scholarly journals PROTEOSE INTOXICATIONS AND INJURY OF BODY PROTEIN

1918 ◽  
Vol 28 (2) ◽  
pp. 213-221 ◽  
Author(s):  
G. H. Whipple ◽  
Donald D. Van Slyke
Keyword(s):  
Blood Urea Nitrogen ◽  
Protein Metabolism ◽  
Vicious Circle ◽  
Acute Intoxication ◽  
Food Proteins ◽  
Protein Nitrogen ◽  
Urea Nitrogen ◽  
Body Protein ◽  
End Products

The acute intoxication following an injection of a toxic proteose is usually associated with a large increase (40 per cent or more) in the non-protein nitrogen of the blood. This increase is found chiefly in the blood urea nitrogen, but the amino and peptide nitrogens also may show small increases. The changes observed in the blood non-protein nitrogen are identical with those which follow the feeding of large amounts of meat (8). These facts indicate that the proteose intoxication causes an abnormally rapid autodigestion of tissue proteins, but that the nitrogenous end-products are, in chief part at least, the same that result from normal catabolism of food proteins. There is no evidence that the autolytic products play any part in causing the intoxication. The possibility of such a part and a resultant vicious circle is not excluded, but from the available facts the autolysis appears more as a result rather than cause of the intoxication. It appears possible that in disease or intoxication tissue catabolism may be enormously accelerated and yet yield the end-products of normal protein metabolism.

The Excretion of Isotope in Urea and Ammonia for Estimating Protein Turnover in Man with [15N]Glycine

1981 ◽  
Vol 61 (2) ◽  
pp. 217-228 ◽  
Author(s):  
E. B. Fern ◽  
P. J. Garlick ◽  
Margaret A. McNurlan ◽  
J. C. Waterlow
Keyword(s):  
Protein Metabolism ◽  
Protein Turnover ◽  
Mean Value ◽  
Intravenous Dose ◽  
Whole Body ◽  
Body Protein ◽  
End Products ◽  
The Mean ◽  
15N Urea ◽  
Normal Adults

1. Four normal adults were given [15N]-glycine in a single dose either orally or intravenously. Rates of whole-body protein turnover were estimated from the excretion of 15N in ammonia and in urea during the following 9 h. The rate derived from urea took account of the [15N]urea retained in body water. 2. In postabsorptive subjects the rates of protein synthesis given by ammonia were equal to those from urea, when the isotope was given orally, but lower when an intravenous dose was given. 3. In subjects receiving equal portions of food every 2 h rates of synthesis calculated from ammonia were much lower than those from urea whether an oral or intravenous isotope was given. Comparison of rates obtained during the post-absorptive and absorptive periods indicated regulation by food intake primarily of synthesis when measurements were made on urea, but regulation primarily of breakdown when measurements were made on ammonia. 4. These inconsistencies suggest that changes in protein metabolism might be assessed better by correlating results given by different end-products, and it is suggested that the mean value given by urea and ammonia will be useful for this purpose.

scholarly journals PROTEOSE INTOXICATIONS AND INJURY OF BODY PROTEIN

1918 ◽  
Vol 28 (2) ◽  
pp. 243-252
Author(s):  
J. V. Cooke ◽  
G. H. Whipple
Keyword(s):  
Intestinal Obstruction ◽  
Clinical Analysis ◽  
Abscess Formation ◽  
Protein Nitrogen ◽  
Urea Nitrogen ◽  
Body Protein ◽  
Acute Infections ◽  
Pathological Conditions ◽  
Septic Inflammation ◽  
Urinary Nitrogen

Sterile abscess formation in the dog is accompanied by a large increase in output of urinary nitrogen and also by a small but definite increase in the blood non-protein nitrogen. All this nitrogenous material of course is derived from body protein injury and autolysis. Septic inflammation in the dog (pleurisy, pneumonia, peritonitis, etc.) likewise shows a distinct rise in the blood non-protein nitrogen. This rise is not often so great as that frequently observed in the intoxication of intestinal obstruction. Many acute infections in man (septicemia, peritonitis, pneumonia, etc.) show a definite rise in the non-protein nitrogen and urea nitrogen of the blood; some cases show a very great rise above normal (over 100 mg. of non-protein nitrogen per 100 cc. of blood). There may be no anatomical change in the kidney beyond the familiar picture of cloudy swelling. This does not exclude the possibility of some transient functional derangement of the kidney epithelium. Certain obscure intoxications in man may show a considerable rise in the non-protein nitrogen of the blood, indicating a large amount of protein disintegration. These findings must be taken into account in any clinical analysis and interpretation of high non-protein nitrogen of the blood in pathological conditions.

