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2011 | 58 | 4 | 471-475
Article title

In vitro effects of compounds isolated from Sideritis brevibracteata on bovine kidney cortex glutathione reductase

Content
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EN
Abstracts
EN
Glutathione reductase (GR, E.C 1.6.4.2) is a flavoprotein that catalyzes NADPH-dependent reduction of oxidized glutathione (GSSG) to reduced glutathione (GSH). The aim of this study was to investigate in vitro effects of phenolic compounds isolated from Sideritis brevibracteata on bovine kidney GR. The Sideritis species are widely found in nature and commonly used as medicinal plants. 7-O-glycosides of 8-OH-flavones (hypolaetin, isoscutellarein and 3'-hydroxy-4'-O-methylisoscutellarein) were isolated from aerial parts of Sideritis brevibracteata. These compounds inhibited bovine kidney cortex GR in a concentration-dependent manner. Kinetic characterization of the inhibition was also performed.
Publisher

Year
Volume
58
Issue
4
Pages
471-475
Physical description
Dates
published
2011
received
2010-04-19
revised
2010-12-10
accepted
2011-11-28
(unknown)
2011-12-06
Contributors
  • Department of Biochemistry, Faculty of Medicine, Hacettepe University, Ankara, Turkey
  • Department of Pharmaceutical Botany, Faculty of Pharmacy, Ankara University, Ankara, Turkey
  • Department of Pharmacognosy, Faculty of Pharmacy, Hacettepe University, Ankara, Turkey
  • Department of Biochemistry, Faculty of Medicine, Hacettepe University, Ankara, Turkey
References
  • Acan NL, Tezcan EF (1989) Sheep brain glutathione reductase: Purification and general properties. FEBS Lett 250: 72-74.
  • Ajay A, Walters WP, Murcko MA (1998) Can we learn to distinguish between drug like and nondrug-likemolecules? J Med Chem 41: 3314-3324.
  • Arscott LD, Veine DM, Williams CH Jr. (2000) Mixed disulfide with glutathione as an intermediate in the reaction catalyzed by glutathione reductase from yeast and as a major form of the enzyme in the cell. Biochemistry 39: 4711-4721.
  • Awasthi YC, Chaudhary P, Vatsyayan R, Sharma A, Awasthi S, Sharma R. (2009) Physiological and pharmacological significance of glutathione-conjugate transport. J Toxicol Environ Health B Crit Rev 12: 540-551.
  • Barberan FA, Manez S, Villar A (1987) Identification of antiinflammatory agents from Sideritis species growing in Spain. J Nat Prod 50: 313-314.
  • Baser KHC, Kirimer N, Tümen G (1997) The Essential Oil of Sideritis scardica Griseb. subsp. scardica. J Essent Oil Res 9: 205-207.
  • Batista R, Silva Ade J Jr, de Oliveira AB (2009) Plant-derived antimalarial agents: new leads and efficient phytomedicines. Part II. Non-alkaloidal natural products. Molecules 14: 3037-3072.
  • Bauer H, Fritz-Wolf K, Winzer A, Kuhner S, Little S, Yardley V, Vezin H, Palfey B, Schirmer RH, Davioud-Charvet E. (2006) A fluoro analogue of the menadione derivative 6-[2'-(3'-methyl)-1',4'-naphthoquinolyl]hexanoic acid is a suicide substrate of glutathione reductase. Crystal structure of the alkylated human enzyme. J Am Chem Soc 128: 10784-10794.
  • Cao S, Kingston DG (2009) Biodiversity conservation and drug discovery: Can they be combined? The Suriname and Madagascar experiences. Pharm Biol 47: 809-823.
  • De Las Heras B, Vivas JM, Villar A (1994) Anti-inflammatory activity of Sideritis javalambrensis extracts. J Ethnopharmacol 41: 15-17.
  • Ezer N, Sakar M K, Rodriguez B, Dela Torre MC (1992) Flavonoid glycosides and a phenylpropanoid glycoside from Sideritis perfoliata. Int J Pharmacog 30: 61-65.
  • Güvenç A, Okada Y, Küpeli Akkol E, Duman H, Okuyama T, Çalış I (2010) Investigations of anti-inflammatory, antinociceptive, antioxidant and aldose reductase inhibitory activities of phenolic compounds from Sideritis brevibracteata. Food Chem 118: 686-692.
  • Koehn FE, Carter GT (2005) The evolving role of natural products in drug discovery. Nature Reviews Drug Discovery 4: 206-220.
  • Krauth-Siegel RL, Arscott LD, Schonleben-Janas A, Schirmer RH, Williams CH Jr (1998) Role of active site tyrosine residues in catalysis by human glutathione reductase. Biochemistry 37: 13968-13977.
  • Lee KH (2010) Discovery and development of natural product-derived chemotherapeutic agents based on a medicinal chemistry approach. J Nat Prod 73: 500-516.
  • Seefeldt T, Dwivedi C, Peitz G, Herman J, Carlson L, Zhang Z, Guan XJ (2005) Acetylamino-3-[4-(2-acetylamino-2-carboxyethylsulfanylcarbonylamino)-phenylcarbamoylsulfanyl] propionic acid and its derivatives as a novel class of glutathione reductase inhibitors. J Med Chem 48: 5224-5231.
  • Segel IH (1975) Enzyme Kinetics. 3rd edn, Chapter 3. pp 100-159. John Wiley and Sons: Toronto.
  • Sun Y (1990) Free radicals, antioxidant enzymes, and carcinogenesis. Free Radic Biol Med 8: 583-599.
  • Tandogan B, Ulusu NN (2010) Purification and kinetics of bovine kidney cortex glutathione reductase. Protein Pept Lett 17: 667-674.
  • Untucht-Grau R, Schirmer RH, Schirmer I, Krauth-Siegel RL (1981) Glutathione reductase from human erythrocytes: amino-acid sequence of the structurally known FAD-binding domain. Eur J Biochem 120: 407-419.
  • Yesilada E, Ezer N (1989) The antiinflammatory activities of some Sideritis spp. growing in Turkey. Int J Crude Drug Res 27: 38-40.
Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv58p471kz
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