• 제목/요약/키워드: Amino acid transport

검색결과 130건 처리시간 0.033초

Effect of hyperthermia on cell viability, amino acid transfer, and milk protein synthesis in bovine mammary epithelial cells

  • Zhou, Jia;Yue, Shuangming;Xue, Benchu;Wang, Zhisheng;Wang, Lizhi;Peng, Quanhui;Hu, Rui;Xue, Bai
    • Journal of Animal Science and Technology
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    • 제64권1호
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    • pp.110-122
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    • 2022
  • The reduction of milk yield caused by heat stress in summer is the main condition restricting the economic benefits of dairy farms. To examine the impact of hyperthermia on bovine mammary epithelial (MAC-T) cells, we incubated the MAC-T cells at thermal-neutral (37℃, CON group) and hyperthermic (42℃, HS group) temperatures for 6 h. Subsequently, the cell viability and apoptotic rate of MAC-T cells, apoptosis-related genes expression, casein and amino acid transporter genes, and the expression of the apoptosis-related proteins were examined. Compared with the CON group, hyperthermia significantly decreased the cell viability (p < 0.05) and elevated the apoptotic rate (p < 0.05) of MAC-T cells. Moreover, the expression of heat shock protein (HSP)70, HSP90B1, Bcl-2-associated X protein (BAX), Caspase-9, and Caspase-3 genes was upregulated (p < 0.05). The expression of HSP70 and BAX (pro-apoptotic) proteins was upregulated (p < 0.05) while that of B-cell lymphoma (BCL)2 (antiapoptotic) protein was downregulated (p < 0.05) by hyperthermia. Decreased mRNA expression of mechanistic target of rapamycin (mTOR) signaling pathway-related genes, amino acid transporter genes (SLC7A5, SLC38A3, SLC38A2, and SLC38A9), and casein genes (CSNS1, CSN2, and CSN3) was found in the heat stress (HS) group (p < 0.05) in contrast with the CON group. These findings illustrated that hyperthermia promoted cell apoptosis and reduced the transport of amino acids into cells, which inhibited the milk proteins synthesis in MAC-T cells.

Dietary supplementation of Eucommia leaf extract to growing-finishing pigs alters muscle metabolism and improves meat quality

  • Zhenglei Shen;Chuxin Liu;Chuangye Deng;Qiuping Guo;Fengna Li;Qingwu W. Shen
    • Animal Bioscience
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    • 제37권4호
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    • pp.697-708
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    • 2024
  • Objective: The objective of this study was to investigate the influence of dietary supplementation of Eucommia ulmoides leaf extract (ELE) on muscle metabolism and meat quality of pigs with and without pre-slaughter transportation. Methods: In a 43-day feeding experiment, a total of 160 pigs with an initial body weight 60.00±2.00 kg were randomly assigned into four groups in a completely randomized design with 10 replicates. Pigs in groups A and C were fed a basal diet and pigs in groups B and D were fed a basal diet supplemented with 0.5% ELE. Pigs were slaughtered with (group B and D) or without (group A and C) pre-slaughter transport. Muscle chemical composition, postmortem glycolysis, meat quality and muscle metabolome were analyzed. Results: Dietary ELE supplementation had no effect on the proximate composition of porcine muscle, but increased free phenylalanine, proline, citruline, norvaline, and the total free amino acids in muscle. In addition, dietary ELE increased decanoic acid and eicosapentaenoic acid, but decreased heptadecanoic acid, oleic acid, trans-oleic acid, and monounsaturated fatty acids in muscle. Meat quality measurement demonstrated that ELE improved meat water holding capacity and eliminated the negative effects of pre-slaughter transport on meat cooking yield and tenderness. Dietary ELE reduced muscle glycolytic potential, inhibited glycolysis and muscle pH decline in the postmortem conversion of muscle to meat and increased the activity of citrate synthase in muscle. Metabolomics analysis by liquid chromatographic tandem mass spectrometric showed that ELE enhanced muscle energy level, regulated AMP-activated protein kinase (AMPK) signaling, modulated glycogenolysis/glycolysis, and altered the metabolism of carbohydrate, fatty acids, ketone bodies, amino acids, purine, and pyrimidine. Conclusion: Dietary ELE improved meat quality and alleviated the negative effect of pre-slaughter transport on meat quality by enhancing muscle oxidative metabolism capacity and inhibiting glycolysis in postmortem muscle, which is probably involved its regulation of AMPK.

