scholarly journals The feeding route (enteral or parenteral) affects the plasma response of the dipetide Ala-Gln and the amino acids glutamine, citrulline and arginine, with the administration of Ala-Gln in preoperative patients

2005 ◽  
Vol 94 (1) ◽  
pp. 19-26 ◽  
Author(s):  
Gerdien C. Melis ◽  
Petra G. Boelens ◽  
Joost R. M. van der Sijp ◽  
Theodora Popovici ◽  
Jean-Pascal De Bandt ◽  
...  
Keyword(s):  
Amino Acids ◽  
Plasma Levels ◽  
Plasma Concentrations ◽  
High Availability ◽  
Blood Samples ◽  
Arterial Blood ◽  
Plasma Response ◽  
Enteral Administration ◽  
Plasma Arginine ◽  
Arginine Concentration

Enhancement of depressed plasma concentrations of glutamine and arginine is associated with better clinical outcome. Supplementation of glutamine might be a way to provide the patient with glutamine, and also arginine, because glutamine provides the kidney with citrulline, from which the kidney produces arginine when plasma levels of arginine are low. The aim of the present study was to investigate the parenteral and enteral response of the administered dipeptide Ala-Gln, glutamine, citrulline and arginine. Therefore, seven patients received 20 g Ala-Gln, administered over 4 h, parenterally or enterally, on two separate occasions. Arterial blood samples were taken before and during the administration of Ala-Gln. ANOVA and a pairedttest were used to test differences (P<0·05). Ala-Gln was undetectable with enteral administration, whereas Ala-Gln remained stable at a plasma concentration of 268 μmol/l throughout parenteral infusion and rapidly decreased towards zero after infusion was stopped. The highest level of glutamine was observed with parenteral infusion of the dipeptide, although enteral infusion also significantly increased plasma levels of glutamine. The highest plasma response of citrulline was observed with the enteral administration of the dipeptide, although parenteral administration also increased plasma levels of citrulline. Plasma arginine increased significantly with parenteral infusion, but not with enteral administration of Ala-Gln. In conclusion, administrations of Ala-Gln, parenteral or enteral, resulted in an increased plasma glutamine response, as compared with baseline. Interestingly, in spite of the high availability of citrulline with enteral administration of the dipeptide, only parenteral infusion of Ala-Gln increased plasma arginine concentration.

Inhibin immunoneutralization by antibodies raised against synthetic peptide sequences of inhibin α subunit: effects on gonadotrophin concentrations and ovulation rate in sheep

1990 ◽  
Vol 124 (1) ◽  
pp. 167-176 ◽  
Author(s):  
J. H. M. Wrathall ◽  
B. J. McLeod ◽  
R. G. Glencross ◽  
A. J. Beard ◽  
P. G. Knight
Keyword(s):  
Plasma Levels ◽  
Synthetic Peptide ◽  
Plasma Concentrations ◽  
Ovulation Rate ◽  
Control Groups ◽  
Α Subunit ◽  
Blood Samples ◽  
Antigenic Properties ◽  
N Terminus ◽  
The Mean

