a functional compartment insofar as amino acid kinetics are concerned. In the case of leucine and alanine, transit between blood and interstitial fluid was potentially rate limiting for muscle amino acid uptake and release in the postabsorptive state. For example, in the case of leucine, the rate of transport between blood and interstitial fluid compared with the corresponding rate between interstitial fluid and muscle was 247 ± 36 vs. 610 ± 95 nmol·min−1·100 ml leg−1, respectively ( P < 0.05). Our results are consistent with the process of diffusion governing transit from blood to interstitial fluid without selectivity, and of specific amino acid transport systems with varying degrees of efficiency governing transit from interstitial fluid to muscle. These results imply that changes in factors that affect the transit of amino acids from blood through interstitial fluid, such as muscle blood flow or edema, could play a major role in controlling the rate of muscle amino acid uptake.

Peptide uptake from the gastrointestinal tract of sheep

1994 ◽  
Vol 1994 ◽  
pp. 95-95
Author(s):  
M. R. Hipólito-Reis ◽  
J. C. MacRae ◽  
F. R. C. Backwell
Keyword(s):  
Amino Acids ◽  
Gastrointestinal Tract ◽  
Amino Acid Uptake ◽  
Peptide Transport ◽  
Transport Systems ◽  
Total Amino Acid ◽  
Acid Uptake ◽  
Ruminant Species ◽  
Peptide Uptake ◽  
Distinct Peptide

It is known that uptake of di- and tripeptides by distinct peptide transport systems is an important biological process by which amino acids are absorbed from the gastrointestinal tract (Rubino et al 1971; Webb and Bergman, 1991). However, until recently it was generally accepted that absorbed peptides had to be completely hydrolysed in to free amino acids within the enterocyte (Krzysik and Adibi, 1977) prior to their transport into the circulation. Nevertheless, it has been suggested that, in ruminant species at least, a substantial proportion of the total amino acid uptake from the gastrointestinal tract may be in the form of peptides (Webb, 1990; Seal and Parker, 1991; Webb and Bergman, 1991) and that a large part of this absorption may occur across the stomach region (i.e. rumen and omasum) (Webb, 1990). Consequently, the present study was designed to assess the uptake of amino acids in the form of low molecular weight peptides across the gastrointestinal tract of growing lambs.

Dual capacity for nutrient uptake in Tetrahymena. V. Utilization of amino acids and proteins

1979 ◽  
Vol 36 (1) ◽  
pp. 343-353
Author(s):  
E. Orias ◽  
L. Rasmussen
Keyword(s):  
Amino Acids ◽  
Plasma Membrane ◽  
Tetrahymena Thermophila ◽  
Amino Acid Uptake ◽  
Food Vacuole ◽  
Transport Systems ◽  
Acid Uptake ◽  
Vacuole Formation ◽  
Carrier Mediated Transport ◽  
Food Vacuoles

We investigated the relative contributions of phagocytosis and plasma membrane transport to the uptake of amino acids and a protein (egg albumin) in amounts which allow Tetrahymena thermophila to grow and multiply. We used a mutant capable of indefinite growth without food vacuole formation (phagocytosis) and its wild type (phagocytosis-competent) isogenic parental strain. Our results suggest that phagocytosis is not required for free amino acid uptake, most or all of which can be attributed to carrier-mediated transport systems, apparently located on the plasma membrane. In contrast, phagocytosis is required for utilization of the protein. Proteins can supply required amino acids in amounts sufficient for growth only when food vacuoles are formed. We conclude that Tetrahymena thermophila either possesses no endocytic mechanisms at the cell surface other than food vacuole formation or, if it does, these putative mechanisms are not capable of nutritionally meaningful rates of protein uptake.

Placental amino acid uptake. III. Transport systems for neutral amino acids

1976 ◽  
Vol 230 (3) ◽  
pp. 706-710 ◽  
Author(s):  
RH Enders ◽  
RM Judd ◽  
TM Donohue ◽  
CH Smith
Keyword(s):  
Amino Acids ◽  
Competitive Inhibition ◽  
Amino Acid Uptake ◽  
Transport Systems ◽  
Acid Uptake ◽  
Transport Pathways ◽  
Neutral Amino Acids ◽  
Placental Transport ◽  
L System

The human placenta is known to concentrate nearly all amino acids intracellularly for transfer to the fetus. To clarify the mechanism and regulation of this process we have determined the specificity of the principal placental transport systems for neutral amino acids. With the use of competitive inhibition techniques, three transport systems of overlapping specificity have been elucidated. These correspond approximately to the "A", "L", and "ASC" systems of Christensen and associates. In the placenta the specificity of these systems is as follows: A system - alpha aminoisobutyric acid (AIB), glycine, proline, N-methylalanine, alanine, serine, threonine, and glutamine; L system - isoleucine, valine, phenylalanine, BCH, alanine, serine, threonine, and glutamine; and ASC system - alanine, serine, threonine, and glutamine. Placental AIB uptake previously has been shown to increase with preincubation of tissue in vitro. This increase has now been found to be limited to the A system. Activity of the other two systems is essentially unaffected, demonstrating that the transport pathways are separately regulated.

