Augmented Thermic Effect of Amino Acids under General Anaesthesia Occurs Predominantly in Extra-Splanchnic Tissues

1996 ◽  
Vol 91 (4) ◽  
pp. 431-439 ◽  
Author(s):  
Eva Selldén ◽  
Robert Bränstróam ◽  
Tomas Brundin

1. Intravenous infusion of amino acid mixtures stimulates human oxidative heat production more effectively under general anaesthesia than in the unanaesthetized state. To analyse the splanchnic and extra-splanchnic regional distribution of this stimulation, whole body and splanchnic oxygen uptake, blood flow and blood temperatures were measured by a catheterization technique in 14 patients undergoing isoflurane anaesthesia for abdominal surgery. During the anaesthesia period, a mixture of 19 amino acids (240 kJ/h) was infused intravenously into seven of the patients while the others served as controls, receiving isovolumic infusions of a nutrient-free saline solution. 2. Whole body oxygen consumption fell by ≈ 40% during anaesthesia and surgery in the controls. Approximately 80–95% of the reduction occurred in the extra-splanchnic tissues. The splanchnic oxygen uptake fell by 31 ± 6% in the controls during the initial phase of anaesthesia, after which it returned to the pre-anaesthesia level. The initial reduction of the controls' splanchnic oxygen consumption accounted for only ≈23% of the simultaneous anaesthesia-induced reduction in pulmonary oxygen uptake. No initial reduction of the splanchnic oxygen uptake was observed in the patients treated with amino acid. 3. The amino acid infusion stimulated the whole body oxidative heat production by ≈18 W during anaesthesia and surgery and by ≈70 W at the emergence from anaesthesia. Approximately 74% of the stimulation occurred in the extra-splanchnic tissues. At awakening, the splanchnic oxygen uptake rose to ≈64% above the pre-anaesthesia level in the amino acid group. 4. During the entire period of anaesthesia, the whole body heat content fell by 282 ± 68 kJ in the controls and by 57 ± 25 kJ in the amino acid group. Amino acid treatment thus prevented ≈80% of the anaesthesia-induced reduction in whole body heat content. 5. During anaesthesia and surgery, cardiac output was ≈25% and ≈6% below the baseline, pre-anaesthesia levels in the control and amino acid groups, respectively. At awakening, it rose to ≈44% above baseline in the amino acid group while in the controls it remained unchanged. In both groups the splanchnic blood flow was unaffected by anaesthesia or by amino acid infusions.

1994 ◽  
Vol 267 (5) ◽  
pp. E648-E655 ◽  
Author(s):  
T. Brundin ◽  
J. Wahren

The renal contribution to the amino acid-induced whole body thermogenesis was examined. Using indirect calorimetry and catheter techniques, pulmonary and renal oxygen uptake and blood flow, blood temperatures, and net renal exchange of amino acids, glucose and lactate were measured in eight healthy men before and during 3 h of intravenous infusion of 720 kJ of an amino acid solution. During the infusion, the pulmonary oxygen uptake increased from 252 +/- 12 to 310 +/- 8 ml/min, cardiac output increased from 5.9 +/- 0.3 to 6.8 +/- 0.3 l/min, and the arterial blood temperature increased from 36.34 +/- 0.04 to 36.68 +/- 0.07 degrees C. Renal oxygen consumption, heat production, blood flow, and net glucose exchange remained unchanged during the infusion. The net renal uptake of amino acid energy from the blood rose from 2 +/- 2 to 11 +/- 4 W. The total renal energy expenditure was 9-10 W throughout the study period. It is concluded that intravenous amino acid infusion greatly augments the uptake and utilization of amino acids in the kidneys but does not stimulate the renal oxygen consumption, heat production, blood flow, or glucose release.


1991 ◽  
Vol 11 (4) ◽  
pp. 223-230 ◽  
Author(s):  
C. Picó ◽  
A. Pons ◽  
A. Palou

It is well known that the amino acids in the blood are distributed between the plasma and inside the cells. This study was conducted to determine whether amino acids can be located adsorbed on blood cell membranes. The amino acid concentration in the deproteinized haemolysed blood was higher than that in the fraction of blood after removal of the blood cell membranes by centrifugation. These results showed that a pool of amino acids representing 21.1% of the whole blood cell amino acids was adsorbed on the blood cell membranes of adult Wistar rats. The non-polar amino acids showed high adsorption on the membrane, whereas out of the polar amino acid group, only the non-ionic amino acids did adsorb.