ABSTRACT Two experiments were conducted to explore the effectiveness of synthetic peptide-based vaccines for active and passive autoimmunization of sheep against inhibin. In the first experiment, adult Romney ewes (n = 20) were actively immunized against a synthetically produced peptide that corresponded to the N-terminus of the α-subunit of bovine inhibin (bIα(1–29)-Tyr30). This peptide was conjugated to tuberculin purified protein derivative (PPD) to increase its antigenic properties. Control groups comprised non-immunized (n = 10) and PPD-immunized (n = 10) ewes. Primary immunization (400 μg conjugate/ewe) was followed by two booster immunizations (200 μg conjugate/ewe), given 5 and 8 weeks later. Following synchronization of oestrus using progestagen sponges, ovulation rates were assessed by laparoscopy. Weekly blood samples were taken throughout the experiment. All inhibin-immunized ewes produced antibodies which bound 125I-labelled bovine inhibin (Mr 32 000), and ovulation rate in inhibin-immunized ewes (2·15 ± 0·22; mean ± s.e.m.) was significantly (P<0·01) greater than in both non-immunized (0·90 ± 0·23) and PPD-immunized (1·20 ± 0·13) control groups. Immunization against the peptide, but not against PPD alone, resulted in a modest rise in plasma FSH, with mean levels after the second boost being significantly (P<0·025) higher (22%) than those before immunization. Moreover, when blood samples were taken (2-h intervals) from randomly selected groups of control (n = 7) and inhibin-immunized (n = 7) ewes for an 84-h period following withdrawal of progestagen sponges, the mean plasma concentration of FSH during the 48 h immediately before the preovulatory LH surge was 37% greater (P< 0·025) in immunized than in control animals. However, more frequent blood sampling (every 15 min for 12 h) during follicular and mid-luteal phases of the oestrous cycle revealed no significant differences between treatment groups in mean plasma concentrations of FSH. In addition, neither mean concentrations of LH nor the frequency and amplitude of LH episodes differed between immunized and control ewes. However, the mean response of LH to a 2 μg bolus of gonadotrophin-releasing hormone, given during the luteal phase, was significantly (P<0·05) less in immunized than in control ewes. These findings indicate that active immunization of Romney ewes against a synthetic fragment of inhibin can promote a controlled increase in ovulation rate, but this response cannot be unequivocally related to an increase in plasma levels of FSH. In the second experiment, passive immunization of seasonally anoestrous ewes (mule × Suffolk crossbred; n = 6 per group) against inhibin, using an antiserum raised in sheep against a synthetic peptide corresponding to the N-terminus of the α-subunit of human inhibin promoted a rapid (<3 h), dose-dependent rise in plasma levels of FSH which remained increased (2·5-fold; P<0·001) for up to 30 h. Plasma concentrations of LH, however, were unaffected by treatment with the antiserum. It is deduced from this observation that, even in the seasonally anoestrous ewe, the ovary secretes physiologically active levels of inhibin, which exert an inhibitory action on the synthesis and secretion of FSH. Journal of Endocrinology (1990) 124, 167–176

Charge-Affected Transperitoneal Movement of Amino Acids in Capd

1996 ◽  
Vol 16 (1_suppl) ◽  
pp. 88-90 ◽  
Author(s):  
Toshiyuki Nakao ◽  
Makoto Ogura ◽  
Hajime Takahashi ◽  
Tomonari Okada
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Dwell Time ◽  
Plasma Concentrations ◽  
University Hospital ◽  
Blood Samples ◽  
Significant Difference ◽  
Molecular Charge ◽  
Solute Movement ◽  
Positively Charged

Our objective was to investigate the influence of molecular charge on transperitoneal solute movement in continuous ambulatory peritoneal dialysis (CAPD). Tests of peritoneal equilibration were performed. Two liters of 2.27% or 2.5% glucose CAPD dialysate were infused and the dialysate samples were taken after 2 hr and 4 hr, and blood samples were obtained after 4-hr dwell time. Dialysate-to-plasma concentrations ratios (DIP) were calculated for creatinine (Cr) and three amino acids with almost the same molecular weight but quite different charges: glutamic acids (Glu: negatively charged), glutamine (Gin: near neutrally charged), and lysine (Lys: positively charged). The setting was a university hospital. There were 23 stable CAPD patients with a mean age of 56.5±9.5 years and a mean CAPD duration of 15.2±19.4 months. DIP ratio of Glu was much lower than those of Gin, Lys and Cr at both 2 hr and 4 hr (p < 0.01), and DIP of Lys was significantly lower than that of Gin (p < 0.01). There was no significant difference of DIP between Gin and Cr. The order of transperitoneal mobility among the three amino acids was Gin > Lys > Glu. Transperitoneal movement of solutes in CAPD is influenced by molecular charge, the movement of negatively charged solutes is most remarkably retarded in cases of amino acids.

