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Aktuelle Ernährungsmedizin 2003; 28(6): 363-370
DOI: 10.1055/s-2003-45376
Originalbeitrag
© Georg Thieme Verlag Stuttgart · New York

In Vivo Determination of Oxidative Stress

In-vivo-Messung von oxidativem StressB.  Wirleitner1 , K.  Schröcksnadel1 , C.  Winkler1 , B.  Frick1 , D.  Fuchs1
  • 1Institute for Medical Chemistry and Biochemistry, University of Innsbruck, and Ludwig Boltzmann Institute for AIDS-Research, Innsbruck, Österreich
1. This work was supported by the Austrian Science Foundation „zur Förderung der wissenschaftlichen Forschung” (Grant P14154-MED)2. Manuskript nach einem Vortrag bei dem 21. Gemeinsamen Kongress von AKE, DGEM und GESKES Nutrition 2003 in Linz vom 12. - 14.6.2003
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Publication History

Publication Date:
16 December 2003 (online)

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Zusammenfassung

Sauerstoff ist für eukaryontische Zellen essenziell für die Energieproduktion. Ein Leben in einer aeroben Umgebung bedeutet aber auch eine ständige Konfrontation mit reaktiven Sauerstoffverbindungen, die z. B. als Nebenprodukte des aeroben Stoffwechsels entstehen. Sauerstoffradikale werden ebenfalls im Rahmen von Immunaktivierungsvorgängen durch immunkompetente Zellen massiv freigesetzt und können Schäden an Zellstrukturen verursachen. Die hauptsächlichen Ziele der Radikale sind hierbei Enzyme, Zellmembrane sowie die DNS. Oxidativer Stress entsteht, wenn eine zu große Bildung von Sauerstoffradikalen einem zu geringen Pool an Antioxidantien gegenübersteht. Die Entdeckung, dass oxidativer Stress eine wichtige Rolle in der Pathogenese einer großen Reihe von Erkrankungen spielt, hat die Erforschung dieser Vorgänge in den Fokus des Interesses gesetzt. Unterschiedliche Methoden wurden entwickelt, um oxidativen Stress in vivo zu quantifizieren, wie die Messungen von Oxidationsprodukten bei der Lipidperoxidation, oxydierte Proteine oder DNS. Alternativ dazu ist die Evaluierung des Verbrauchs von Antioxidantien. Diese Zusammenfassung gibt einen Überblick über verschiedener Methoden zur Quantifizierung von oxidativem Stress in vivo.

Abstract

Oxygen is required by eukaryotic cells for energy production. Living in an aerobic environment brings with the exposure of cells to reactive oxygen species (ROS). ROS for example accumulate as byproducts of the aerobic metabolism, and a substantial endogenous generation of ROS occurs during immune response by immunocompetent cells. Massive occurrence of ROS results in oxidative damage of cellular components. The primary targets of ROS are enzymes, cell membranes, and DNA. Oxidative stress is defined by an overwhelming occurrence of ROS opposed by an exhausted pool of antioxidants. In the last decade, the role of oxidative stress in the pathogenesis of a wide range of human diseases became obvious, and determination of the phenomenon of oxidative stress moved into the focus of interest. Several approaches were developed to quantify this condition. Among them are measurements of oxidation products such as lipid peroxidation, oxidized protein, or DNA. Alternatively, oxidative stress can be determined by the loss of antioxidants. This review briefly summarizes current available methods for the quantification of oxidative stress in vivo.

