• Title/Summary/Keyword: Regulation of Protein Synthesis

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Cissus quadrangularis Extracts Decreases Body Fat Through Regulation of Fatty acid Synthesis in High-fat Diet-induced Obese Mice

  • Lee, Hae Jin;Lee, Dong-Ryung;Choi, Bong-Keun;Park, Sung-Bum;Jin, Ying-Yu;Yang, Seung Hwan;Suh, Joo-Won
    • Journal of Applied Biological Chemistry
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    • v.59 no.1
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    • pp.49-56
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    • 2016
  • The current study investigated the anti-obesity effect of Cissus quadrangularsis extracts (CQR-300) and its molecular action mechanism on obese mice induced high-fat diet (HFD). To induce the obesity, mice were fed a HFD for 6 weeks and then fed HFD only or HFD with CQR-300 at 50 and 200 mg/kg. Then, body weight gain and white adipose tissue weights were measured. We investigated the reduction in body fat and the regulation of fatty acid synthesis was measured by dual energy X-ray absorptiometry and real-time PCR with Western blot, respectively. In vitro study, CQR-300 inhibited pancreatic lipase activity. The CQR-300 treatment was significantly decreased the body weight gain and adipocytes size as well as white adipose tissues weights in HFD-induced obese mice. Furthermore, CQR-300 reduced the body fat and fat mass with regulating of adipose tissue hormones as leptin. Treatment with 50 mg/kg CQR-300 showed effectively lower expression levels of adipogenesis/lipogenesis related genes and proteins such as CCAAT/enhancer binding protein ${\alpha}$ ($C/EBP{\alpha}$), peroxisome proliferator-activated receptor ${\gamma}$ ($PPAR{\gamma}$), Sterol regulatory element binding protein-1c (SREBP-1c), and fatty acid synthase (FAS) in white adipose tissue (WAT) as compared with the HFD fed only mice. These results suggest that the CQR-300 has an anti-obesity effect via inhibition of lipase activity, decrease the body fat mass by regulating the adipogenesis and lipogenesis related genes and proteins in epididymal adipose tissue with evaluate body fat reduce in the HFD-induced obese mice.

Whitening Efficacy of Water Soluble Royal Jelly Removed Allergenic Protein (알러지 유발 단백질이 제거된 수용성 로열젤리의 피부미백 효과)

  • Han, Sang Mi;Kim, Jung Min;Kim, Se Gun;Jang, Hye Ri;Yeo, Joo Hong;Hong, In Pyo;Woo, Soon Ok
    • Korean Journal of Pharmacognosy
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    • v.45 no.3
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    • pp.262-267
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    • 2014
  • Royal jelly composes of many components, especially protein. Protein is a major factor which cause allergy. We focused on water soluble royal jelly (WSRJ) that was removed allergy - inducing protein. 10-hyroxy-2-decenoic acid content of WSRJ is 2.42 g/100 g, which is double compared to that of lypophilized RJ. To further access WSRJ as a cosmetic ingredient and potential external treatment for topical use, we investigated its ability to inhibit tyrosinase activity and melanin biosynthesis on melanogenesis in B16F1 melanoma cells. We found that WSRJ increased the cell viability in B16F1 melanoma cell and WSRJ (1~10 mg/ml) inhibited melanin synthesis in with 10 nM ${\alpha}$-melanocyte-stimulating hormone (${\alpha}$-MSH) for 48 h. WSRJ inhibited direct tyrosinase activity, which decreased melanin synthesis in ${\alpha}$-MSH stimulated B16F1 melanoma cells. Thease findings suggest that WSRJ induces the down regulation of melanogenesis by inhibiting tyrosinase activation.

Construction of a High-Quality Yeast Two-Hybrid Library and Its Application in Identification of Interacting Proteins with Brn1 in Curvularia lunata

