• Title/Summary/Keyword: GalN

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Differential Expression of O-glycoprotein Glycans in Cholangiocarcinoma Cell Lines

  • Talabnin, Krajang;Talabnin, Chutima;Ishihara, Mayumi;Azadi, Parastoo;Wongkham, Sopit;Sripa, Banchob
    • Asian Pacific Journal of Cancer Prevention
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    • v.17 no.2
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    • pp.691-695
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    • 2016
  • Protein glycosylation is the most common posttranslational modification in mammalian cells. Aberrant protein glycosylation has been reported in various diseases, including cancer. We identified and quantified the glycan structures of O-linked glycoprotein from cholangiocarcinoma (CCA) cell lines from different histological types and compared their profiles by nanospray ionization-linear ion trap mass spectrometry (NSI-$MS^n$). Five human CCA cell lines, K100, M055, M139, M213 and M214 were characterized. The results showed that the O-linked glycans of the CCA cell lines comprised tri- to hexa-saccharides with terminal galactose and sialic acids: NeuAc1Gal1GalNAc1, Gal2GlcNAc1GalNAc1, NeuAc2Gal1GalNAc1 NeuAc1Gal2GlcNAc1GalNAc1 and NeuAc2Gal2GlcNAc1GalNAc1 All five CCA cell lines showed a similar glycan pattern, but with differences in their quantities. NeuAc1Gal1GalNAc1 proved to be the most abundant structure in poorly differentiated adenocarcinoma (K100; 57.1%), moderately differentiated adenocarcinoma (M055; 42.6%) and squamous cell carcinoma (M139; 43.0%), while moderately to poorly differentiated adenocarcinoma (M214; 40.1%) and adenosquamous cell carcinoma (M213; 34.7%) appeared dominated by $NeuA_{c2}Gal_1GalNA_{c1}$. These results demonstrate differential expression of the O-linked glycans in the different histological types of CCA. All five CCA cell lines have abundant terminal sialic acid (NeuAc) O-linked glycans, suggesting an important role for sialic acid in cancer cells. Our structural analyses of glycans may provide important information regarding physiology of disease-related glycoproteins in CCA.

Synthesis of the 2'-Azidoethyl Trisaccharide, 6d-altroHepp-GlcNAc-Gal Hapten, an O-Antigenic Repeating Unit of Campylobacter jejuni Serotypes O:23 and O:36

  • Yun, Mi-Kyung;Shin, Jeong E. Nam
    • Bulletin of the Korean Chemical Society
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    • v.29 no.7
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    • pp.1315-1319
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    • 2008
  • A trisaccharide, 6d-Altro-Hepp$\alpha$ (1$\rightarrow$3) GlcNAc$\beta$ (1$\rightarrow$3) Gal$\alpha$ (1$\rightarrow$$OCH_2CH_2N_3$, as an O-antigenic repeating unit of Campylobacter jejuni serotypes O:23 and O:36, was synthesized. Coupling of the 6d-altro-Hepp$\alpha$ (1$\rightarrow$3) GlcNAc$\beta$ (1$\rightarrow$SEt donor with Gal$\alpha$ (1${\rightarrow}OCH_2CH_2Cl$ acceptor in the presence of NIS-TfOH promoter afforded the trisaccharide having the $\beta$ (1$\rightarrow$3) Gal linkage. $\beta$ -Stereospecificity and the desired regioselectivity for the 3-OH Gal are obtained. Subsequent hydrogenation, acetylation, azide displacement, hydrazinolysis, Nacetylation, and finally deacetylation furnished the title trisaccharide hapten for further glycoconjugation.