ANNUAL VARIATIONS IN PLASMA LEVELS OF TESTOSTERONE AND LUTEINIZING HORMONE IN THE LABORATORY MALE MONGREL DOG

1980 ◽  
Vol 86 (3) ◽  
pp. 425-430 ◽  
Author(s):  
R. E. FALVO ◽  
L. R. DEPALATIS ◽  
J. MOORE ◽  
T. A. KEPIC ◽  
J. MILLER
Keyword(s):  
Plasma Levels ◽  
Plasma Concentrations ◽  
Significant Rise ◽  
Release Mechanism ◽  
Cyclic Pattern ◽  
Blood Samples ◽  
Annual Variations ◽  
Mongrel Dog ◽  
The Mean ◽  
Cyclic Changes

Blood samples, drawn every 15 days (September 1975–September 1976) from four laboratory-housed male mongrel dogs, were assayed by radioimmunoassay for levels of testosterone and LH in the plasma. The mean plasma concentrations of testosterone remained relatively constant for most of the year with the exception of a significant rise in late August and early September. Mean plasma levels of LH showed a cyclic pattern throughout the year which could be represented by a cosine function curve. However, this cyclic pattern of LH was not accompanied by cyclic changes in plasma levels of testosterone and there was no relationship between these two hormones during the period of 1 year. As the cyclic pattern of LH was altered, the plasma level of testosterone began to rise and reached its highest concentration. Since this alteration of the LH cycle occurred before the increased concentrations of testosterone, and since there was no relationship between these two hormones for the period of a year, we have concluded that there may be another hormone(s) involved which either alters the sensitivity of the canine testis to LH or alters the LH synthesis/release mechanism of the pituitary gland.

scholarly journals Influence of Circulating Epinephrine and Norepinephrine on Insulin-Like Growth Factor Binding Protein-1 in Humans

1997 ◽  
Vol 82 (8) ◽  
pp. 2677-2680 ◽  
Author(s):  
Eva Fernqvist-Forbes ◽  
Agneta Hilding ◽  
Karin Ekberg ◽  
Kerstin Brismar
Keyword(s):  
Growth Factor ◽  
Binding Protein ◽  
Serum Insulin ◽  
Plasma Concentrations ◽  
Insulin Like Growth Factor ◽  
Blood Samples ◽  
C Peptide ◽  
Healthy Men ◽  
Factor Binding ◽  
Arterial Blood

The aim of the present study was to investigate the influence of circulating epinephrine (Epi) and norepinephrine (Norepi) on serum insulin-like growth factor binding protein-1 (IGFBP-1) concentrations. Healthy men received 0.3 nmol·kg·min Epi iv (n = 6), 0.5 nmol·kg·min Norepi iv (n = 7), or saline (n= 5) during 30 min. Arterial blood samples were obtained before, during, and 120 min after infusion. During the catecholamine infusion arterial Epi and Norepi plasma concentrations reached 6.35 ± 0.53 and 15.65 ± 2.71 nmol/L, respectively, which resulted in significant increases in glucose concentrations. When Epi was infused, IGFBP-1 increased from 45 ± 6 μg/L to 76 ± 10 μg/L (P &lt; 0.05) 60 min after the infusion. Epi was also followed by increases in insulin, C-peptide, and glucagon. Norepi resulted in a slight increase in circulating IGFBP-1 (43 ± 6 to 54 ± 8 nmol/L, NS). The findings suggest that Epi, at plasma concentrations similar to those reached during physical stress, stimulates the production of IGFBP-1 in humans.

scholarly journals Interactions among the branched-chain amino acids and their effects on methionine utilization in growing pigs: effects on plasma amino– and keto–acid concentrations and branched-chain keto-acid dehydrogenase activity

2000 ◽  
Vol 83 (1) ◽  
pp. 49-58 ◽  
Author(s):  
Stefan Langer ◽  
Peter W. D. Scislowski ◽  
David S. Brown ◽  
Peter Dewey ◽  
Malcolm F. Fuller
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Plasma Concentrations ◽  
Biceps Femoris ◽  
Branched Chain Amino Acids ◽  
Growing Pigs ◽  
Keto Acid ◽  
Blood Samples ◽  
Acid Dehydrogenase ◽  
Branched Chain