  • Gao, Jin-Xin;Jing, Jing;Yu, Chuan-Jin;Chen, Jie
    • The Plant Pathology Journal
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    • v.31 no.2
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    • pp.108-114
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    • 2015
  • Curvularia lunata is an important maize foliar fungal pathogen that distributes widely in maize growing area in China, and several key pathogenic factors have been isolated. An yeast two-hybrid (Y2H) library is a very useful platform to further unravel novel pathogenic factors in C. lunata. To construct a high-quality full length-expression cDNA library from the C. lunata for application to pathogenesis-related protein-protein interaction screening, total RNA was extracted. The SMART (Switching Mechanism At 5' end of the RNA Transcript) technique was used for cDNA synthesis. Double-stranded cDNA was ligated into the pGADT7-Rec vector with Herring Testes Carrier DNA using homologous recombination method. The ligation mixture was transformed into competent yeast AH109 cells to construct the primary cDNA library. Eventually, a high qualitative library was successfully established according to an evaluation on quality. The transformation efficiency was about $6.39{\times}10^5$ transformants/$3{\mu}g$ pGADT7-Rec. The titer of the primary cDNA library was $2.5{\times}10^8cfu/mL$. The numbers for the cDNA library was $2.46{\times}10^5$. Randomly picked clones show that the recombination rate was 88.24%. Gel electrophoresis results indicated that the fragments ranged from 0.4 kb to 3.0 kb. Melanin synthesis protein Brn1 (1,3,8-hydroxynaphthalene reductase) was used as a "bait" to test the sufficiency of the Y2H library. As a result, a cDNA clone encoding VelB protein that was known to be involved in the regulation of diverse cellular processes, including control of secondary metabolism containing melanin and toxin production in many filamentous fungi was identified. Further study on the exact role of the VelB gene is underway.

mTOR signalling pathway - A root cause for idiopathic autism?

  • Ganesan, Harsha;Balasubramanian, Venkatesh;Iyer, Mahalaxmi;Venugopal, Anila;Subramaniam, Mohana Devi;Cho, Ssang-Goo;Vellingiri, Balachandar
    • BMB Reports
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    • v.52 no.7
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    • pp.424-433
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    • 2019
  • Autism spectrum disorder (ASD) is a complex neurodevelopmental monogenic disorder with a strong genetic influence. Idiopathic autism could be defined as a type of autism that does not have a specific causative agent. Among signalling cascades, mTOR signalling pathway plays a pivotal role not only in cell cycle, but also in protein synthesis and regulation of brain homeostasis in ASD patients. The present review highlights, underlying mechanism of mTOR and its role in altered signalling cascades as a triggering factor in the onset of idiopathic autism. Further, this review discusses how distorted mTOR signalling pathway stimulates truncated translation in neuronal cells and leads to downregulation of protein synthesis at dendritic spines of the brain. This review concludes by suggesting downstream regulators such as p70S6K, eIF4B, eIF4E of mTOR signalling pathway as promising therapeutic targets for idiopathic autistic individuals.

The Fission Yeast Gene Encoding Monothiol Glutaredoxin 5 Is Regulated by Nitrosative and Osmotic Stresses

  • Kim, Hong-Gyum;Park, Eun-Hee;Lim, Chang-Jin
    • Molecules and Cells
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    • v.20 no.1
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    • pp.43-50
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    • 2005
  • Glutaredoxin (Grx) is a small, heat-stable redox protein acting as a multi-functional glutathione (GSH)-dependent disulfide oxidoreductase. We have cloned the monothiol Grx5 gene from the genomic DNA of the fission yeast Schizosaccharomyces pombe. It has 1,904 bp, with one intron, and encodes a putative protein of 146 amino acids with a molecular mass of 16.5 kDa. Recombinant Grx5 produced functional Grx in S. pombe cells. NO-generating sodium nitroprusside (SNP, 1.0 and 2.0 mM) and potassium chloride (KCl, 0.2 and 0.5 M) increased the synthesis of ${\beta}$-galactosidase from a Grx5-lacZ fusion gene, and transcription of Grx5 was also enhanced by SNP and KCl. Synthesis of ${\beta}$-galactosidase from the Grx5-lacZ fusion was lower in Pap1-negative TP108-3C cells than in wild type KP1 cells, and when Pap1 was overproduced in KP1 cells, the level of ${\beta}$-galactosidase increased. We also found that Pap1 is involved in the induction of Grx5 by SNP and KCl. S. pombe Grx5 may play a crucial role in responses to nitrosative and osmotic stresses.

Glutamine Synthetase of some Fermentation Bacteria: Function and Application

  • Tachiki, Takashi
    • Proceedings of the Korean Society for Applied Microbiology Conference
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    • 1986.12a
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    • pp.506-508
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    • 1986
  • Metabolic activity of inorganic nitrogenous compounds affects not only microbial growth but also metabolite production in fermentation technology. We have worked on the enzymes participating in ammonia assimulation of some fermentation bacteria. This paper summarizes the results on glutamine synthetase and its application in practical field. Glutamine synthetase (L-glutamate:ammonia ligase, EC. 6.3.1.2) catalyzes the formation of glutamine from glutamate and ammonia at the expense of cleavage of ATP and inorganic phosphate. The enzyme plays a dual role in nitrogen metabolism in bacteria; it is a key enzyme not only in the biosynthesis of various compounds through glutamine but also in the regulation of synthesis of some enzymes involved in the metabolism of nitrogenous compounds. The detailed works with the Eschericia coli and other enterobacterial enzymes revealed that glutamine synthetase is controlled by the following complex of mechanisms: (a) feedback inhibition by end products, (b) repression and derepression of enzyme synthesis, (c) modulation of enzyme activity in response to divalent cation and (d) covalent modification of enzyme protein by adenylylation and its cascade control. Comparative studies have also been made on the enzymes from other organisms.

