O.71 Plasma insulin (IRI), branched-chain amino acids (BCAA) and the in vitro capacity of muscle and adipose tissue to metabolize bcaa in frequently used rat models

1983 ◽  
Vol 2 ◽  
pp. 38
Author(s):  
J.E.G. de Boer ◽  
P.B. Soeters ◽  
M.A. Janssen ◽  
R.J. Oostenbroek
Author(s):  
Moath Alqaraleh ◽  
Violet Kasabri ◽  
Ibrahim Al-Majali ◽  
Nihad Al-Othman ◽  
Nihad Al-Othman ◽  
...  

Background and aims: Branched chain amino acids (BCAAs) can be tightly connected to metabolism syndrome (MetS) which can be counted as a metabolic indicator in the case of insulin resistance (IR). The aim of this study was to assess the potential role of these acids under oxidative stress. Material and Methods: the in vitro antioxidant activity of BCAAs was assessed using free radical 1, 1-diphenyl-2-picryl-hydrazyl (DPPH) scavenging assays. For further check, a qRT-PCR technique was madefor detection the extent of alterations in gene expression of antioxidative enzymes (catalase and glutathione peroxidase (Gpx)) in lipopolysaccharides (LPS(-induced macrophages RAW 264.7 cell line. Additionally, BCAAs antioxidant activity was evaluated based on plasma H2O2 levels and xanthine oxidase (XO) activity in prooxidative LPS-treated mice. Results: Different concentrations of BCAAs affected on DPPH radical scavenging activity but to lesser extent than the ascorbic acid. Besides, BCAAs obviously upregulated the gene expression levels of catalases and Gpx in LPS-modulated macrophage RAW 264.7 cell line. In vivo BCAAs significantly minimized the level of plasma H2O2 as well as the activity of XO activity under oxidative stress. Conclusion: our current findings suggest that BCAAs supplementation may potentially serve as a therapeutic target for treatment of oxidative stress occurs with atherosclerosis, IR-diabetes, MetS and tumorigenesis.


1990 ◽  
Vol 73 (3A) ◽  
pp. NA-NA
Author(s):  
H. Yamada ◽  
Y. Ohta ◽  
I. Chaudhry ◽  
H. Nagashima ◽  
J. Askanazi ◽  
...  

2008 ◽  
Vol 190 (18) ◽  
pp. 6134-6147 ◽  
Author(s):  
Shigeo Tojo ◽  
Takenori Satomura ◽  
Kanako Kumamoto ◽  
Kazutake Hirooka ◽  
Yasutaro Fujita

ABSTRACT Branched-chain amino acids are the most abundant amino acids in proteins. The Bacillus subtilis ilv-leu operon is involved in the biosynthesis of branched-chain amino acids. This operon exhibits a RelA-dependent positive stringent response to amino acid starvation. We investigated this positive stringent response upon lysine starvation as well as decoyinine treatment. Deletion analysis involving various lacZ fusions revealed two molecular mechanisms underlying the positive stringent response of ilv-leu, i.e., CodY-dependent and -independent mechanisms. The former is most likely triggered by the decrease in the in vivo concentration of GTP upon lysine starvation, GTP being a corepressor of the CodY protein. So, the GTP decrease derepressed ilv-leu expression through detachment of the CodY protein from its cis elements upstream of the ilv-leu promoter. By means of base substitution and in vitro transcription analyses, the latter (CodY-independent) mechanism was found to comprise the modulation of the transcription initiation frequency, which likely depends on fluctuation of the in vivo RNA polymerase substrate concentrations after stringent treatment, and to involve at least the base species of adenine at the 5′ end of the ilv-leu transcript. As discussed, this mechanism is presumably distinct from that for B. subtilis rrn operons, which involves changes in the in vivo concentration of the initiating GTP.


1999 ◽  
Vol 181 (9) ◽  
pp. 2889-2894 ◽  
Author(s):  
Kunapuli T. Madhusudhan ◽  
Jinhe Luo ◽  
John R. Sokatch

ABSTRACT BkdR is the transcriptional activator of the bkdoperon, which encodes the four proteins of the branched-chain keto acid dehydrogenase multienzyme complex of Pseudomonas putida. In this study, hydroxyl radical footprinting revealed that BkdR bound to only one face of DNA over the same region identified in DNase I protection assays. Deletions of even a few bases in the 5′ region of the BkdR-binding site greatly reduced transcription, confirming that the entire protected region is necessary for transcription. In vitro transcription of the bkd operon was obtained by using a vector containing the bkdR-bkdA1 intergenic region plus the putative ρ-independent terminator of the bkdoperon. Substrate DNA, BkdR, and any of thel-branched-chain amino acids or d-leucine was required for transcription. Branched-chain keto acids,d-valine, and d-isoleucine did not promote transcription. Therefore, the l-branched-chain amino acids and d-leucine are the inducers of the bkdoperon. The concentration of l-valine required for half-maximal transcription was 2.8 mM, which is similar to that needed to cause half-maximal proteolysis due to a conformational change in BkdR. A model for transcriptional activation of the bkdoperon by BkdR during enzyme induction which incorporates these results is presented.


