scholarly journals Quantity as Well as Quality of Dietary Protein Affects Serine Dehydratase Gene Expression in Rat Liver

2003 ◽  
Vol 49 (1) ◽  
pp. 33-39 ◽  
Author(s):  
Saeko IMAM ◽  
Iyo YAGI ◽  
Tohru SAEKI ◽  
Makoto KOTARU ◽  
Kimikazu IWAMI
Keyword(s):  
Gene Expression ◽  
Rat Liver ◽  
Dietary Protein ◽  
Serine Dehydratase

Inverse Correlation between the Nitrogen Balance and Induction of Rat Liver Serine Dehydratase (SDH) by Dietary Protein

2004 ◽  
Vol 68 (4) ◽  
pp. 888-893 ◽  
Author(s):  
Ryuhei KANAMOTO ◽  
Kousuke FUJITA ◽  
Megumi KUMASAKI ◽  
Saeko IMAI ◽  
Makoto KOTARU ◽  
...  
Keyword(s):  
Rat Liver ◽  
Nitrogen Balance ◽  
Dietary Protein ◽  
Inverse Correlation ◽  
Serine Dehydratase

scholarly journals Response of the Induction of Rat Liver Serine Dehydratase to Changes in the Dietary Protein Requirement

2003 ◽  
Vol 67 (2) ◽  
pp. 383-387 ◽  
Author(s):  
Saeko IMAI ◽  
Ryuhei KANAMOTO ◽  
Iyo YAGI ◽  
Makoto KOTARU ◽  
Tohru SAEKI ◽  
...  
Keyword(s):  
Rat Liver ◽  
Dietary Protein ◽  
Protein Requirement ◽  
Serine Dehydratase

Effect of X-irradiation on gene expression of rat liver chemokines: in vivo and in vitro studies

2008 ◽  
Vol 46 (01) ◽  
Author(s):  
F Moriconi ◽  
H Christiansen ◽  
H Christiansen ◽  
N Sheikh ◽  
J Dudas ◽  
...  
Keyword(s):  
Gene Expression ◽  
Rat Liver ◽  
In Vitro Studies ◽  
X Irradiation

scholarly journals The impact of RNA extraction method on accurate RNA sequencing from formalin-fixed paraffin-embedded tissues

BMC Cancer ◽  
2019 ◽  
Vol 19 (1) ◽  
Author(s):  
Michal Marczyk ◽  
Chunxiao Fu ◽  
Rosanna Lau ◽  
Lili Du ◽  
Alexander J. Trevarton ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Gene Expression ◽  
Rna Sequencing ◽  
Rna Extraction ◽  
Formalin Fixed Paraffin ◽  
Ffpe Samples ◽  
Formalin Fixed Paraffin Embedded ◽  
The Impact ◽  
Formalin Fixed

Abstract Background Utilization of RNA sequencing methods to measure gene expression from archival formalin-fixed paraffin-embedded (FFPE) tumor samples in translational research and clinical trials requires reliable interpretation of the impact of pre-analytical variables on the data obtained, particularly the methods used to preserve samples and to purify RNA. Methods Matched tissue samples from 12 breast cancers were fresh frozen (FF) and preserved in RNAlater or fixed in formalin and processed as FFPE tissue. Total RNA was extracted and purified from FF samples using the Qiagen RNeasy kit, and in duplicate from FFPE tissue sections using three different kits (Norgen, Qiagen and Roche). All RNA samples underwent whole transcriptome RNA sequencing (wtRNAseq) and targeted RNA sequencing for 31 transcripts included in a signature of sensitivity to endocrine therapy. We assessed the effect of RNA extraction kit on the reliability of gene expression levels using linear mixed-effects model analysis, concordance correlation coefficient (CCC) and differential analysis. All protein-coding genes in the wtRNAseq and three gene expression signatures for breast cancer were assessed for concordance. Results Despite variable quality of the RNA extracted from FFPE samples by different kits, all had similar concordance of overall gene expression from wtRNAseq between matched FF and FFPE samples (median CCC 0.63–0.66) and between technical replicates (median expression difference 0.13–0.22). More than half of genes were differentially expressed between FF and FFPE, but with low fold change (median |LFC| 0.31–0.34). Two out of three breast cancer signatures studied were highly robust in all samples using any kit, whereas the third signature was similarly discordant irrespective of the kit used. The targeted RNAseq assay was concordant between FFPE and FF samples using any of the kits (CCC 0.91–0.96). Conclusions The selection of kit to purify RNA from FFPE did not influence the overall quality of results from wtRNAseq, thus variable reproducibility of gene signatures probably relates to the reliability of individual gene selected and possibly to the algorithm. Targeted RNAseq showed promising performance for clinical deployment of quantitative assays in breast cancer from FFPE samples, although numerical scores were not identical to those from wtRNAseq and would require calibration.

Dietary protein paradox: decrease of amino acid availability induced by high-protein diets

1993 ◽  
Vol 264 (6) ◽  
pp. G1057-G1065 ◽  
Author(s):  
C. Moundras ◽  
C. Remesy ◽  
C. Demigne
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Dietary Protein ◽  
High Protein ◽  
Glutamine Metabolism ◽  
Metabolic Adaptation ◽  
Casein Diet ◽  
Serine Dehydratase ◽  
High Protein Diets ◽  
Protein Diets

The aim of the present study was to evaluate the effect of changes in dietary protein level on overall availability of amino acids for tissues. For this purpose, rats were adapted to diets containing various concentrations of casein (7.5, 15, 30, and 60%) and were sampled either during the postprandial or postabsorptive period. In rats fed the protein-deficient diet, glucogenic amino acids (except threonine) tended to accumulate in plasma, liver, and muscles. In rats fed high-protein diets, the hepatic balance of glucogenic amino acids was markedly enhanced and their liver concentrations were consistently depressed. This response was the result of a marked induction of amino acid catabolism (a 45-fold increase of liver threonine-serine dehydratase activity was observed with the 60% casein diet). The muscle concentrations of threonine, serine, and glycine underwent changes parallel to plasma and liver concentrations, and a significant reduction of glutamine was observed. During the postabsorptive period, adaptation to high-protein diets resulted in a sustained catabolism of most glucogenic amino acids, which accentuated the drop in their concentrations (especially threonine) in all the compartments studied. The time course of metabolic adaptation from a 60 to a 15% casein diet has also been investigated. Adaptation of alanine and glutamine metabolism was rapid, whereas that of threonine, serine, and glycine was delayed and required 7-11 days. This was paralleled by a relatively slow decay of liver threonine-serine dehydratase (T-SDH) activity in contrast to the rapid adaptation of pyruvate kinase activity after refeeding a high-carbohydrate diet.(ABSTRACT TRUNCATED AT 250 WORDS)

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