구강 편평세포암종 KB세포에서 아미노산 수송억제제 BCH에 의한 세포성장 억제 (Induction of Growth Inhibition by BCH in KB Human Oral Epidermoid Carcinoma Cells)

  • 윤정훈;김윤배;김도경
    • 한국식품영양과학회지
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    • 제32권5호
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    • pp.758-763
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    • 2003
  • 구강 편평 세포암종 KB 세포를 이용하여 아미노산 수송계 L억제제인 BCH의 세포 성장억제에 미치는 효과를 밝히기 위해, KB세포에서 uptake실험, MTT분석 및 DNA frag-mentation분석 등을 시행하여 다음과 같은 결과를 얻었다. KB 세포에서는 아미노산 수송계 L 중에서 LAT1과 그 보조인자 4F2hc를 통해 BCH및 중성 아미노산들이 수송되었다. BCH는 시간과 농도에 의존적으로 KB세포의 성장을 억제시켰다. BCH를 처리한 실험군에서 DNA fragmentation 현상은 볼 수 없었다. 본 연구의 결과로서 구강암 세포주인 구강 편평세포암종 KB 세포에서 LAT1과 그 보조인자 4F2hc를 통해 BCH및 중성 아미노산의 수송이 이루어지고 있다는 것을 확인할 수 있었으며 BCH는 이 LAT1을 차단하여 중성 아미노산들의 세포 내 고갈을 유도함으로서 KB 세포 성장의 억제를 유도하는 것으로 사료된다.

Reabsorption of Neutral Amino Acids Mediated by Amino Acid Transporter LAT2 and TAT1 in The Basolateral Membrane of Proximal Tubule

  • Park Sun Young;Kim Jong-Keun;Kim In Jin;Choi Bong Kyu;Jung Kyu Yong;Lee Seoul;Park Kyung Jin;Chairoungdua Arthit;Kanai Yoshikatsu;Endou Hitoshi;Kim Do Kyung
    • Archives of Pharmacal Research
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    • 제28권4호
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    • pp.421-432
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    • 2005
  • In order to understand the renal reabsorption mechanism of neutral amino acids via amino acid transporters, we have isolated human L-type amino acid transporter 2 (hLAT2) and human T-type amino acid transporter 1 (hTAT1) in human, then, we have examined and compared the gene structures, the functional characterizations and the localization in human kidney. Northern blot analysis showed that hLAT2 mRNA was expressed at high levels in the heart, brain, placenta, kidney, spleen, prostate, testis, ovary, lymph node and the fetal liver. The hTAT1 mRNA was detected at high levels in the heart, placenta, liver, skeletal muscle, kidney, pancreas, spleen, thymus and prostate. Immunohistochemical analysis on the human kidney revealed that the hLAT2 and hTAT1 proteins coexist in the basolateral membrane of the renal proximal tubules. The hLAT2 transports all neutral amino acids and hTAT1 transports aromatic amino acids. The basolateral location of the hLAT2 and hTAT1 proteins in the renal proximal tubule as well as the amino acid transport activity of hLAT2 and hTAT1 suggests that these transporters contribute to the renal reabsorption of neutral and aromatic amino acids in the basolateral domain of epithelial proximal tubule cells, respectively. Therefore, LAT2 and TAT1 play essential roles in the reabsorption of neutral amino acids from the epithelial cells to the blood stream in the kidney. Because LAT2 and TAT1 are essential to the efficient absorption of neutral amino acids from the kidney, their defects might be involved in the pathogenesis of disorders caused by a disruption in amino acid absorption such as blue diaper syndrome.

