scholarly journals Alterations and Association of Fecal Microbiota and Amino Acids in Parkinson's Patients

2020 ◽  
Author(s):  
Zhenzhen Yan ◽  
Fan Yang ◽  
Jingwei Cao ◽  
Wencai Ding ◽  
Shi Yan ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Intestinal Microbiota ◽  
Adaptive Immune Response ◽  
Fecal Microbiota ◽  
Adaptive Immune ◽  
Severe Motor ◽  
Stool Samples ◽  
Amino Acid Concentrations

Abstract Background: Intestinal microbiota and amino acids that are one of their metabolites play important roles in the mechanism of pathology of Parkinson's disease (PD). It has been reported that the level of amino acids in vivo participate in neurodegeneration by regulating adaptive immune response, while the current researches on alteration of amino acids in intestinal microbiota are still insufficient. Here, we evaluate the correlation between gut microbiota alterations and clinical parameters of PD, amino acid concentrations.Methods: Stool samples from PD and healthy controls were collected for microbiome and targeted metabolome analyses. Results: At the genus level, there was a greater abundance of Rikenellaceae_RC9_gut_group in PD patients with more severe motor symptoms. Metabonomics analysis showed that multiple fecal amino acid concentrations in PD patients were decreased. Moreover, the findings that by spearman analysis Rikenellaceae_RC9_gut_group associated with PD had a significantly negative correlation with phenylalanine (r = -0.488, P < 0.01), tyrosine (r = -0.541, P < 0.01) and isoleucine (r = -0.434, P < 0.01). Conclusions: Our results not only find Rikenellaceae_RC9_gut_group, a new pro-inflammatory genus of intestinal microbiota in PD, but also reveal that it's related to amino acids. These findings are beneficial to identifying microbial therapeutic targets for PD.

On the Role of Branched-Chain Amino Acids in Protein Turnover of Skeletal Muscle. Studies in vivo with L-Norleucine

1985 ◽  
Vol 40 (5-6) ◽  
pp. 427-437 ◽  
Author(s):  
Klaus-Joachim Schott ◽  
Jochen Gehrmann ◽  
Ulla Potter ◽  
Volker Neuhoff
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Small Intestine ◽  
Amino Acid ◽  
Protein Metabolism ◽  
Protein Turnover ◽  
Protein Concentration ◽  
Amino Acid Concentrations

Abstract 1. The effect of ʟ-norleucine, an isomer of leucine, on protein metabolism in vivo was studied in suckling rats. Rats were injected subcutaneously with various doses of ʟ-norleucine (0.5 and 5.0 μmol/g body wt.) every 12 h from 3 to 15 days post partum. Protein concentration, amino acid concentrations, and incorporation of [3H]tyrosine into protein were analyzed in liver, muscles of thigh and small intestine. Amino acid concentrations and insulin levels in serum were also measured. 2. At 5 days of age, norleucine induced an increase in protein concentration of skeletal muscle with an increased incorporation of [3H]tyrosine into protein indicating an accelerated protein synthesis. Changes in protein metabolism were paralleled by alterations in the amino acid pattern of this tissue. 3. When protein concentration and protein synthesis were increased in skeletal muscle, protein concentration of small intestine was decreased, accompanied by elevated levels of amino acids in tissue. Protein synthesis of small intestine was not altered by the norleucine treatment. The results suggest a close interrelationship between skeletal muscle and small intestine with respect to protein turnover. 4. The effects of norleucine were less pronounced at 10 and 15 days of age, which indicates a metabolic adaptation to the treatment. 5. Alterations in amino acid concentrations of tissue due to changes in protein metabolism were not uniform but tissue-specific. 6. Current concepts for explaining the effects of branched-chain amino acids (BCAA) on protein turnover in skeletal muscle are based on the assumption that the BCAA or leucine alone might become rate-limiting for protein synthesis in muscle under catabolic conditions. The amino acid analogue norleucine, however, cannot replace any of the BCAA in protein. Additionally, norleucine affected protein metabolism in highly anabolic organisms. Therefore, the present thoughts on this issue appear to be incomplete.