Developmental Patterns of Gal$\beta$1,3(4)GlcNAc $\alpha$2,3-Sialyltransferase (ST3Gal III) Expression in the Mouse: In Situ Hybridization Using DIG-labeled RNA Probes

  • Ji, Min-Young;Lee, Young-Choon;Kim, Kyoung-Sook;Cho, Jin-Won;Jung, Kyu-Yong;Kim, Cheorl-Ho;Choo, Young-Kug
    • Archives of Pharmacal Research
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    • v.22 no.3
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    • pp.243-248
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    • 1999
  • Sialic acids are key determinants for biological processes, such as cell-cell interaction and differentiation. Sialyltransferases contribute to the diversity in carbohydrate structure through their attachment of sialic acid in various terminal positions on glycolipid and glycoprotein (N-linked and O-linked) carbohydrate groups. Gal$\beta$ 1,3(4)GlcNAc $\alpha$2,3-sialyltransferase (ST3Gal III) is involved in the biosynthesis of $sLe^{X}$ and sLe^{a}$ known as selection ligands and tumor-associated carbohydrate structures. The appearance and differential distribution of ST3Gal III mRNA during mice embryogenesis [embryonic (E) days; E9, E11, E13, E15] were investigated by in situ hybridization with digoxigenin-labeled RNA probes coupled with alkaline phosphatase detection. On E9, all tissues were positive for ST3Gal III mRNA expression whereas ST3Gal III mRNA on E11 was not detected throughout all tissues. On E13, ST3GAl III mRNA was expressed in different manner in various tissues. In this stage, ST3Gal III mRNA was positive only in the liver, pancreas and bladder. On E15, specific signal for ST3GAl III was detected in the liver, lung and forebrain. These results indicate that ST3Gal III is differently expressed at developmental stages of mice embryo, and this may be importantly related with regulation of organogenesis in mice.

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Hepatoprotective Activity of Bacopa monniera on D-galactosamine Induced Hepatotoxicity in Rats

  • Ramakrishnan, S.;Sumathi, T.
    • Natural Product Sciences
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    • v.13 no.3
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    • pp.195-198
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    • 2007
  • Hepatoprotective action of alcoholic extract of Bacopa monniera (BME) was evaluated on Dgalactosamine (D-GalN) induced rat liver toxicity. Bacopa monniera extract reduced the elevated serum enzyme activities of ALT, AST, ALP, LDH, ${\gamma}-GT$ and the formation of hepatic malondialdehyde induced by D-GalN. The alcholic extract of Bacopa monniera also significantly restored the decreased levels of glutathione and the decreased activities of glutathione peroxidase, glutathione reductase, superoxide dismutase, catalase and glucose-6-phosphatase. Therefore these results suggest that Bacopa monniera has hepatoprotective effect against D-GalN induced hepatotoxicity.

Inhibitory Effects of Oriental Medicinal Herbs on Enzymatic Activity of Sialyltransferases (ST3Gal I and ST6Gal I) Associated with Cancer

  • Kim, Kyoung-Sook;Kim, Cheorl-Ho;Kim, June-Ki;Lee, Young-Choon
    • Journal of Life Science
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    • v.10 no.1
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    • pp.51-56
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    • 2000
  • In many cases of human cancer, the appearance of hypersialylated glycan structures is related to a precise stage of the disease ; this may depend on the elebated sialyltransferase activity during carcinogenesis. The aim of this study was to investigate the inhibitory effects of Oriental medicinal herbs on enzymatic activities of two kinds ofsialyltransferase, Gal $\beta$ 1,3GalNAc$\alpha$2,3-sialyltransferase(ST3Gal I) and Gal $\beta$ 1,4GlcNAc $\alpha$2,6-sialyltransterases(ST6Gal I), which are well known as glycosyltransterases associated with cancer. The aqueous extracts of Scutellaria Baicalensis Georgi, Coptidis Rhizoma, Glycyrrhiza urlensis Fisch, Bupleuri Radix and Platycodi Radix were prepared and tested, respectively. At concentration of 100$\mu$g, Glycyrrhiza uralensis Fisch showed the highest inhibitory effects(about 42% and 57%, respectively) on ST3Gal Iand ST6Gal Iactivities. ST3GAl I was inhibited about 23% by Scutellaria baicalensi G댁햐, but not by the other samples, whereas ST6Gal I was inhibited about 20% and 40%,respectively, by Scutellaria baicalensis Georgi and Bupleuri Radix. All inhibitory effects were obtained in a concentration-dependent manner.