INHIBITORY EFFECT OF THE IONOPHORE SALINOMYCIN ON DEAMINATION BY MIXED RUMEN BACTERIA

  • Kobayashi, Y.;Suda, K.;Wakita, M.;Baran, M.;Hoshino, S.
    • Asian-Australasian Journal of Animal Sciences
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    • 제9권1호
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    • pp.45-49
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    • 1996
  • A series of in vitro experiments was conducted to investigate response of rumen bacterial deamination to the ionophore salinomycin. Addition of salinomycin to the inoculum, strained rumen fluid, depressed ammonia production from casein, while increased accumulation of ${\alpha}$-amino acids. This suggests an inhibitory effect of salinomycin on ruminal deamination. When the effect in washed bacterial suspension was monitored with individual amino acid, aspartic acid degradation was markedly inhibited by salinomycin. This inhibition was not observed when the mixed rumen bacteria were ultrasonically disrupted and used as the enzyme source. Extent of the inhibition tended to be higher in the bacteria source from sheep on a high roughage diet. From these results it was speculated that the inhibition of deamination with salinomycin is caused by a decreased transport of amino acid into the bacterial cells as well as a decreased proportion of deaminating bacteria in the rumen.

Identification of Amino Acid Residues in the Carboxyl Terminus Required for Malonate-Responsive Transcriptional Regulation of MatR in Rhizobium leguminosarum bv. trifolii

  • Lee, Hwan-Young;Kim, Yu-Sam
    • BMB Reports
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    • 제34권4호
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    • pp.305-309
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    • 2001
  • MatR in Rhizobium trifolii is a malonate-responsive transcription factor that regulates the expression of genes, matABC, enabling decarboxylation of malonyl-CoA into acetyl-CoA, synthesis of malonyl-CoA from malonate and CoA, and malonate transport. According to an analysis of the amino acid sequence homology, MatR belongs to the GntR family The proteins of this family have two-domain folds, the N-terminal helix-turn-helix DNA-binding domain and the C-terminal ligand-binding domain. In order to End the malonate binding site and amino acid residues that interact with RNA polymerase, a site-directed mutagenesis was performed. Analysis of the mutant MatR suggests that Arg-160 might be involved in malonate binding, whereas Arg-102 and Arg-174 are critical for the repression activity by interacting with RNA polymerase.

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현탁배양 세포내에서 특수 중성 아미노산의 수송 (Transport System of Specific Neutral Amino Acids in Suspension-Cultured Cells)

  • Bong-Heuy CHO
    • 식물조직배양학회지
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    • 제21권4호
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    • pp.201-206
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    • 1994
  • Glycine, valine, alanine과 histidine의 수송은 모든 실험된 중성 아미노산에 의해 경쟁적인 방해를 당하였다.그리고 reciprocal 연구 결과로 이들 중성 아미노산들은 서로 carrier reciprocal의 활성부위를 점유하기위해 경쟁하므로 같은 운반자를 소유한다. Histidine은 전하를 띄우지 않은 상태로 중성 아미노산 운반자를 통해서 능동수송된다. 중성 운반자의 $K_m$ 값은 아미노산이 운반자에 대한 친화성에 따라서 3가지로 분류하였다. 0.1 mM 보다 작은 값, 0.1 mM에서 0.5 mM 사이에 있는 값고 0.5 mM 보다 큰 값이다. $V_{max}\;는\;3.12mol{\cdot}h^{-1}{\cdot}g{\;}fresh{\;}weight^{-1}\;과\;15.1\;{\mu}mole{\cdot}h^{-1}{\cdot}g{\;}fresh{\;}weight^{-1}$ 사이에 있다. 중성 아미노산은 아미노산 한개당 수소이온 한개가 동반수송되고, $K^{+}$ 한개가 전하보상을 위해서 배출된다. Histidine 분자도 1 분자당 1개의 수소이온과 동반수송되나 전하를 띄운 histidine 분자로부터 수소이온 한개가 배지로 떨어져 나오므로 동반수송된 수소이온의 움직임을 일시적으로 측정 할 수 없다.