The present experiment was designed to elucidate the mechanism of the methionine-sparing effect of excess branched-chain amino acids (BCAA) reported in the previous paper (Langer & Fuller, 2000). Twelve growing gilts (30–35 kg) were prepared with arterial catheters. After recovery, they received for 7 d a semipurified diet with a balanced amino acid pattern. On the 7th day blood samples were taken before (16 h postabsorptive) and after the morning meal (4 h postprandial). The animals were then divided into three groups and received for a further 7 d a methionine-limiting diet (80 % of requirement) (1) without any amino acid excess; (2) with excess leucine (50 % over requirement); or (3) with excesses of all three BCAA (leucine, isoleucine, valine, each 50 % over the requirement). On the 7th day blood samples were taken as in the first period, after which the animals were killed and liver and muscle samples taken. Plasma amino acid and branched-chain keto acid (BCKA) concentrations in the blood and branched-chain keto-acid dehydrogenase (BCKDH; EC 1.2.4.4) activity in liver and muscle homogenates were determined. Compared with those on the balanced diet, pigs fed on methionine-limiting diets had significantly lower (P < 0·05) plasma methionine concentrations in the postprandial but not in the postabsorptive state. There was no effect of either leucine or a mixture of all three BCAA fed in excess on plasma methionine concentrations. Excess dietary leucine reduced (P < 0·05) the plasma concentrations of isoleucine and valine in both the postprandial and postabsorptive states. Plasma concentrations of the BCKA reflected the changes in the corresponding amino acids. Basal BCKDH activity in the liver and total BCKDH activity in the biceps femoris muscle were significantly (P < 0·05) increased by excesses of leucine or all BCAA.

scholarly journals Postprandial Plasma Amino Acid Responses Between Standard Whey Protein Isolate and Whey Protein Isolate Plus Novel Technology

2019 ◽  
Vol 12 ◽  
pp. 117863881982797 ◽  
Author(s):  
Matthew H Sharp ◽  
Matthew W Stefan ◽  
Ryan P Lowery ◽  
Jacob M Wilson
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Whey Protein ◽  
Plasma Levels ◽  
Muscle Protein ◽  
Plasma Concentrations ◽  
Whey Protein Isolate ◽  
Protein Isolate ◽  
Plasma Amino Acid ◽  
Whole Body

Background: Muscle mass is an important determinant of metabolic health and physical function. It has previously been demonstrated that the postprandial rise in circulating essential amino acids (EAA) acts as the main stimulus for muscle protein synthesis (MPS). This study investigated postprandial plasma amino acid (AA) responses of 2 different forms of whey protein isolate (WPI) with iso-caloric and iso-nitrogenous profiles to investigate plasma concentrations of EAA. Methods: In all, 12 healthy men (n = 12) between 19 and 32 years of age were recruited for a randomized, cross-over design, which involved consumption of protein supplements on 2 testing days separated by a 6-day washout period between conditions. On each testing day, subjects consumed either 29.6 g of WPI or WPI + io (whey protein isolate plus Ingredient Optimized Protein®) mixed with 236 mL of water. Plasma EAA and branch chain amino acid (BCAA) concentrations were assessed from whole body donated by subjects at pre-consumption and 30, 60, 90, 120, and 180 minutes post consumption. Results: Plasma levels of total EAA concentration was significantly greater in WPI + io at 30, 60, 90, and 120 minutes post consumption ( P < .01, P < .001, P < .01, and P < .01, respectively). Plasma levels of total BCAA concentration was significantly greater in WPI + io at 30, 60, 90, and 120 minutes post consumption ( P < .01, P < .001, P < .01, and P < .05, respectively) compared with WPI. For leucine, only WPI + io had elevated levels compared with pre-test at 90 minutes post consumption ( P < .001). Discussion: Both conditions significantly elevated EAA, BCAA, and leucine from basal levels. However, we conclude that the consumption of the treated WPI significantly raises plasma EAA, BCAA, and leucine to a greater extent compared with WPI with no treatment. Thus, supplementation with WPI that has undergone Ingredient Optimized® technology may be highly beneficial for those who partake in regular exercise, elderly individuals, or those affected by a reduced sensitivity to amino acids.