1994 ◽  
Vol 266 (3) ◽  
pp. E396-E402 ◽  
Author(s):  
T. Brundin ◽  
J. Wahren

The thermic effect of amino acid administration was examined in healthy subjects. Pulmonary and splanchnic oxygen uptake, cardiac output, splanchnic blood flow, and blood temperatures were measured in eight healthy men before and during 2.5 h of intravenous infusion of 600 kJ of a mixture of 19 amino acids. Indirect calorimetry and catheter techniques were used, including thermometry in arterial and a hepatic venous blood. During the infusion, pulmonary oxygen uptake rose progressively from a basal value of 269 +/- 6 to 321 +/- 8 ml/min after 2.5 h. The splanchnic oxygen consumption increased from a basal level of 64 +/- 4 to a peak value of 91 +/- 7 ml/min after 2 h of infusion. The 2.5 h average splanchnic proportion of the amino acid-induced whole body thermogenesis was 51 +/- 11%. Cardiac output increased from 6.2 +/- 0.3 in the basal state to 7.3 +/- 0.4 l/min, whereas the splanchnic blood flow remained unchanged during the infusion period. The arteriohepatic venous oxygen difference increased from 51 +/- 4 in the basal state to 65 +/- 5 ml/l after 2 h of amino acid infusion. The blood temperature rose by approximately 0.25 degrees C during the amino acid infusion, reflecting an increased heat accumulation in the body. It is concluded that the splanchnic tissues account for approximately one-half of the amino acid-induced whole body thermogenesis, that amino acid infusion augments blood flow in the extrasplanchnic but not in the splanchnic tissues, and stimulates the accumulation of heat in the body most likely via a resetting of the central thermosensors.


1981 ◽  
Author(s):  
U T Yardimci ◽  
A Özbilen ◽  
O N Ulutin

We have studied the transport systems for amino acids in platelets. Na+/K+ dependent active transport systems were found to be responsible for the transport of amino acids through the platelet membrane (Km’s being at uM ranges). We have also isolated the binding proteins for amino acids from platelet membranes as the carriers involved in these active transport systems by cold osmotic shock procedure. Each amino acid besides being transported by a specific active transport system may be subject to transport by group amino acid transport systems.Group amino acid transport systems are classified by countertransport experiments as follows: Neutral amino acid group transport systems: IA: glycine, alanine, serine, threonine IB: valine, leucine, isoleucine, serine,threonine IC: cysteine, methionine, proline Basic amino acid group transport systems: lie: lysine IIB: histidine, arginine Acidic amino acid group transport systems: III A: Aspartic acid, glutamic acid Aromatic amino acid group transport systems: IVC: Phenylalanine,tyrosine, histidine, proline.


1947 ◽  
Vol 25c (1) ◽  
pp. 20-26 ◽  
Author(s):  
A. G. Lochhead ◽  
R. H. Thexton

Comparative studies of the relative incidence of bacteria of different nutritional requirements in soil indicate that one of the most characteristic rhizosphere effects is the preferential stimulation of bacteria requiring amino acids for maximum growth. Organisms for which amino acids are either essential or stimulative were proportionately increased in the rhizosphere. No similar effect was noted with respect to bacteria responding to growth factors.The findings suggest, by indirect evidence, that the effect is to be ascribed to the excretion of amino acids by the growing plant. However, though this may be the chief factor, the preferential stimulation of the amino acid group of bacteria may be related to associative and antibiotic effects exerted by other bacteria, stimulated in the rhizosphere, observed to have different degrees of compatibility towards those responding respectively to amino acids and growth factors.