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Effects of AMP-activated Protein Kinase Activating Compounds and Its Mechanism (AMP-activated protein kinase 활성화 기전과 관련 약물의 효과)

  • Choi, Hyoung Chul
    • Journal of Yeungnam Medical Science
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    • v.29 no.2
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    • pp.77-82
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    • 2012
  • AMP-activated protein kinase (AMPK) is an important cellular fuel sensor. Its activation requires phosphorylation at Thr-172, which resides in the activation loop of the ${\alpha}1$ and ${\alpha}2$ subunits. Several AMPK upstream kinases are capable of phosphorylating AMPK at Thr-172, including LKB1 and CaMKK${\beta}$ ($Ca^{2+}$/calmodulin-dependent protein kinase kinase${\beta}$). AMPK has been implicated in the regulation of physiological signals, such as in the inhibition of cholesterol fatty acid, and protein synthesis, and enhancement of glucose uptake and blood flow. AMPK activation also exhibits several salutary effects on the vascular function and improves vascular abnormalities. AMPK is modulated by numerous hormones and cytokines that regulate the energy balance in the whole body. These hormone and cytokines include leptin, adiponectin, ghrelin, and even thyroid hormones. Moreover, AMPK is activated by several drugs and xenobiotics. Some of these are in being clinically used to treat type 2 diabetes (e.g., metformin and thiazolidinediones), hypertension (e.g., nifedipine and losartan), and impaired blood flow (e.g., aspirin, statins, and cilostazol). I reviewed the precise mechanisms of the AMPK activation pathway and AMPK-modulating drugs.

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Identification of a Regulatory Region within the luxR Structural Gene in a Marine Symbiotic Bacterium, Vibrio fischeri

  • Choi, Sang-Ho
    • Journal of Microbiology and Biotechnology
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    • v.4 no.3
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    • pp.176-182
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    • 1994
  • The light-organ symbiont of pine cone fish, Vibrio fischeri, senses its presence in the host and responds to environmental changes by differentially expressing its symbiosis-related luminescence genes. The V. fischeri luminescence genes are activated by LuxR protein in the presence of an autoinducer. In an effort to elucidate the mechanism of regulation of luxR, a plasmid containing luxR was mutagenized in vitro with hydroxylamine and a luxR mutant plasmid was isolated by its ability to activate luminescence genes cloned in E. coli in the absence of the autoinducer. The specific base change identified by DNA sequencing was only single base transition at +78 from the transcriptional start of luxR. Based on a Western immunoblot analysis, the nucleotide change directed the synthesis of much higher level of LuxR protein without any amino acid substitutions. The results suggest that the region including the +78th base is presumably internal operator required for autorepression of luxR, and the increased cellular level of LuxR results in activation of luminescence genes by autoinducer independent fashion.

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Regulation of Macrophage Ceruloplasmin Gene Expression: One Paradigm of 3'-UTR-mediated Translational Control

  • Mazumder, Barsanjit;Sampath, Prabha;Fox, Paul L.
    • Molecules and Cells
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    • v.20 no.2
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    • pp.167-172
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    • 2005
  • Ceruloplasmin (Cp) is a copper protein with important functions in iron homeostasis and in inflammation. Cp mRNA expression is induced by interferon (IFN)-${\gamma}$ in U937 monocytic cells, but synthesis of Cp protein is halted after about 12 h by transcript-specific translational silencing. The silencing mechanism requires binding of a 4-component cytosolic inhibitor complex, IFN-gamma-activated inhibitor of translation (GAIT), to a defined structural element (GAIT element) in the Cp 3'-UTR. Translational silencing of Cp mRNA requires the essential proteins of mRNA circularization, suggesting that the translational inhibition requires end-to-end mRNA closure. These studies describe a new mechanism of translational control, and may shed light on the role that macrophage-derived Cp plays at the intersection of iron homeostasis and inflammation.

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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    • v.34 no.4
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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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