Plasma concentrations of tryptophan and other amino acids in manic-depressive patients

1974 ◽  
Vol 4 (3) ◽  
pp. 334-337 ◽  
Author(s):  
Jancis R. Rees ◽  
M. N. E. Allsopp ◽  
R. P. Hullin
Keyword(s):  
Amino Acids ◽  
Plasma Concentrations ◽  
Affective State ◽  
Depressive Patient ◽  
Blood Samples ◽  
Short Cycle ◽  
Serial Blood ◽  
Plasma Tryptophan ◽  
Manic Depressive ◽  
Depressive Patients

SYSNOPSISPlasma tryptophan concentrations were determined in serial blood samples from a short cycle (two to three day) manic-depressive patient and four manic-depressive patients with longer (60 day) affective cycles. Tryptophan levels varied significantly with affective state in the short cycle patient and one of the longer cycle patients. Correlation in the short cycle patient was better with blood samples taken at 3 p.m. than at 9 a.m.

Effects of small C-ANF receptor ligands on plasma levels of atrial natriuretic factor, blood pressure, and renal function in the rat

1991 ◽  
Vol 69 (10) ◽  
pp. 1561-1566 ◽  
Author(s):  
Juraj Okolicany ◽  
Glenn A. McEnroe ◽  
Lisa C. Gregory ◽  
John A. Lewicki ◽  
Thomas Maack
Keyword(s):  
Blood Pressure ◽  
Amino Acids ◽  
Glomerular Filtration Rate ◽  
Glomerular Filtration ◽  
Plasma Levels ◽  
Sodium Excretion ◽  
Filtration Rate ◽  
Recovery Period ◽  
Receptor Ligands ◽  
Arterial Blood

In this article, after a very brief review on ANF receptors, we report our study on the effects of small C-ANF receptor ligands in the rat. Two small ligands were synthesized: 2-napthoxyacetyl-isonipecotyl-rANF 11–15-NH2 (5 aa), containing 5 amino acids; and Ala7-rANF 8–17-NH2 (10 aa), containing 10 amino acids from the ring structure of ANF 1–28. After control periods, 5 aa or 10 aa were infused i.v. at a dose of 10 μg∙min−1∙kg−1 body weight for 70 min in anesthetized rats, followed by a 60-min recovery period. The 5 aa and 10 aa peptides significantly and reversibly increased plasma levels of endogenous immunoreactive ANF by 106 ± 29 and 52 ± 24 pg/mL, respectively. Infusion of the 5 aa peptide significantly decreased mean arterial blood pressure from 113 ± 1 to 100 ± 3 mmHg (1 mmHg = 133.32 Pa) and increased glomerular filtration rate from 1.6 ± 0.2 to 2.3 ± 0.2 mL/min, sodium excretion from 0.6 ± 0.3 to 3.4 ± 0.4 μmol/min, and potassium excretion from 0.5 ± 0.2 to 1.2 ± 0.2 μmol/min. Similar results were obtained with the 10 aa peptide. The effects of both peptides on blood pressure and sodium excretion persisted throughout the recovery period. The results confirm and extend previous observations showing that C-ANF receptors mediate the removal of ANF from the circulation. The shortening of the minimal peptide length necessary to bind to C-ANF receptors markedly enhances the possibility of developing orally active C-ANF receptor ligands for the treatment of cardiovascular and renal diseases.Key words: C-ANF receptors, linear atrial peptides, glomerular filtration rate, natriuresis, kaliuresis.