scholarly journals Nutritional aspects of amino acid metabolism

1972 ◽  
Vol 27 (2) ◽  
pp. 233-247 ◽  
Author(s):  
D. L. Bloxam
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Essential Amino Acids ◽  
Blood Levels ◽  
Low Protein ◽  
Extrahepatic Tissues ◽  
D Values ◽  
Liver Changes ◽  
Amino Acid Concentrations

1. Concentrations of the amino acids in the plasma of blood from the portal vein and hepatic vein and in the liver of fed rats and rats starved for 1 d or 3 d were measured. The 1 d values were compared with the equilibrium concentrations of the amino acids found in the perfusion medium during perfusion of livers from rats starved for 1 d.2. The measurements of portal–venous differences in amino acid concentrations confirmed the idea that postprandially and during starvation most of the amino acids flow from extrahepatic tissues to the liver but also showed that during starvation tryptophan, cystine, ornithine, valine, leucinc and isoleucine flow in the opposite direction, from liver to extrahepatic tissues.3. The blood levels of the non-essential amino acids fell markedly during starvation while those of the essential ones tended to be maintained. This contrasts with the pattern of changes known to take place in rats and man given low-protein diets. In the liver, changes in amino acid concentrations were generally related to those in the blood but not strictly parallel. The relative changes in amino acid concentrations in blood and liver indicate that as starvation progresses the concentrative ability of the liver is enhanced for most of the amino acids which are taken up and that the increased output of those which are released is also due to changed membrane transport.4. The changes in plasma amino acid concentrations in the blood passing through livers of rats starved for 1 d were, except for tryptophan and perhaps cystine, consistent with the extracellular changes found during perfusion of livers form rats straved for 1 d, indicating that the perfused liver influences concentrations of extracellular amino acids substantially as it does in vivo.5. The results suggest of mechanism wherby the liver may control the maintenance of the essential amino acids during starvation.

scholarly journals Primary structure requirements for correct sorting of the yeast mitochondrial protein ADH III to the yeast mitochondrial matrix space.

1987 ◽  
Vol 7 (1) ◽  
pp. 294-304 ◽  
Author(s):  
D Pilgrim ◽  
E T Young
Keyword(s):  
Amino Acids ◽  
Enzyme Activity ◽  
Amino Acid ◽  
Proteolytic Processing ◽  
Mitochondrial Matrix ◽  
Wild Type ◽  
Mature Form ◽  
Amino Terminal ◽  
The Matrix

Alcohol dehydrogenase isoenzyme III (ADH III) in Saccharomyces cerevisiae, the product of the ADH3 gene, is located in the mitochondrial matrix. The ADH III protein was synthesized as a larger precursor in vitro when the gene was transcribed with the SP6 promoter and translated with a reticulocyte lysate. A precursor of the same size was detected when radioactively pulse-labeled proteins were immunoprecipitated with anti-ADH antibody. This precursor was rapidly processed to the mature form in vivo with a half-time of less than 3 min. The processing was blocked if the mitochondria were uncoupled with carbonyl cyanide m-chlorophenylhydrazone. Mutant enzymes in which only the amino-terminal 14 or 16 amino acids of the presequence were retained were correctly targeted and imported into the matrix. A mutant enzyme that was missing the amino-terminal 17 amino acids of the presequence produced an active enzyme, but the majority of the enzyme activity remained in the cytoplasmic compartment on cellular fractionation. Random amino acid changes were produced in the wild-type presequence by bisulfite mutagenesis of the ADH3 gene. The resulting ADH III protein was targeted to the mitochondria and imported into the matrix in all of the mutants tested, as judged by enzyme activity. Mutants containing amino acid changes in the carboxyl-proximal half of the ADH3 presequence were imported and processed to the mature form at a slower rate than the wild type, as judged by pulse-chase studies in vivo. The unprocessed precursor appeared to be unstable in vivo. It was concluded that only a small portion of the presequence contains the necessary information for correct targeting and import. Furthermore, the information for correct proteolytic processing of the presequence appears to be distinct from the targeting information and may involve secondary structure information in the presequence.

scholarly journals BIOSYNTHESIS IN ISOLATED ACETABULARIA CHLOROPLASTS

1972 ◽  
Vol 54 (2) ◽  
pp. 279-294 ◽  
Author(s):  
David C. Shephard ◽  
Wendy B. Levin
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Technical Problems ◽  
Hydrolyzed Protein ◽  
Protein Amino Acids ◽  
Amino Acid Labeling ◽  
Labeling Pattern