A comparison of the estimates of whole-body protein turnover in parenterally fed neonates obtained using three different end products

1989 ◽  
Vol 67 (6) ◽  
pp. 624-628 ◽  
Author(s):  
P. Pencharz ◽  
J. Beesley ◽  
P. Sauer ◽  
J. Van Aerde ◽  
U. Canagarayar ◽  
...  
Keyword(s):  
Nitrogen Metabolism ◽  
Protein Metabolism ◽  
Protein Turnover ◽  
The Other ◽  
Whole Body ◽  
Turnover Rates ◽  
Body Protein ◽  
Future Studies ◽  
Simultaneous Measurements ◽  
End Products

Protein turnover rates in neonates have been calculated largely by measuring urinary [15N]urea enrichment following administration of [15N]glycine. Although ammonia has been increasingly recognized as an end product of nitrogen metabolism, in neonates it yields a different estimate of protein turnover than does urea. Comparisons of ammonia and urea end products in parenterally fed neonates have not previously been reported. A third and independent way of estimating protein turnover, developed for adults, is to use breath 13CO2 as an end product following administration of [1-3C]leucine. We therefore carried out simultaneous measurements of protein turnover in 10 parenterally fed neonates, using the three end products. The infants were clinically stable, weighed 2.6 ± 0.2 kg, and received 3.1 ± 0.2 g∙kg−1∙d−1 of amino acid, 2.2 ± 0.1 g∙kg−1∙d−1 of lipids, and an energy intake of 90 ± 4 kcal∙kg−1∙d−1 (1 kcal = 4.186 kJ). The turnover estimates derived from the 13CO2 and [15N]urea end products were very similar. The [15N]ammonia end product produced values approximately 66% (p < 0.01) of the other two. We conclude that the ammonia and urea end products probably originate in different precursor pools. The similarity of the urea and breath carbon dioxide results helps validate the use of the urea end product in studying the nitrogen metabolism of parenterally fed neonates. Ideally in future studies two or more end products should be used, since they provide information about different aspects of the nenonates' protein metabolism.Key words: neonates, protein metabolism, nitrogen-15, [1-13C]leucine.

622 Blood urea nitrogen — an important prognostic marker in patients with chronic heart failure

2006 ◽  
Vol 5 (1) ◽  
pp. 145-146
Author(s):  
M ROIK ◽  
M STARCZEWSKA ◽  
S STAWICKI ◽  
Z HUCZEK ◽  
J KOCHANOWSKI ◽  
...  
Keyword(s):  
Heart Failure ◽  
Chronic Heart Failure ◽  
Prognostic Marker ◽  
Blood Urea Nitrogen ◽  
Urea Nitrogen

Association between Blood Urea Nitrogen-to-creatinine Ratio and Three-Month Outcome in Patients with Acute Ischemic Stroke

2019 ◽  
Vol 16 (2) ◽  
pp. 166-172 ◽  
Author(s):  
Linghui Deng ◽  
Changyi Wang ◽  
Shi Qiu ◽  
Haiyang Bian ◽  
Lu Wang ◽  
...  
Keyword(s):  
Logistic Regression ◽  
Ischemic Stroke ◽  
Clinical Outcome ◽  
Acute Ischemic Stroke ◽  
Blood Urea Nitrogen ◽  
Univariate Analysis ◽  
Density Lipoprotein ◽  
Hydration Status ◽  
Creatinine Ratio ◽  
Urea Nitrogen