Uptake of amino acids by the marine centric diatom Cyclotella cryptica

1974 ◽  
Vol 20 (8) ◽  
pp. 1109-1118 ◽  
Author(s):  
Ming Sai Liu ◽  
Johan A. Hellebust
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
High Capacity ◽  
Kinetic Studies ◽  
Amino Acid Uptake ◽  
Transport Systems ◽  
Strong Temperature Dependence ◽  
Acid Uptake ◽  
Centric Diatom ◽  
High Concentration

The transport systems for all of the amino acids studied, with the exception of isoleucine, obey saturation kinetics. The strong inhibition of the process by cyanide and dinitrophenol provides evidence that energy is required. Additional evidence for the requirement of energy for amino acid transport is the strong temperature dependence (Q10 about 2) and the high concentration ratios measured for transported amino acids.Transport parameters (Ks and Vmax) for several amino acids were determined from data for two different concentration ranges. The results of the kinetic studies indicate the presence of two or more transport systems that become saturated at different substrate concentrations for each of the amino acids. The presence of a high affinity – high capacity transport system for arginine indicates that this amino acid may be utilized efficiently by the diatom when present at low concentrations in the natural environment.Interactions between pairs of amino acids suggest that several transport systems are available. There appears to be one system for ornithine and arginine, one for glutamate and aspartate, and several for neutral amino acids.Restriction of nitrogen in the growth medium produces a marked increase in the rate of amino acid uptake, indicating that amino acids are acquired more rapidly from the medium by nitrogen-limited cells.

Gamma-Glutamyl-Amino Acids as Signals for the Hormonal Regulation of Amino Acid Uptake by the Mammary Gland of the Lactating Rat

Neonatology ◽  
1985 ◽  
Vol 48 (4) ◽  
pp. 250-256 ◽  
Author(s):  
Juan R. Viña ◽  
Inmaculada R. Puertes ◽  
Juan B. Montoro ◽  
Guillermo T. Saez ◽  
José Viña
Keyword(s):  
Amino Acids ◽  
Mammary Gland ◽  
Amino Acid ◽  
Hormonal Regulation ◽  
Amino Acid Uptake ◽  
Acid Uptake ◽  
Gamma Glutamyl

scholarly journals Utilization in vivo of glucose and volatile fatty acids by sheep brain for the synthesis of acidic amino acids

1966 ◽  
Vol 101 (3) ◽  
pp. 591-597 ◽  
Author(s):  
R M O'Neal ◽  
R E Koeppe ◽  
E I Williams
Keyword(s):  
Amino Acids ◽  
Fatty Acids ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Free Amino Acids ◽  
Free Amino ◽  
Specific Activity ◽  
Tricarboxylic Acid Cycle ◽  
Sheep Brain ◽  
The Brain

1. Free glutamic acid, aspartic acid, glutamic acid from glutamine and, in some instances, the glutamic acid from glutathione and the aspartic acid from N-acetyl-aspartic acid were isolated from the brains of sheep and assayed for radioactivity after intravenous injection of [2-(14)C]glucose, [1-(14)C]acetate, [1-(14)C]butyrate or [2-(14)C]propionate. These brain components were also isolated and analysed from rats that had been given [2-(14)C]propionate. The results indicate that, as in rat brain, glucose is by far the best precursor of the free amino acids of sheep brain. 2. Degradation of the glutamate of brain yielded labelling patterns consistent with the proposal that the major route of pyruvate metabolism in brain is via acetyl-CoA, and that the short-chain fatty acids enter the brain without prior metabolism by other tissue and are metabolized in brain via the tricarboxylic acid cycle. 3. When labelled glucose was used as a precursor, glutamate always had a higher specific activity than glutamine; when labelled fatty acids were used, the reverse was true. These findings add support and complexity to the concept of the metabolic; compartmentation' of the free amino acids of brain. 4. The results from experiments with labelled propionate strongly suggest that brain metabolizes propionate via succinate and that this metabolic route may be a limited but important source of dicarboxylic acids in the brain.

scholarly journals Action of growth hormone in vitro on the net uptake and incorporation into protein of amino acids in muscle from intact rabbits given protein-deficient diets

1976 ◽  
Vol 35 (1) ◽  
pp. 1-10 ◽  
Author(s):  
M. R. Turner ◽  
P. J. Reeds ◽  
K. A. Munday
Keyword(s):  
Amino Acids ◽  
Growth Hormone ◽  
Protein Synthesis ◽  
Amino Acid ◽  
De Novo ◽  
Amino Acid Uptake ◽  
Acid Uptake ◽  
Amino Acid Incorporation ◽  
Acid Incorporation

1. Net amino acid uptake, and incorporation into protein have been measured in vitro in the presence and absence of porcine growth hormone (GH) in muscle from intact rabbits fed for 5 d on low-protein (LP), protein-free (PF) or control diets.2. In muscle from control and LP animals GH had no effect on the net amino acid uptake but stimulated amino acid incorporation into protein, although this response was less in LP animals than in control animals.3. In muscle from PF animals, GH stimulated both amino acid incorporation into protein and the net amino acid uptake, a type of response which also occurs in hypophysectomized animals. The magnitude of the effect of GH on the incorporation of amino acids into protein was reduced in muscle from PF animals.4. The effect of GH on the net amino acid uptake in PF animals was completely blocked by cycloheximide; the uptake effect of GH in these animals was dependent therefore on de novo protein synthesis.5. It is proposed that in the adult the role of growth hormone in protein metabolism is to sustain cellular protein synthesis when there is a decrease in the level of substrate amino acids, similar to that which occurs during a short-term fast or when the dietary protein intake is inadequate.

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