The ability of chloroplasts isolated from Acetabulana mediterranea to synthesize the protein amino acids has been investigated. When this chloroplast isolate was presented with 14CO2 for periods of 6–8 hr, tracer was found in essentially all amino acid species of their hydrolyzed protein Phenylalanine labeling was not detected, probably due to technical problems, and hydroxyproline labeling was not tested for The incorporation of 14CO2 into the amino acids is driven by light and, as indicated by the amount of radioactivity lost during ninhydrin decarboxylation on the chromatograms, the amino acids appear to be uniformly labeled. The amino acid labeling pattern of the isolate is similar to that found in plastids labeled with 14CO2 in vivo. The chloroplast isolate did not utilize detectable amounts of externally supplied amino acids in light or, with added adenosine triphosphate (ATP), in darkness. It is concluded that these chloroplasts are a tight cytoplasmic compartment that is independent in supplying the amino acids used for its own protein synthesis. These results are discussed in terms of the role of contaminants in the observed synthesis, the "normalcy" of Acetabularia chloroplasts, the synthetic pathways for amino acids in plastids, and the implications of these observations for cell compartmentation and chloroplast autonomy.

scholarly journals Regulation of rat magnocellular neurosecretory system by D-aspartate: evidence for biological role(s) of a naturally occurring free D-amino acid in mammals

2000 ◽  
Vol 167 (2) ◽  
pp. 247-252 ◽  
Author(s):  
H Wang ◽  
H Wolosker ◽  
J Pevsner ◽  
SH Snyder ◽  
DJ Selkoe
Keyword(s):  
Gene Expression ◽  
Amino Acids ◽  
Amino Acid ◽  
Physiological Function ◽  
Neurosecretory System ◽  
Milk Ejection ◽  
Magnocellular Neurons ◽  
Rat Hypothalamus ◽  
Naturally Occurring

Little evidence is available for the physiological function of D-amino acids in species other than bacteria. Here we demonstrate that naturally occurring freed -aspartate (D-Asp) is present in all magnocellular neurons of rat hypothalamus. The levels of this naturally occurring D-amino acid were elevated during lactation and returned to normal thereafter in the magnocellular neurosecretory system, which produces oxytocin, a hormone responsible for milk ejection during lactation. Intraperitoneal injections of D-Asp reproducibly increased oxytocin gene expression and decreased the concentration of circulating oxytocin in vivo. Similar changes were observed in the vasopressin system. These results provide evidence for the role(s) of naturally occurring free D-Asp in mammalian physiology. The findings argue against the conventional concept that only L-stereoisomers of amino acids are functional in higher species.

Effect of Cycloheximide on In Vitro and In Vivo Protein Synthesis by Certain Tissues of Rats and Pigeons with Special Reference to Muscle

1973 ◽  
Vol 51 (12) ◽  
pp. 933-941 ◽  
Author(s):  
Njanoor Narayanan ◽  
Jacob Eapen
Keyword(s):  
Amino Acids ◽  
Body Weight ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Incorporation ◽  
Contrast Administration ◽  
Acid Incorporation ◽  
Tissue Homogenates

The effect of cycloheximide in vitro and in vivo on the incorporation of labelled amino acids into protein by muscles, liver, kidneys, and brain of rats and pigeons was studied. In vitro incorporation of amino acids into protein by muscle microsomes, myofibrils, and myofibrillar ribosomes was not affected by cycloheximide. In contrast, administration of the antibiotic into intact animals at a concentration of 1 mg/kg body weight resulted in considerable inhibition of amino acid incorporation into protein by muscles, liver, kidneys, and brain. This inhibition was observed in all the subcellular fractions of these tissues during a period of 10–40 min after the administration of the precursor. Tissue homogenates derived from in vivo cycloheximide-treated animals did not show significant alteration in in vitro amino acid incorporation with the exception of brain, which showed a small but significant enhancement.