Background: Hydration status significantly affects the clinical outcome of acute ischemic stroke (AIS) patients. Blood urea nitrogen-to-creatinine ratio (BUN/Cr) is a biomarker of hydration status. However, it is not known whether there is a relationship between BUN/Cr and three-month outcome as assessed by the modified Rankin Scale (mRS) score in AIS patients. Methods: AIS patients admitted to West China Hospital from 2012 to 2016 were prospectively and consecutively enrolled and baseline data were collected. Poor clinical outcome was defined as three-month mRS > 2. Univariate and multivariate logistic regression analyses were performed to determine the relationship between BUN/Cr and three-month outcome. Confounding factors were identified by univariate analysis. Stratified logistic regression analysis was performed to identify effect modifiers. Results: A total of 1738 patients were included in the study. BUN/Cr showed a positive correlation with the three-month outcome (OR 1.02, 95% CI 1.00-1.03, p=0.04). However, after adjusting for potential confounders, the correlation was no longer significant (p=0.95). An interaction between BUN/Cr and high-density lipoprotein (HDL) was discovered (p=0.03), with a significant correlation between BUN/Cr and three-month outcome in patients with higher HDL (OR 1.03, 95% CI 1.00-1.07, p=0.04). Conclusion: Elevated BUN/Cr is associated with poor three-month outcome in AIS patients with high HDL levels.

Theaflavin Enriched Black Tea Extract Alleviates Diabetic Nephropathy by Suppressing Hyperglycaemia-Mediated Oxidative Stress and Inflammation in Streptozotocin-Induced Rats

2020 ◽  
Vol 10 ◽  
Author(s):  
Dhrubajyoti Sarkar ◽  
Sekhar Kumar Bose ◽  
Tania Chakraborty ◽  
Souvik Roy
Keyword(s):  
Oxidative Stress ◽  
Diabetic Nephropathy ◽  
Blood Glucose ◽  
Blood Urea Nitrogen ◽  
Phenolic Content ◽  
Black Tea ◽  
Total Phenolic ◽  
Urea Nitrogen ◽  
Black Tea Extract ◽  
Tea Extract

Background: Diabetic nephropathy (DN), a microvascular complication of diabetes has been a significant health issue globally. However, theaflavin enriched black tea extract (BTE-TF) could restrain DN. Objective: The main objective of this exploration was to elucidate the effect of BTE-TF on DN, though the underlying mechanism remains unclear and requires further investigation. Method: The tea leaves were fermented to get black tea extract. Total phenolic content and HPLC were carried out to determine the phenolic content and theaflavin in the extract. Streptozotocin induced diabetic rats were treated with 100, 200, and 400 mg/kg/day BTE-TF extract for 12 weeks. Biochemical parameters like blood glucose, creatinine, blood urea nitrogen (BUN), triglyceride and antioxidant parameters of kidney tissue were measured. Histology, immunohistochemistry and TUNEL assay were performed to observe the effect of the extract with comparison to the standard drug (Metformin 200mg/kg/day). Result: Treated animals exhibited reduced blood glucose levels, blood urea nitrogen (BUN), creatinine, and serum triglycerides. Further, BTE-TF restored the histological alterations in the kidney. Chronic hyperglycaemia resulted in a significant increase in oxidative stress and pro-inflammatory cytokines of NF-kβ pathway. BTE-TF attenuated oxidative stress (p<0.01), inflammation (p<0.05) and apoptosis (p<0.05). Conclusion: This study suggests that BTE-TF exerts a protective role against diabetes-induced renal injury by ameliorating oxidative stress, inflammation, and apoptosis.

scholarly journals Comprehensive assessment of post-prandial protein handling by the application of intrinsically labelled protein in vivo in human subjects

2021 ◽  
pp. 1-9
Author(s):  
Jorn Trommelen ◽  
Andrew M. Holwerda ◽  
Philippe J. M. Pinckaers ◽  
Luc J. C. van Loon
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Stable Isotope ◽  
Dietary Protein ◽  
Protein Metabolism ◽  
Muscle Protein ◽  
Human Subjects ◽  
Whole Body ◽  
Body Protein