Molecular Cloning and Substrate Specificity of Human NeuAc ${\alpha}$2,3Gal${\beta}$ 1,3GalNAc GalNac ${\alpha}$2,6-Sialyltransferase (hST6GalNac IV)

  • Lee, Young-Choon;Kim, Kyoung-Sook;Kim, Sang-Wan;Min, Kwan-Sik;Kim, Cheorl-Ho;Choo, Young-Kug
    • Journal of Life Science
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    • v.11 no.1
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    • pp.57-64
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    • 2001
  • The cDNA encoding human NeuAc ${\alpha}$2,3Gal$\beta$ 1,3GalNAc GalNac ${\alpha}$2,6-Sialyltransferase (hST6GalNac IV) was isolated by screening of human fetal liver cDNA library with a DNA probe generated from the cDNA sequence of mouse ST6Gal NAc IV (mkST6GalNAc IV). The cDNA sequence included an open reading frame coding for 302 amino acids, and comparative analysis of this cDNA with mST6GalNAc IV showed that each sequence of the predicted coding region contains 88% and 85% identifies in nucleotide and amino acid levels, respecively. The primary structure of this enzyme suggested a putative domain structure, like that in other glycosyltransferases, consisting of a short N-terminal cytoplamic domain, a transmembrane domain and a large C-terminal active domain. This enzyme expressed in COS-7 cells echibited transferase activity toward NeuAc ${\alpha}$2,3Gal$\beta$ 1,3GalNAc, fetuin and GM1b, although the activity toward the later is very low, no significant activity being detected toward Gal${\beta}$ 1,3Gal NAc or asialofetuin, the other glycoprotein substrates tested. The $^{14}$ C-sialylated residue of fetuin sialylated by this enzyem with CMP-[$^{14}$C]NeuAc was sensitive to treatment with ${\alpha}$2,8-specific sialidase of Vibrio cholerae but resistant to treatment with ${\alpha}$2,3-specific sialidase (NaNase I), and ${\alpha}$2,3- and ${\alpha}$2,8-specific sialidase of Newcastle disease virus. These results clearly indicated that the expressed enzyme is a type of GalNAc ${\alpha}$2,6-sialyltransferase like mST6GalNAc IV, which requires sialic acid residues linked to Gal${\beta}$1,3GalNAc-residues for its activity.

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GALOIS GROUPS OF MODULES AND INVERSE POLYNOMIAL MODULES

  • Park, Sang-Won;Jeong, Jin-Sun
    • Bulletin of the Korean Mathematical Society
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    • v.44 no.2
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    • pp.225-231
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    • 2007
  • Given an injective envelope E of a left R-module M, there is an associative Galois group Gal$({\phi})$. Let R be a left noetherian ring and E be an injective envelope of M, then there is an injective envelope $E[x^{-1}]$ of an inverse polynomial module $M[x^{-1}]$ as a left R[x]-module and we can define an associative Galois group Gal$({\phi}[x^{-1}])$. In this paper we describe the relations between Gal$({\phi})$ and Gal$({\phi}[x^{-1}])$. Then we extend the Galois group of inverse polynomial module and can get Gal$({\phi}[x^{-s}])$, where S is a submonoid of $\mathbb{N}$ (the set of all natural numbers).

ON CONGRUENCES OF n-ARY GROUPS

  • Gal'mak, Alexandr M.
    • East Asian mathematical journal
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    • v.21 no.2
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    • pp.241-248
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    • 2005
  • Properties of congruences on n-ary groups are investigated.