Schlüsselwörter

Sauerstoffradikale - Antioxidantien - Immunantwort - Neopterin

Key words

Reactive oxygen species - antioxidants - immune response - neopterin

References

  • 1 Hurst J K, Barette W C. Leukocyte oxygen activation and microbicidal oxidative toxins.  Crit Rev Biochem Mol Biol. 1989;  24 271-328
    PubMedSearch in Google Scholar
  • 2 Kohen R, Nydka A. Oxidation of biological systems: oxidative stress phenomena, antioxidants, redox reactions, and methods for their quantification.  Toxicol Pathol. 2002;  30 620-650
    CrossrefPubMedSearch in Google Scholar
  • 3 Halliwell B. Free radicals, antioxidants, and human disease: curiosity, cause, or consequence?.  Lancet. 1984;  344 721-724
    PubMedSearch in Google Scholar
  • 4 Powis G, Briehl M, Oblong J. Redox signalling and the control of cell growth and death.  Pharmac Ther. 1995;  65 149-173
    PubMedSearch in Google Scholar
  • 5 Davies K J. Protein damage and degradation of oxygen radicals. I. General aspects.  J Biol Chem. 1987;  262 9895-9901
    PubMedSearch in Google Scholar
  • 6 Halliwell B, Gutteridge J MC. Free radicals in biology and medicine. 2nd ed. Oxford; Clarendon Press 1990
    Search in Google Scholar
  • 7 Beckman K B, Ames B N. Oxidative decay of DNA.  J Biol Chem. 1997;  272 19633-19636
    CrossrefPubMedSearch in Google Scholar
  • 8 Esterbauer H, Schaur R J, Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes.  Free Radic Biol Med. 1991;  11 81-128
    CrossrefPubMedSearch in Google Scholar
  • 9 Bird R P, Draper H H. Comparative studies on different methods of malondialdehyde determination.  Methods Enzymol. 1984;  105 299-305
    PubMedSearch in Google Scholar
  • 10 Marnett L F, Tuttle M A. Comparison of the mutagenicities of malondialdehyde and the side products formed during its chemical synthesis.  Cancer Res. 1980;  40 276-282
    PubMedSearch in Google Scholar
  • 11 Benzie I F. Lipid peroxidation: a review of causes, consequences, measurement and dietary influences.  Int J Fodd Sci Nutr. 1996;  47 233-261
    PubMedSearch in Google Scholar
  • 12 Dib M, Garrel C, Favie A, Robin V, Desnuelle C. Can malondialdehyde be used as a biological marker of progression in neurodegenerative disease?.  J Neurol. 2002;  249 367-374
    PubMedSearch in Google Scholar
  • 13 Valles J, Aznar J, Santos M T, Fernandez M A. Elevated lipid peroxide levels in platelets of chronic ischemic heart disease patients.  Thromb Res. 1882;  27 585-589
    PubMedSearch in Google Scholar
  • 14 Roberts L J, Morrow J D. Measurement of F2-isoprostanes as an index of oxidative stress in vivo.  Free Radic Biol Med. 2000;  28 505-513
    CrossrefPubMedSearch in Google Scholar
  • 15 Praticò D. F2-isoprostanes, sensitive and specific non-invasive indices of lipid peroxidation in vivo.  Atherosclerosis. 1999;  147 1-10
    CrossrefPubMedSearch in Google Scholar
  • 16 Patrono C, FitzGerald G A. Isoprostanes: potential markers of oxidant stress in atherothrombotic disease.  Arterioscler Thromb Vasc Biol. 1997;  17 2309-2315
    PubMedSearch in Google Scholar
  • 17 Jiang Z Y, Hunt J V, Wolff S P. Ferrous ion oxidation in the presence of xylenol orange for detection of lipid hydroperoxide in lowdensity lipoprotein.  Anal Biochem. 1992;  202 384-389
    CrossrefPubMedSearch in Google Scholar
  • 18 Davies M F, Fu S, Wang H, Dean R T. Stable markers of oxidant damage to proteins and their application in the study of human disease.  Free Radic Biol Med. 1999;  27 1151-1163
    CrossrefPubMedSearch in Google Scholar
  • 19 Beckman J S, Koppenol W H. Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly.  Am J Physiol. 1996;  271 C1424-1437
    PubMedSearch in Google Scholar
  • 20 Halliwell B. Reactive oxygen species and the central nervous system.  J Neurochem. 1992;  59 1609-1623
