• 제목/요약/키워드: arginine

검색결과 1,641건 처리시간 0.031초

Regulation of Pluripotency-related Genes and Differentiation in Mouse Embryonic Stem Cells by Direct Delivery of Cell-penetrating Peptide-conjugated CARM1 Recombinant Protein

  • Choi, Sara;Jo, Junghyun;Seol, Dong-Won;Cha, Soo Kyung;Lee, Jeoung Eun;Lee, Dong Ryul
    • 한국발생생물학회지:발생과생식
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    • 제17권1호
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    • pp.9-16
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    • 2013
  • Coactivator-associated arginine methyltransferase 1 (CARM1) is included in the protein arginine methyltransferase (PRMT) family, which methylates histone arginine residues through posttranslational modification. It has been proposed that CARM1 may up-regulate the expression of pluripotency-related genes through the alteration of the chromatin structure. Mouse embryonic stem cells (mESCs) are pluripotent and have the ability to self-renew. The cells are mainly used to study the genetic function of novel genes, because the cells facilitate the transmission of the manipulated genes into target mice. Since the up-regulated methylation levels of histone arginine residue lead to the maintenance of pluripotency in embryos and stem cells, it may be suggested that CARM1 overexpressing mESCs elevate the expression of pluripotency-related genes in reconstituted embryos for transgenic mice and may resist the differentiation into trophectoderm (TE). We constructed a fusion protein by connecting CARM1 and 7X-arginine (R7). As a cell-penetrating peptide (CPP), can translocate CARM1 protein into mESCs. CPP-CARM1 protein was detected in the nuclei of the mESCs after a treatment of 24 hours. Accordingly, the expression of pluripotency-related genes was up-regulated in CPP-CARM1-treated mESCs. In addition, CPP-CARM1-treated mESC-derived embryoid bodies (EBs) showed an elevated expression of pluripotency-related genes and delayed spontaneous differentiation. This result suggests that the treatment of recombinant CPP-CARM1 protein elevates the expression of pluripotency-related genes of mESCs by epigenetic modification, and this protein-delivery system could be used to modify embryonic fate in reconstituted embryos with mESCs.

Differential Effects of Nitric Oxide Synthase Inhibitors in Rats

  • Lee, Jun-Hee;Shin, Chang-Yell;Kang, Bong-Su;Jeong, Ji-Hoon;Choi, Kyeong-Bum;Min, Young-Sil;Kim, Jin-Hak;Huh, In-Hoi;Sohn, Uy-Dong
    • The Korean Journal of Physiology and Pharmacology
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    • 제4권2호
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    • pp.99-104
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    • 2000
  • We investigated the action of NOS inhibitors on NOS in rats. Both of nitric oxide synthase inhibitors, $N^G$-monomethyl-L-arginine $(L-NMMA,\;3\;{\mu}M)$ or $N^G$-nitro-L-arginine methylester $(L-NAME,\;30\;{\mu}M),$ augmented phenylephrine $(PE,\;10^{-7}\;M)-induced$ contraction which was inhibited by acetylcholine (ACh) in rat thoracic aorta. This augmentation by L-NAME or L-NMMA was attenuated with the treatment of NO precursor, arginine. ACh, however, decreased the augmentation induced by L-NMMA, but not by L-NAME. Superoxide dismutase (SOD, 50 u/ml) potentiated an inhibitory effect of ACh on the PE $(10^{-7}\;M)-induced$ contraction. It has been known that platelet activating factor itself induces iNOS. Platelet activating factor $(PAF,\;10^{-7}\;M)$ inhibited PE $(10^{-7}\;M)-induced$ contraction. Pretreatment with L-NMMA (30 mM) or L-NAME (30 mM) significantly blocked the inhibitory action of PAF on PE-induced contraction. L-NMMA (100 mM) or L-NAME (100 mM) reduced nerve conduction velocity (NCV) relevant to nNOS in rat sciatic nerve. ACh attenuated the reduction of NCV by L-NMMA-, but not by L-NAME-induced reduction of NCV. These results suggest that L-NMMA and/or L-NAME have different action on three types of NOS in rats.