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Effects of dietary spermine supplementation on cell cycle, apoptosis, and amino acid transporters of the thymus and spleen in piglets

  • Cao, Wei;Wu, Xianjian;Jia, Gang;Zhao, Hua;Chen, Xiaoling;Wu, Caimei;Cai, Jingyi;Wang, Jing;Liu, Guangmang
    • Asian-Australasian Journal of Animal Sciences
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    • 제31권8호
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    • pp.1325-1335
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    • 2018
  • Objective: This study investigated whether spermine supplementation could regulate cell cycle, apoptosis, and amino acid transporter-related genes expression in the thymus and spleen of early weaned piglets. Methods: Eighty female piglets were randomly distributed to receive adequate nutrients supplemented with spermine (0.4 mmol/kg body weight/24 h) or to be provided with restricted nourishment supplemented with normal saline for 7 h or 3, 6, or 9 d in pairs. Results: Regardless of administration time, spermine supplementation significantly up-regulated cyclin A2 gene expression but down-regulated p21 and cyclin D3 mRNA levels in the thymus and spleen and reduced cyclin E2 gene expression in the thymus of piglets (p<0.05). Irrespective of the treatment period, the reduced Bax and caspase-3 gene expressions and improved Bcl-2 mRNA level were observed in the thymus and spleen of spermine-administrated piglets (p<0.05). Regardless of supplementation time, spermine intake significantly enhanced the expressions of amino acid transporter-related genes (SLC1A1, SLC1A5, SLC7A1, SLC7A7, and SLC15A1) in both thymus and spleen, as well as SLC7A9 in the spleen of piglets (p<0.05). In addition, extended spermine administration also markedly promoted cell proliferation, depressed apoptosis and modulated amino acid transport (p<0.05), and such effects were the greatest during prolonged spermine supplementation (6 d) compared to the other time periods (p<0.05). Conclusion: Spermine supplementation may regulate cell cycle during the G1/S phase, suppress apoptosis and modulate amino acid transport. A period of 6 d of spermine supplementation is required to produce the optimal effects on nutritional implications.

Proteolytic System of Streptococcus thermophilus

  • Rodriguez-Serrano, G.M.;Garcia-Garibay, M.;Cruz-Guerrero, A.E.;Gomez-Ruiz, L.;Ayala-Nino, A.;Castaneda-Ovando, A.;Gonzalez-Olivares, L.G.
    • Journal of Microbiology and Biotechnology
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    • 제28권10호
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    • pp.1581-1588
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    • 2018
  • The growth of lactic acid bacteria (LAB) generates a high number of metabolites related to aromas and flavors in fermented dairy foods. These microbial proteases are involved in protein hydrolysis that produces necessary peptides for their growth and releases different molecules of interest, like bioactive peptides, during their activity. Each genus in particular has its own proteolytic system to hydrolyze the necessary proteins to meet its requirements. This review aims to highlight the differences between the proteolytic systems of Streptococcus thermophilus and other lactic acid bacteria (Lactococcus and Lactobacillus) since they are microorganisms that are frequently used in combination with other LAB in the elaboration of fermented dairy products. Based on genetic studies and in vitro and in vivo tests, the proteolytic system of Streptococcus thermophilus has been divided into three parts: 1) a serine proteinase linked to the cellular wall that is activated in the absence of glutamine and methionine; 2) the transport of peptides and oligopeptides, which are integrated in both the Dpp system and the Ami system, respectively; according to this, it is worth mentioning that the Ami system is able to transport peptides with up to 23 amino acids while the Opp system of Lactococcus or Lactobacillus transports chains with less than 13 amino acids; and finally, 3) peptide hydrolysis by intracellular peptidases, including a group of three exclusive of S. thermophilus capable of releasing either aromatic amino acids or peptides with aromatic amino acids.