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Hepatoprotective effect of Ainsliaea acerifolia water extract on LPS/D-GalN-induced acute liver injury in human HepG2 cells (단풍취 열수 추출물의 HepG2 인간간세포의 LPS/D-Gal에 의해 유발된 급성 간 손상에 대한 간보호 효과)

  • Lee, Sun-Yeop;Han, Joon-Hee;Choi, Da-Hye;Hong, Min;Kwon, Tae-Hyung;Lee, Yong-Jin;Yu, Keun-Hyung
    • Korean Journal of Food Science and Technology
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    • v.52 no.5
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    • pp.476-481
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    • 2020
  • This study investigated the antioxidant and hepatoprotective effects of Ainsliaea acerifolia water extract (AAWE) on HepG2 cells. Five types of caffeoylquinic acid (CQA) were detected in AAWE, namely, 4,5-di-O-caffeoylquinic acid (4,5-DCQA; 11.16 mg/g), 3,4-di-O-caffeoylquinic acid (3,4-DCQA; 5.23 mg/g), 5-O-caffeoylquinic acid (5-CQA; 4.88 mg/g), 3,5-di-O-caffeoylquinic acid (3,5-DCQA; 3.51 mg/g), and 4-O-caffeoylquinic acid (4-CQA; 3.31 mg/g). AAWE exerted ABTS+ antioxidant effects, evidenced by polyphenol content and 2,2'2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) and 2,2-diphenyl-1-picryl-hydrazyl-hydrate (DPPH radical scavenging) activities. AAWE (300 ㎍/mL) treatment significantly decreased the activities of gamma glutamyl transferase (GGT), aspartate transaminase (AST), and lactate dehydrogenase (LDH) as compared to control and exerted protective effects against the increase in liver function index induced by lipopolysaccharide (LPS)/galactosamine (D-GalN) in HepG2 cells. In addition, the secretion of tumor necrosis factor (TNF)-α by HepG2 cells induced by LPS/D-GalN significantly increased in all treatment groups compared to that in the control. However, AAWE (100-300 ㎍/mL) treatment significantly decreased the secretion of TNF-α compared to that in the control. These results suggest that AAWE treatment reduces hepatotoxicity by increasing antioxidant activities, reducing GGT, AST, and LDH activities, and inhibiting TNF-α secretion.

Effect of High-Intensity Interval Training on Acute Liver Failure Induced by D-Galactosamine/Lipopolysaccharide in Balb/c Mice (고강도 인터벌 트레이닝이 D-Gal/LPS로 유도된 마우스의 급성 간 부전에 미치는 효과)

  • Cho, Jin-Kyung;Park, Soo-Hyun;Kang, Hyun-Sik
    • Exercise Science
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    • v.26 no.3
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    • pp.223-228
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    • 2017
  • PURPOSE: This study investigated the protective role of high-intensity interval training against acute liver injury induced by D-galactosamine (D-Gal)/lipopolysaccharide (LPS). METHODS: A total of 30 male BALB/c mice aged 5-week were randomly assigned to high-intensity, interval training group (EX, n=10) or control group in cage (Non-EX, n=20) for 10 weeks. Peritoneal injection of D-Gal (700 mg/kg body weight) and LPS ($10{\mu}g/kg$ body weight) was applied to induce acute liver injury, and liver tissue was harvested 6 hours after the injection. Hematoxylin and Eosin (H&E) staining was used for liver histology. Real-time PCR was used to quantify expression of pro-inflammatory and anti-inflammatory genes in the liver. RESULTS: The liver histology showed that D-Gal/LPS treatment resulted in hepatic damage and increased number of neutrophils in conjunction with upregulation of hepatic IL-6 and $TNF-{\alpha}$ mRNAs and downregulation of hepatic $PPAR{\alpha}$ and SIRT1 mRNAs. On the other hand, the 10-week interval training resulted in a significant improvement in cardiorespiratory fitness assessed as run time to exhaustion on a treadmill. In addition, the interval training attenuated the D-Gal/LPS-induced liver damage and increased number of neutrophil in conjunction with downregulation of hepatic IL-6 and $TNF-{\alpha}$ mRNAs and upregulation of hepatic $PPAR{\alpha}$ and SIRT1 mRNAs. CONCLUSIONS: This study suggests that high-intensity interval training suppresses the D-Gal and LPS-induced acute liver damage and inflammatory responses.