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일부 아미노산과 식품 추출물의 에탄올 간독성에 대한 보호효과 (Protective Effect of Selected Amino Acids and Food Extracts on Ethanol Toxicity Decrement in Rat Liver)

  • 이자현;김낙경;이도연;이철호
    • 한국식품과학회지
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    • 제31권3호
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    • pp.802-808
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    • 1999
  • 본 실험에서는 aspartate, arginine, glutamate가 에탄올로 처리한 간세포에 대한 lipid peroxidation의 변화를 비교분석하고 예로부터 숙취제거 식품으로 잘 알려진 콩나물, 북어 및 영지버섯 추출액의 in vitro 실험을 통하여 에탄올로 처리된 간세포에 대한 lipid peroxidation 변화를 보았다. 또한 에탄올처리에 대한 숙취제거 식품의 처리순서에 따른 lipid peroxidation의 변화를 보았다. S9분획(간세포)에 에탄올(0.56 M)을 $50\;{\mu}L$씩 처리한 후 아미노산용액과 식품추출물을 6.25, 12.5, 25, 50 mg/mL 농도로 처리하였다. 이 실험의 결과는 다음과 같다. Aspartate, arginine, glutamate중 arginine이 가장 큰 간 보호 효과를 나타내었다. 콩나물, 북어, 영지의 단백질 함량은 콩나물이 $8.916\;{\mu}g/mL$으로 가장 많았다. 콩나물, 북어, 영지중에서 콩나물 추출물이 가장 큰 간 보호 효과를 나타내었다. 각각의 식품추출물을 에탄올 다음에 처리하였을 경우 전처리보다 간 보호 효과가 더욱 증가하는 경향을 나타내었다.

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Amino-Carbonyl 반응(反應)에 미치는 온도(溫度)의 영향(影響) (Effect of Temperature on Amino-Carbonyl Reaction)

  • 김용년;김창목;한강완;오성기
    • 한국식품영양과학회지
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    • 제11권1호
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    • pp.51-56
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    • 1982
  • 가공식품(加工食品)의 가장 중요(重要)한 색소형성(色素形成)으로 알려 진 비효소적(非酵素的) 갈변반응(褐變反應)인 amino-carbonyl반응(反應)에 대(對)한 온도(溫度)의 영향을 규명(究明)하기 위하여 0.05M glucose-arginine을 model system으로 선정하여 처리온도(處理溫度) 및 시간(時間)에 따라 분해(分解)되는 glucose 및 arginine의 함량변화(含量變化)와 생성(生成)되는 melanoidin 색소(色素)의 강도(强度)로써 반응속도상수(反應速度常數)와 반감기(半減期)를 구(求)하였으며, 또 Arrhenius 식(式)에 따라 반응속도상수(反應速度常數)의 온도의존성(溫度依存性)을 조사(調査)하였다. 1. 처리온도(處理溫度) 및 시간별(時間別)로 분해(分解)되는 glucose 및 arginine의 정량(定量)은 carbohydrate analysis 및 $\mu$ Bondapak $C_{18}$ column을 사용(使用)한 HPLC를 이용(利用)함이 효과적(效果的)이었다. 2. glucose 및 arginine의 분해반응(分解反應)은 $100^{\circ}C$$120^{\circ}C$에서의 glucose를 제외하고는 모두 1차반응(次反應)에 따랐으나, $100^{\circ}C$이상에서의 glucose에 있어서는 2상(相) 1차반응(次反應)(two-phase first-order reaction)에 따랐다. 또 melanoidin 생성반응(生成反應)에 있어서 $60^{\circ}C$$80^{\circ}C$에서는 1차반응(次反應)에 따랐으나 $100^{\circ}C$이상에서는 역시 2상(相) 1차반응(次反應)에 따랐다. 3. glucose-arginine 반응(反應)에 의한 melanoidin 색소(色素)의 생성반응(生成反應)은 $100^{\circ}C$$120^{\circ}C$에서 3$\sim$5시간(時間)동안에 거의 완성단계에 있었으며 $100^{\circ}C$이상에서는 거의 차(差)가 없었다. 4. glucose 및 arginine의 분해반응(分解反應)과 melanoidin의 생성반응(生成反應)의 속도상수(速度常數)가 $100^{\circ}C$$120^{\circ}C$에서 현저한 증가현상(增加現象)을 나타내므로 amino-carbonyl 반응(反應)에 의(依)한 갈색색소형성(褐色色素形成)은 $100^{\circ}C$이상의 고온에서 심하게 일어남을 알 수 있었다. 5. glucose 및 arginine의 분해반응(分解反應)과 이에 따른 melanoidin의 생성반응(生成反應)에 대(對)한 반응속도상수(反應速度常數)의 온도(溫度) 의존성(依存性)은 $100^{\circ}C$이하에서는 Arrhenius식(式)에 따랐으나 $120^{\circ}C$이상의 고온(高溫)에서는 이에 따르지 않았다. 6. glucose 및 arginine 분해반응(分解反應)의 활성화(活性化)에너지는 각각(各各) 12.512kcal/mole과 12.122kcal/mole로서 거의 비슷하고 melanoidin생성반응(生成反應)의 활성화(活性化)에너지는 18.142kcal/mole로서 melanoidin생성반응(生成反應)이 온도(溫度)에 더 민감함을 보여주었다.

