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RNA Profiles of the Korat Chicken Breast Muscle with Increased Carnosine Content Produced through Dietary Supplementation with β-Alanine or L-Histidine

ABSTRACT: RNA Profiles of the Korat Chicken Breast Muscle with Increased Carnosine Content Produced through Dietary Supplementation with β-Alanine or L-Histidine

PROVIDER: PRJNA744469 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR15058846_1.fastq.gz	Fastqsanger.gz
	SRR15058846_2.fastq.gz	Fastqsanger.gz
	SRR15058847_1.fastq.gz	Fastqsanger.gz
	SRR15058847_2.fastq.gz	Fastqsanger.gz
	SRR15058848_1.fastq.gz	Fastqsanger.gz

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RNA Profiles of the Korat Chicken Breast Muscle with Increased Carnosine Content Produced through Dietary Supplementation with β-Alanine or L-Histidine

Project description:Carnosine is a bioactive food component with several potential health benefits for humans due to its physiological functions. Dietary　supplementation with β-alanine or L-histidine can increase the carnosine content of skeletal muscles in chickens. Dietary supplementation with β-alanine or L-histidine has produced a slow-growing chicken variety　with high carnosine content in the breast meat; however, the　supplementation with L-histidine alone softens the meat toughness, which may affect consumers’ willingness to buy the meat. Gene　expression is a key factor that influences meat quality. Understanding the molecular mechanisms that affect carnosine content and meat toughness would allow the production of more value-added slow-growing chickens. We compared global gene expression in chicken breast muscles with differing carnosine contents and meat toughness produced through dietary supplementation with β-alanine or L-histidine. We identified differentially expressed genes involved in regulating myosin, collagen, intramuscular fat, and calpain—factors that may affect meat tenderness. Pathway enrichment analysis indicated that the insulin-related and adipocytokine signaling pathways were altered by dietary supplementation with β-alanine or L-histidine. These data will be useful for future studies on carnosine content and meat toughness in slow-growing chickens.

2021-09-04 | GSE179643 | GEO

RNA Profiles of the Korat Chicken Breast Muscle with Increased Carnosine Content Produced through Dietary Supplementation with β-Alanine or L-Histidine.

Project description:Korat chicken (KRC) is a slow-growing chicken bred in Thailand, whose meat exhibits a unique toughness. A previous study produced KRC breast meat containing high carnosine content through dietary supplementation with β-alanine or L-histidine; however, the KRC that were fed an L-histidine-supplemented diet produced meat that was significantly more tender. Herein, we performed RNA-Seq to identify candidate genes involved in the regulation of carnosine content and meat toughness. Total RNA was isolated from five female KRC breast muscles in each treatment group that KRC fed diets without supplementation, supplemented with β-alanine or L-histidine. Compared to the non-supplemented group, we identified 118 and 198 differentially expressed genes (DEGs) in the β-alanine or L-histidine supplementation groups, respectively. Genes potentially related to meat tenderness-i.e., those regulating myosin, collagen, intramuscular fat, and calpain-were upregulated (LOC107051274, ACSBG1, and CAPNS2) and downregulated (MYO7B, MYBPH, SERPINH1, and PGAM1). However, carnosine synthase gene was not identified. Functional enrichment analysis identified pathways affected by dietary supplementation, including the insulin signaling pathway (β-alanine supplementation) and the insulin resistance and adipocytokine signaling pathways (L-histidine supplementation). The FoxO signaling pathway was identified as a regulatory network for both supplementation groups. The identified genes can be used as molecular markers of meat tenderness in slow-growing chickens.

| S-EPMC8464878 | biostudies-literature

Studying the effects of endogenous and exogenous histidine supplementation on Pichia pastoris cultured in YPA

Project description:A histidine prototrophic strain achieves A600 three-four fold higher than a histidine auxotroph when cultured in nutrient rich media YPA, which is abundant in amino acids. This retaded growth of histidine auxotroph in YPA can also be rescued by supplementing media with exogenous histidine. Here, we aim to study the transcriptomic changes associated with culturing of histidine auxotroph and prototroph in YPA and also the effects of histidine addition to the culture medium of histidine auxotroph.

2022-04-06 | GSE174633 | GEO

Effect of d-alanine

Project description:Effect of d-alanine

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Effects of dietary supplementation with histidine and β-alanine on blood plasma metabolome of broiler chickens at different ages.