2019 ◽  
Vol 110 (2) ◽  
pp. 255-264 ◽  
Author(s):  
Paolo Tessari

ABSTRACT Background Essential amino acids (EAAs) are key factors in determining dietary protein quality. Their RDAs have been estimated. However, although nonessential amino acids (NEAAs) are utilized for protein synthesis too, no estimates of their usage for body protein replenishment have been proposed so far. Objective The aim of this study was to provide minimum, approximate estimates of NEAA usage for body protein replenishment/conservation in humans. Methods A correlation between the pattern of both EAAs and NEAAs in body proteins, and their usage, was assumed. In order to reconstruct an “average” amino acid pattern/composition of total body proteins (as grams of amino acid per gram of protein), published data of relevant human organs/tissues (skeletal muscle, liver, kidney, gut, and collagen, making up ∼74% of total proteins) were retrieved. The (unknown) amino acid composition of residual proteins (∼26% of total proteins) was assumed to be the same as for the sum of the aforementioned organs excluding collagen. Using international EAA RDA values, an average ratio of EAA RDA to the calculated whole-body EAA composition was derived. This ratio was then used to back-calculate NEAA usage for protein replenishment. The data were calculated also using estimated organ/tissue amino acid turnover. Results The individual ratios of World Health Organization/Food and Agriculture Organization/United Nations University RDA to EAA content ranged between 1.35 (phenylalanine + tyrosine) and 3.68 (leucine), with a mean ± SD value of 2.72 ± 0.81. In a reference 70-kg subject, calculated NEAA usage for body protein replenishment ranged from 0.73 g/d for asparagine to 3.61 g/d for proline. Use of amino acid turnover data yielded similar results. Total NEAA usage for body protein replenishment was ∼19 g/d (45% of total NEAA intake), whereas ∼24 g/d was used for other routes. Conclusion This method may provide indirect minimum estimates of the usage of NEAAs for body protein replacement in humans.


Author(s):  
M.F. Fuller ◽  
R. McWilliam ◽  
T.C. Wang

The optimal balance of amino acids in the diet of the growing pig was estimated by ARC (1981) on the basis of a number of disparate studies augmented by data on the amino acid composition of the whole body on the premise that the amino acids incorporated into accreted body proteins are the major determinant of requirements and that this pattern is not distorted by inequalities in the utilisation of individual amino acids. In an accompanying paper (Wang & Fuller, paper no. 91) an optimal pattern was derived by direct experiment which was shown to be utilised better than that described by ARC (1981). That pattern, however, which related to one particular rate of nitrogen input and the particular rate of protein accretion which that input supported, includes two components, a requirement for maintenance and a requirement for protein accretion. There is clear evidence from studies with rats and chicks that the optimal pattern of amino acids for maintenance and growth are quite different and so the optimal pattern for any particular rate of growth will depend on the relative contributions of the two components. The purpose of this experiment was to estimate both.


1997 ◽  
Vol 272 (4) ◽  
pp. E592-E599 ◽  
Author(s):  
B. B. Poindexter ◽  
C. A. Karn ◽  
J. A. Ahlrichs ◽  
J. Wang ◽  
C. A. Leitch ◽  
...  

To determine how increased amino acid availability alters rates of whole body proteolysis and the irreversible catabolism of the essential amino acids leucine and phenylalanine throughout the neonatal period, leucine and phenylalanine kinetics were measured under basal conditions and in response to intravenous amino acids in two separate groups of healthy, full-term newborns (at 3 days and 3 wk of age). The endogenous rates of appearance of leucine and phenylalanine (reflecting proteolysis) were suppressed equally in both groups and in a dose-dependent fashion (by approximately 10% with 1.2 g x kg(-1) x day(-1) and by approximately 20% with 2.4 g x kg(-1) x day(-1)) in response to intravenous amino acid delivery. Insulin concentrations remained unchanged from basal values during amino acid administration. The irreversible catabolism of leucine and phenylalanine increased in a stepwise fashion in response to intravenous amino acids; again, no differences were observed between the two groups. This study clearly demonstrates that the capacity to acutely increase rates of leucine oxidation and phenylalanine hydroxylation is fully present early in the neonatal period in normal newborns. Furthermore, these data suggest that amino acid availability is a primary regulator of proteolysis in normal newborns throughout the neonatal period.


2005 ◽  
Vol 88 (3) ◽  
pp. 923-934 ◽  
Author(s):  
Malcolm F Fuller ◽  
Daniel Tomé

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.


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