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Optimum Conditions for the Formation of Ammonia as a Precursor of Tetramethylpyrazine by Lactococcus lactis ssp. lactis biovar. diacetilactis FC1

  • Kim, Kyoung-Heon
    • Journal of Microbiology and Biotechnology
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    • 제1권4호
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    • pp.281-284
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    • 1991
  • To investigate the optimum conditions for the production of ammonia as a precursor of tetramethylpyrazine flavor compound from arginine by Lactococcus lactis ssp. lactis biovar. diacetilactis FC1, fermentation factors such as initial pH of culture media, fermentation temperature, concentration of arginine-HC1, and sugars were examined. The optimum conditions were initial pH 5.5 of the culture media, fermentation temperature of $34^{\circ}C$, 6% (w/v) of arginine-HC1, and 1% (w/v) of galactose as a carbon source. Under the optimum fermentation conditions, 40 mmole/l of ammonia was produced after 40 h.

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Inhibition of Purine Nucleoside Phosphorylase (PNP) in Micrococcus luteus by Phenylglyoxal

  • Choi, Hye-Seon
    • Journal of Microbiology
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    • 제34권3호
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    • pp.270-273
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    • 1996
  • Micrococcus luteus purine nucleoside phosphorylase (PNP) has been purified and characterized. The physical and kinetic properties have been described previously. Chemical modification of the enzyme was attempted to gain insight on the active site. The enzyme was inactivated in a time-dependent manner by the arginine- specific modifying reagent phenylglyoxal. There was a linear relationship between the observed rate of inactivation and the phenylglyoxal concentration. At 30 $^{\circ}C$ the bimolecular rate constant for the modification was 0.015 $min^{-1}mM^{-1}$ in 50 mM $NaHCO_3$ buffer, pH 7.5. The plot of logk versus log phenylglyoxal concentration was a strainght line with a slope value of 0.9, indicating that modification of one arginine residue was needed to inactivate the enzyme. Preincubation with saturated solutions of substrates protected the enzyme from inhibition of phenylglyoxal, indicating that reactions with phenylglyoxal were directed at arginyl residues essential for the catalytic functioning of the enzyme.