Project description:Histidine is an essential amino acid for broiler chickens and a precursor for the dipeptides carnosine and anserine, but little information is available about its metabolism in modern, fast-growing broilers. We used untargeted metabolomics to investigate the metabolic changes caused by the use of different standardized ileal digestible His:Lys ratios in broiler diets with and without β-alanine supplementation. A total of 2204 broilers were randomly divided into 96 pens of 23 birds each. The pens were divided into 16 blocks, each containing one pen for all six feeding groups (total of 16 pens per group). These feeding groups were fed three different His:Lys ratios (0.44, 0.54, and 0.64, respectively) without and with a combination of 0.5% β-alanine supplementation. Five randomly selected chickens of one single randomly selected pen per feeding group were slaughtered on day 35 or 54, blood was collected from the neck vessel, and plasma was used for untargeted metabolomic analysis. Here we show that up to 56.0% of all metabolites analyzed were altered by age, whereas only 1.8% of metabolites were affected by the His:Lys ratio in the diet, and 1.5% by β-alanine supplementation. Two-factor analysis and metabolic pathway analysis showed no interaction between the His:Lys ratio and β-alanine supplementation. The effect of the His:Lys ratio in the diet was limited to histidine metabolism with a greater change in formiminoglutamate concentration. Supplementation of β-alanine showed changes in metabolites of several metabolic pathways; increased concentrations of 3-aminoisobutyrate showed the only direct relationship to β-alanine metabolism. The supplementation of β-alanine indicated few effects on histidine metabolism. These results suggest that the supplements used had limited effects or interactions on both His and β-alanine metabolism. In contrast, the birds' age has the strongest influence on the metabolome.

| S-EPMC9662743 | biostudies-literature

WGS histidine overproducers

Project description:Whole genomes sequencing to determine mutations in histidine overproducers generated with a toxic histidine analog

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Histidine supplementation can escalate or rescue HARS deficiency in a Charcot Marie Tooth Disease model

Project description:Aminoacyl-tRNA synthetases (ARSs) are essential enzymes responsible for charging amino acids onto cognate tRNAs during protein synthesis¬. In histidyl-tRNA synthetase (HARS), autosomal dominant mutations in the HARS catalytic domain are associated with Charcot Marie Tooth Disease Type 2W (CMT2W), while anticodon-binding domain mutations cause Usher Syndrome Type IIIB (USH3B). We use yeast as a model system to study disease-causing HARS mutations (V133F, V155G, Y330C, S356N) associated with CMT2W, and Y454S, associated with USH3B. All human HARS variants complemented genomic deletion of the yeast ortholog HTS1 at high expression levels. CMT2W associated mutations, but not Y454S, result in reduced growth. HARS V155G and S356N cause accumulation of insoluble proteins and mistranslation in yeast, and the growth defect of these mutants was rescued by histidine addition to the growth media, restoring the soluble proteome. V133F and Y330C, on the other hand, lead to decreased HARS abundance. Histidine supplementation further reduced viability in yeast expressing V133F and Y330C, and lead to insoluble protein accumulation, indicating histidine toxicity associated with these mutants. Because histidine is in clinical trials as treatment for USH3B, our data will inform future treatment options for these as well as CMT patients, where histidine supplementation may either have a toxic or compensating effect dependingon the nature of the causative HARS variant.

2023-03-10 | PXD034865 | Pride

Carnosine effect in scaffold free human dermis spheroids model

Project description:Carnosine is an endogenous β-alanyl-L-histidine dipeptide endowed of antioxidant and carbonyl scavenger properties, able to significantly prevent the visible signs of aging and photoaging. To deeply investigate the mechanism of action of carnosine on human skin proteome, a 3D scaf-fold-free spheroids model of primary dermal fibroblasts from 50-years-old donor, was here adopted in combination with quantitative proteomics

2022-02-22 | PXD031053 | Pride

PrEC response to Alanine or Sarcosine at 6 hours

Project description:PrEC cells treated with either 50uM alanine or 50uM sarcosine (N-methylglycine). Gene expression is measured after 6 hours. We wish to look at the effects of sarcosine addition in relation to alanine addition. Keywords: Amino acid addition response

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Transcriptional response of Corynebacterium glutamicum C1 to 3 mM indole-alanine dipeptide

Project description:Differential gene expression analysis of C. glutamicum C1 in presence of 3 mM indole-alanine dipeptide compared to control conditions without indole-alanine dipeptide. C. glutamicum C1 cells were cultivated in CGXII minimal medium with 40 g per litre glucose in presence or absence of 3 mM indole-alanine dipeptide and harvested during exponential phase (o.d.600 6).

2020-12-31 | GSE159888 | GEO

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