2011 ◽  
Vol 49 (No. 4) ◽  
pp. 137-143
Author(s):  
J. Antalíková ◽  
M. Baranovská ◽  
J. Jankela

We studied the influence of branched chain amino acids on the muscle proteosynthesis of Japanese quail during ontogenesis. We used in vitro incubation of these muscles: musculus extensor metacarpalis radialis (EMR) &ndash; wing muscle, musculus ambiens (MA) &ndash; leg muscle. The incorporation of <sup>14</sup>C-tyrosine into the individual protein fractions was evaluated. Influences of valine, leucine and isoleucine on proteosynthesis on day 14, 28 and 53 of life of Japanese quails were compared. Different patterns of individual protein fractions were detected. During ontogenesis, in the MA the number of fractions remained unchanged while in the EMR it differed. Four fractions with molecular weight 200&ndash;1 000 kDa present on day 14 and 28 were absent on day 53. A new fraction over 200 kDa was detected on day 53. The <sup>14</sup>C-tyrosine incorporation after leucine treatment was enhanced only in the MA of 28&nbsp;days old quails. The protein content in the EMR decreased (50%) in several fractions. The addition of valine had no effect in the MA while in the EMR the protein content decreased in 14 and 28 days old quails. The incorporation of <sup>14</sup>C-tyrosine was decreased by the influence of isoleucine in the EMR of 28 and 53 days old quails, in the MA only in 28 days old birds. We assume that the effect of regulatory amino acids on proteosynthesis depends both on muscle type and on the age of Japanese quail. &nbsp;


2016 ◽  
Vol 5 ◽  
Author(s):  
Annemarie Rietman ◽  
Takara L. Stanley ◽  
Clary Clish ◽  
Vamsi Mootha ◽  
Marco Mensink ◽  
...  

AbstractPlasma branched-chain amino acids (BCAA) are elevated in obesity and associated with increased cardiometabolic risk. β-Aminoisobutyric acid (B-AIBA), a recently identified small molecule metabolite, is associated with decreased cardiometabolic risk. Therefore, we investigated the association of BCAA and B-AIBA with each other and with detailed body composition parameters, including abdominal visceral adipose tissue (VAT) and subcutaneous adipose tissue (SAT). A cross-sectional study was carried out with lean (n 15) and obese (n 33) men and women. Detailed metabolic evaluations, including measures of body composition, insulin sensitivity and plasma metabolomics were completed. Plasma BCAA were higher (1·6 (se 0·08) (×107) v. 1·3 (se 0·06) (×107) arbitrary units; P = 0·005) in obese v. lean subjects. BCAA were positively associated with VAT (R 0·49; P = 0·0006) and trended to an association with SAT (R 0·29; P = 0·052). The association between BCAA and VAT, but not SAT, remained significant after controlling for age, sex and race on multivariate modelling (P < 0·05). BCAA were also associated with parameters of insulin sensitivity (Matsuda index: R −0·50, P = 0·0004; glucose AUC: R 0·53, P < 0·001). BCAA were not associated with B-AIBA (R −0·04; P = 0·79). B-AIBA was negatively associated with SAT (R −0·37; P = 0·01) but only trended to an association with VAT (R 0·27; P = 0·07). However, neither relationship remained significant after multivariate modelling (P > 0·05). Plasma B-AIBA was associated with parameters of insulin sensitivity (Matsuda index R 0·36, P = 0·01; glucose AUC: R −0·30, P = 0·04). Plasma BCAA levels were positively correlated with VAT and markers of insulin resistance. The results suggest a possible complex role of adipose tissue in BCAA homeostasis and insulin resistance.


1995 ◽  
Vol 145 (2) ◽  
pp. 315-323 ◽  
Author(s):  
J A Downing ◽  
J Joss ◽  
R J Scaramuzzi

Abstract The positive relationship between nutritional state and ovulation rate in sheep may involve the action of specific nutrients on gonadotrophin release. LH and FSH secretion is controlled in part by hypothalamic GnRH, which is in turn influenced by central adrenergic and serotonergic neuronal systems. In this experiment the branched chain amino acids (BCAAs) leucine, isoleucine and valine were examined for effects on LH and FSH secretion. A mixture of the three amino acids was infused into ewes for 5 days immediately before luteolysis, a time when nutritional effects on ovulation rate occur. The infusion significantly increased ovulation rate without any associated increase in FSH or LH. However, the infusion did increase plasma insulin concentrations and this effect, together with the high levels of blood urea observed, suggests that these amino acids had increased the supply of energy substrates to the follicles. An increase in insulin-mediated glucose uptake by follicles could be the stimulus responsible for the increase in ovulation rate. The ability of the animal to utilize BCAAs for energy metabolism may be an important component of the ovulation responses to nutrition. Journal of Endocrinology (1995) 145, 315–323


2018 ◽  
Vol 115 (25) ◽  
pp. 6446-6451 ◽  
Author(s):  
Mingxu Fang ◽  
Carl E. Bauer

When faced with amino acid starvation, prokaryotic cells induce a stringent response that modulates their physiology. The stringent response is manifested by production of signaling molecules guanosine 5′-diphosphate,3′-diphosphate (ppGpp) and guanosine 5′-triphosphate,3′-diphosphate (pppGpp) that are also called alarmones. In many species, alarmone levels are regulated by a multidomain bifunctional alarmone synthetase/hydrolase called Rel. In this enzyme, there is an ACT domain at the carboxyl region that has an unknown function; however, similar ACT domains are present in other enzymes that have roles in controlling amino acid metabolism. In many cases, these other ACT domains have been shown to allosterically regulate enzyme activity through the binding of amino acids. Here, we show that the ACT domain present in theRhodobacter capsulatusRel alarmone synthetase/hydrolase binds branched-chain amino acids valine and isoleucine. We further show that the binding of these amino acids stimulates alarmone hydrolase activity both in vitro and in vivo. Furthermore, we found that the ACT domain present in Rel proteins from many diverse species also binds branched-chain amino acids. These results indicate that the cellular concentration of amino acids can directly affect Rel alarmone synthetase/hydrolase activity, thus adding another layer of control to current models of cellular control of the stringent response.


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