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Analysis of Arginine, Glucose, Sucrose, and Polyethylene Glycols using a Wood Charcoal Matrix for MALDI-MS

  • Lee, Sun-Young;Kim, Jin-Hee;Yang, Hyo-Jik;Shin, Seong-Jae;Hong, Jang-Mi;Kim, Jeong-Kwon
    • Mass Spectrometry Letters
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    • 제1권1호
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    • pp.33-36
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    • 2010
  • Wood charcoal was investigated to determine its potential as an alternative matrix for matrix-assisted laser desorption/ionization of various samples. Wood charcoal was an effective matrix for analyzing glucose, sucrose, arginine, and polyethylene glycols (PEGs), with detection levels of 100 pmol for glucose, 1 nmol for sucrose, 100 pmol for arginine, 100 pmol for PEG 400, 1 pmol for PEG 1540, and 10 pmol for PEG 3350. No analyte signal was observed for peptides or proteins.

포유류 뇌의 미엘린 염기성 단백질에서 단백질-아르기닌 메칠화 (Protein-arginine methylation in myelin basic protein from mammalian brain)

  • 박종옥;박형숙;김경순
    • 생명과학회지
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    • 제8권1호
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    • pp.109-117
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    • 1998
  • The synthesis and methylation in vivo of myleline basic protein(MBP) during the mouse brain devlopment was found to be the highest in youngest brain and declined progressively in mature brains. The relative rate of protein synthesis and methylation was a maximal ration in the youngest brain, This high ratio was wdll correlated with the higher protein methylase I (PM I) activity in younger brains. The jimpy mouse is the most severely affected dysmyelinating mutant and is characterized by failure to incorporate MBP into myelin. sheath. The MBP-specific PM I activity in 15-, 18-, and 21-days old hemizygous jimpy mice(jp/y)brains decreased by 20, 50 and 75%, respectively. Myelin fraction with different degrees of compaction were isolated from bovine brain, the most compact myelin fraction exhibited higher methylaccepting activity than the less compact dense fractions.

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오수유가 N-nitro-L-arginine methyl ester로 유발한 고혈압흰쥐의 심혈관계에 미치는 영향 (Studies on the Effects of Evodiae Fructus on the Cardiovascular System in N-nitro-L-arginine Methyl Ester-induced Hypertensive Wistar Rats)

  • 정수연;이숙영;유태무;안미령;최현진;정면우;류항묵;양지선
    • 약학회지
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    • 제43권3호
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    • pp.397-403
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    • 1999
  • The present study examined the effect of a methanol extract of Evodiae Fructus on the cardiovascular function in N-nitro-L-arginine methyl ester (NAME)-induced hypertensive Wistar rats after treatment over 6 weeks. In rats treated with NAME, blood pressure, weight of heart, aorta media thickness and media/lumen ratio significantly (p<0.05) increased, whereas coronary flow and heart rate of isolated heart significantly (p<0.05) decreased compared with control group at 6 weeks. In rats treated with NAME and Evodiae Fructus, blood pressure, aorta media/lumen ratio significantly(p<0.05) decreased compared with NAME treated group at 6 weeks. These results suggest that Evodiae Fructus is applicable to the treatment of hypertension and vascular hypertrophy.

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Canavanine에 의한 보리 무배부 종자의 Amylase 활성과 단백질 함량의 변화 (Canavanine Effects on the Amylase Activity and Protein Content in Barley Half Seeds)

  • 전방욱
    • Journal of Plant Biology
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    • 제26권4호
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    • pp.173-180
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    • 1983
  • L-canavanine was added to GAs treated barley seeds, and induced amylase activity, soluble protein content, and arginine content were mesured. Canavanine, added at the beginning of the incubation period, inhibited amylase activity and protein accumulation. Amylase activity decreased markedly by addition of canavanine at 6 hr after incubation, where soluble protein content was not affected. The addition of canavanine after 12 hr incubation did not show serioud inhibited effect on the amylase activity and protein accumulation. GAs incubation caused decrement in arginine content per mg protein, but it was somewhat recovered by canavanine treatment. The longer the time between GAs and canavanine addition was, the less the recovery ration was. Arginine content in the $\alpha$-amylase fraction (ammonium sulfate 20~50% saturation) was lower than in 0~20% fraction, but higher than in 50~80% fraction. These results and control expreiments, using cordycepin and cycloheximide, support the idea that canavanine might incorporate into protein.

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