In vivo metabolizable branched poly(ester amide) based on inositol and amino acids as drug nanocarrier for cancer therapy

2021 ◽  
Author(s):  
Jun Wu ◽  
Qi-Juan Yuan ◽  
Li Wang ◽  
Jun Huang ◽  
Wei Zhao
Keyword(s):  
Mechanical Property ◽  
Amino Acids ◽  
Amino Acid ◽  
Cancer Therapy ◽  
Biomedical Applications ◽  
Bioactive Components ◽  
Good Biocompatibility

Amino acid-based poly(ester amide) (PEA) has been utilized for various biomedical applications for its tunable mechanical property, good biocompatibility, and biodegradability. However, bioactive components have rarely been incorporated into the...

Potential differences influence amino acid/Na+ symport rates in larval Manduca sexta midgut brush-border membrane vesicles.

1994 ◽  
Vol 189 (1) ◽  
pp. 55-67
Author(s):  
R Parthasarathy ◽  
W R Harvey
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Manduca Sexta ◽  
Brush Border ◽  
Brush Border Membrane ◽  
Membrane Vesicles ◽  
Brush Border Membrane Vesicles ◽  
Rate Determining Step ◽  
Half Saturation Constant

The time-dependent fluorescence intensity of an intravesicular potential-sensitive dye was used to probe the real-time kinetics of potential difference (PD)-dependent amino acid/Na+ symport at pH9 into brush-border membrane vesicles obtained from larval Manduca sexta midgut. Neutral amino acids (alanine, proline) are symported at higher rates as the vesicles are hyperpolarized. The symport rates of acidic (glutamate) and basic (arginine) amino acids are almost PD-independent. The half-saturation constant of alanine is PD-independent between -108 and -78 mV, although the maximal symport velocity increases by half as the voltage is increased. Amino acid throughput is evidently enhanced as the relatively high transmembrane PDs (&gt; 150 mV, lumen positive) measured in vivo are approached. The half-saturation concentrations of Na+ were in the range 15-40 mmol l-1 for most of the amino acids examined and increased with voltage for alanine. The Vmax observed as a function of cation or amino acid concentration increased as the vesicle was hyperpolarized in the case of leucine and alanine. The data support the hypothesis that carrier and substrates are at equilibrium inasmuch as substrate translocation seems to be the rate-determining step of symport.

scholarly journals Rabbit Carcasses for Use in Feline Diets: Amino Acid Concentrations in Fresh and Frozen Carcasses With and Without Gastrointestinal Tracts

2021 ◽  
Vol 7 ◽  
Author(s):  
Tammy J. Owens ◽  
Andrea J. Fascetti ◽  
C. Christopher Calvert ◽  
Jennifer A. Larsen
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Crude Protein ◽  
Protein Body ◽  
National Research Council ◽  
Body Water ◽  
Taurine Supplementation ◽  
Frozen Ground ◽  
Taurine Deficiency ◽  
Amino Acid Concentrations

Whole-prey diets for exotic feline species are common, and this practice has also increased in popularity for domestic cats. However, prior analyses of prey indicate possible essential amino acid inadequacy, and dilated cardiomyopathy from taurine deficiency was reported in cats fed whole ground rabbit. Crude protein, body water, and amino acid concentrations were evaluated in fresh and frozen ground rabbits with (n=10) or without (n = 10) gastrointestinal tracts. Amino acids were greater in fresh samples without gastrointestinal tracts (p &lt; 0.05) except taurine, glycine, and cysteine. When normalized for protein content, only glutamate, alanine, methionine, isoleucine, tyrosine, lysine, histidine, and arginine were greater in fresh rabbits without gastrointestinal tracts (g/16 g N basis; p &lt; 0.05). Freezing at −18°C for 30 days had no effect on crude protein or body water content. After freezing, only methionine was lower and only proline was higher when gastrointestinal tracts were omitted (g/16 g N basis; p &lt; 0.05). Regardless, all essential amino acids except taurine exceeded Association of American Feed Control Officials and National Research Council nutrient recommendations for all feline life stages. In contrast, there was minimal impact of treatment on taurine concentrations. However, although feline taurine requirements for prey and other raw or fresh food diets remain undefined, none of the rabbit samples met any recommendation for taurine concentrations for commercial canned or dry extruded diets, ranging from 20 to 90% of the minimum values. Taurine supplementation is recommended when feeding rabbit to cats. Determination of taurine requirements of cats fed whole-prey diets is warranted.

Sign in / Sign up

Export Citation Format

Share Document