Urinary Excretion and Plasma Levels of Free Ninhydrin Reactive Compounds in X-Irradiated Rats

1956 ◽  
Vol 186 (1) ◽  
pp. 175-179 ◽  
Author(s):  
R. E. Kay ◽  
D. C. Harris ◽  
C. Entenman
Keyword(s):  
Amino Acids ◽  
Urinary Excretion ◽  
Plasma Levels ◽  
Plasma Concentrations ◽  
Liver Glycogen ◽  
Cysteic Acid ◽  
Whole Body ◽  
X Rays ◽  
X Irradiation ◽  
Sulfur Containing

Urinary excretion and plasma levels of ninhydrin-reactive compounds in x-irradiated rats were quantitatively studied. In the urinary excretion studies fasted rats were exposed to either a sublethal (450 r) or superlethal (2500 r) dose of whole-body 250 kvp x-rays. Twenty-four-hour urines, taken from two days preirradiation to 3 days postirradiation, were analyzed for ninhydrin-reactive compounds. During the day following x-irradiation, rats exposed to either sublethal or superlethal irradiation excreted increased amounts of urinary taurine, cysteic acid, leucine and valine. In the plasma studies four groups of rats were exposed to 600 r of whole-body x-irradiation. At 6, 12, 24 and 30 hours after irradiation plasma was analyzed for ninhydrin-reactive compounds and creatinine. Transitory elevations in plasma concentrations of lysine, glutamine, taurine, methionine, valine and leucine were observed, while elevations in the levels of arginine, serine plus glycine, threonine, alanine and creatinine were not noted. The increased urinary excretion of nonglycogenic amino acids and the increased plasma concentrations of the nonglycogenic amino acids may be the result of a breakdown of protein or protein-like compounds to amino acids with the subsequent rapid conversion of the excess glycogenic amino acids to liver glycogen. The early excessive excretion of taurine in the x-irradiated rat suggests an increased oxidation of sulfur containing compounds.

Pulmonary Disposition of Propofol in Surgical Patients

2000 ◽  
Vol 93 (4) ◽  
pp. 986-991 ◽  
Author(s):  
Yan-Ling He ◽  
Hiroshi Ueyama ◽  
Chikara Tashiro ◽  
Takashi Mashimo ◽  
Ikuto Yoshiya
Keyword(s):  
Plasma Concentrations ◽  
Area Under The Curve ◽  
Back Diffusion ◽  
Blood Samples ◽  
Arterial Blood ◽  
Pulmonary Uptake ◽  
Human Lungs ◽  
Infusion Study ◽  
Significant Difference ◽  
First Pass

Background The lungs have been mentioned as a possible site contributing to the extrahepatic clearance of propofol. The objective of the present study was to clarify the pulmonary disposition of propofol directly in human lungs by investigating both the first-pass uptake and pulmonary extraction at pseudo-steady state. Methods Nine patients were enrolled in the first-pass uptake study. Propofol (5 mg) and indocyanine green (ICG; 15 mg) were simultaneously administered via a central venous catheter within 1 s, and sequential arterial blood samples were obtained from the radial artery at 1-s intervals up to 45 s. Eleven patients were included in the infusion study, and propofol was infused via the jugular vein at a rate of 50 microgram. kg-1. min-1. Blood samples were simultaneously collected from pulmonary and radial arteries up to 60 min. Results A pronounced difference in the dilution curves between propofol and ICG was observed, and 28.4 +/- 11.6% (mean +/- SD) of propofol was taken up during the single passage through the human lung. The mean pulmonary transit time of propofol (31.3 +/- 6.0 s) was significantly longer than that of ICG (22.4 +/- 2.7 s; P &lt; 0.01), indicating that some of the propofol trapped by lungs returned to the circulation by back diffusion. In the constant infusion study, no significant differences were observed with the plasma concentrations of propofol between pulmonary and radial arteries except for that at 2 min. The area under the curve of pulmonary and radial arterial concentration curves to 60 min were 59.1 +/- 14.8 and 56.8 +/- 12.5 microg. ml-1. min-1, respectively. No significant difference was observed with the area under the curve, suggesting that metabolism was not involved in the pulmonary uptake in human lungs. Conclusions Most of the propofol that undergoes pulmonary uptake during the first pass was released back to the circulation by back diffusion. Metabolism was not involved in the pulmonary uptake in human lungs.

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