All human tissues are in a constant state of remodelling, regulated by the balance between tissue protein synthesis and breakdown rates. It has been well-established that protein ingestion stimulates skeletal muscle and whole-body protein synthesis. Stable isotope-labelled amino acid methodologies are commonly applied to assess the various aspects of protein metabolism in vivo in human subjects. However, to achieve a more comprehensive assessment of post-prandial protein handling in vivo in human subjects, intravenous stable isotope-labelled amino acid infusions can be combined with the ingestion of intrinsically labelled protein and the collection of blood and muscle tissue samples. The combined application of ingesting intrinsically labelled protein with continuous intravenous stable isotope-labelled amino acid infusion allows the simultaneous assessment of protein digestion and amino acid absorption kinetics (e.g. release of dietary protein-derived amino acids into the circulation), whole-body protein metabolism (whole-body protein synthesis, breakdown and oxidation rates and net protein balance) and skeletal muscle metabolism (muscle protein fractional synthesis rates and dietary protein-derived amino acid incorporation into muscle protein). The purpose of this review is to provide an overview of the various aspects of post-prandial protein handling and metabolism with a focus on insights obtained from studies that have applied intrinsically labelled protein under a variety of conditions in different populations.

scholarly journals The energy equivalents of ATP and the energy values of food proteins and fats

1984 ◽  
Vol 51 (1) ◽  
pp. 15-28 ◽  
Author(s):  
Geoffrey Livesey
Keyword(s):  
Fatty Acid ◽  
Amino Acid ◽  
Oxidative Phosphorylation ◽  
G Protein ◽  
Compositional Data ◽  
Metabolizable Energy ◽  
Food Proteins ◽  
Protein Nitrogen ◽  
Food Composition Tables ◽  
Heats Of Combustion

1. Heats of combustion and energy equivalents of cytoplasmic ATP have been estimated for glucose, 101 food proteins and 116 food fats based on amino acid and fatty acid composition data from food composition tables and the heats of combustion and energy equivalents of cytoplasmic ATP of each individual amino acid, fatty acid, glycerol and glucose. The isodynamic equivalents of carbohydrate, fat and protein at the biochemical level have been investigated.2. Heats of combustion of food proteins and fats derived from compositional data were within 1 % of published values obtained by calorimetry.3. Cytoplasmic ATP equivalents for glucose, fat and protein range from 9·0 to 14·7, 8·6 to 14·6 and 6·4 to 13·2 mol cytoplasmic ATP/MJ of metabolizable energy respectively, depending on the choice of mitochondrial proton stoichiometries for these estimations. The range is extended further when considering the level and type of mitochondrial ‘uncoupling’.4. Isobioenergetic relationships between the efficiencies of glucose (G) and fat (F) (F = 1·05 G-0·9) and glucose and protein (P) (P = G(1·02–0·19f)-(1.8+0·5f)) energy conversions (wheref is the fraction of protein oxidized via gluconeogenesis) were obtained and were essentially independent of the choice of mitochondrial proton stoichiometry and the level and type of uncoupling of oxidative phosphorylation.5. Potential errors in previous estimates of ATP yield from protein are shown to be as much as -17·6 to < 118%; accounting for the efficiency of mitochondrial oxidative phosphorylation narrows this to between -7·9 and 17·4% and accounting for the fraction of protein oxidized via gluconeogenesis limits this further to between - 7·9 and 11·1%. Remaining uncertainty is attributed mostly to lack of knowledge about the energy cost of substrate absorption from the gut and transport across cell membranes.6. Coefficients of variation (cv) in the cytoplasmic ATP yield/g protein and /g protein nitrogen for the 101 food proteins were large (0·033 and 0·058 respectively). This is attributed mostly to variation in the metabolizable heats of combustion (cv 0·033 and 0·053 respectively) and to a much smaller extent in the efficiency with which cytoplasmic ATP equivalents are generated/MJ of metabolizable energy (cv 0·01).7. It is concluded that the current understanding of biochemical energy transduction is sufficient to permit only a crude estimate of the energy equivalents of cytoplasmic ATP but that these equivalents vary by less than 5% between both different food proteins and different food fats. Isobioenergetic equivalents for carbohydrates, fats and protein which could be applied to modify the Atwater conversion factors are possible but require first an accurate quantification of the energy equivalent of cytoplasmic ATP for glucose in vivo, and an indication that oxidative phosphorylation is similarly efficient in different individuals.

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