    CrossrefPubMedSearch in Google Scholar
  • 21 Good P F, Hsu A, Werner P, Perl D P, Oanow C W. Protein nitration in Parkinson's disease.  J Neuropathol Exp Neurol. 1998;  57 338-342
    CrossrefPubMedSearch in Google Scholar
  • 22 Shigenaga M K, Gimeno C J, Ames B N. Urinary 8-hydroxy-2'-deoxyguanosine as a biomarker of in vivo oxidative DNA damage.  Proc Natl Acad Sci USA. 1989;  86 9697-9701
    PubMedSearch in Google Scholar
  • 23 Iiada T, Furuta A, Kawashima M, Nishida J, Nakabeppu Y, Iwaki T. Accumulation of 8-oxo-2'-deoxyguanosine and increased expression of hMTH1 protein in brain tumors.  Neurooncol. 2001;  3 73-81
    PubMedSearch in Google Scholar
  • 24 Tietze F. Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues.  Anal Biochem. 1969;  27 502-522
    CrossrefPubMedSearch in Google Scholar
  • 25 Brigelius R, Muckel C, Akerboom T P, Sies H. Identification and quantitation of glutathione in hepatic protein mixed disulfides and its relationship to glutathione disulfide.  Biochem Pharmacol. 1983;  32 2529-2534
    CrossrefPubMedSearch in Google Scholar
  • 26 Reed D J, Babson J R, Beatty P W, Brodie A E, Ellis W W, Potter D W. High-performance liquid chromatography analysis of nanomole levels of glutathione, glutathione disulfide, and related thiols and disulfides.  Anal Biochem. 1980;  106 55-62
    CrossrefPubMedSearch in Google Scholar
  • 27 Newton G L, Dorian R, Fahey R C. Analysis of biological thiols: derivatization with monobromobimane and separation by reverse phase high-performance liquid chromatography.  Anal Biochem. 1981;  114 383-387
    CrossrefPubMedSearch in Google Scholar
  • 28 Samiec P S, Drews-Botsch F, Flagg E W, Kurtz J C, Sterinberg P, Reed R L, Jones D P. Glutathione in human plasma: decline in association with aging, age-related macular degeneration, and diabetes.  Free Radic Biol Med. 1998;  24 699-704
    CrossrefPubMedSearch in Google Scholar
  • 29 Navarro J, Obrador E, Carretero J, Petschen I, Avino J, Perez P, Estrela J M. Changes in glutathione status and the antioxidant system in blood and in cancer cells associated with tumour growth in vivo.  Free Radic Biol Med. 1999;  26 410-418
    CrossrefPubMedSearch in Google Scholar
  • 30 Herzenberg L A, Rosa S C De, Dubs J G, Roederer M, Anderson M T, Ela S W, Dereninski S C, Herzenberg L A. Glutathione deficiency is associated with impaired survival in HIV disease.  Proc Natl Acad Sci USA. 1997;  94 1967-1972
    CrossrefPubMedSearch in Google Scholar
  • 31 Ross R, Milzani A, Dalle-Donne I, Giustarini D, Lusini L, Colombo R, Simplicio P Di. Blood glutathione disulfide: In vivo factor or in vitro artefact?.  Clin Chem. 2002;  48 742-753
    PubMedSearch in Google Scholar
  • 32 Brigelium-Flohé R, Kelly F J, Salonen J R, Neuzil J, Zingg J M, Azzi A. The European perspective on vitamin E: current knowledge and future research.  Am J Clin Nutr. 2002;  76 703-716
    PubMedSearch in Google Scholar
  • 33 Benzie I F, Strain J J. The ferric reducing ability of plasma (FRAP) as a measure of „antioxidant power”: the FRAP assay.  Anal Biochem. 1996;  239 70-76
    CrossrefPubMedSearch in Google Scholar
  • 34 Güler K, Palanduz S, Ademoglu E, Sahnayenli N, Gökkusu C, Vatanserver S. Total antioxidant status, lipid parameters, lipid peroxidation and glutathione levels in patients with acute myocardial infarction.  Med Sci Res. 1998;  26 105-106
    PubMedSearch in Google Scholar
  • 35 Miller N J, Rice-Evans C, Davies M J, Gopinathan V, Milner A. A novel method for measuring antioxidant capacity and its application to monitoring the antioxidant status in plasma and body fluids.  Meth Enzymol. 1994;  234 279-293
    PubMedSearch in Google Scholar
  • 36 Rice-Evans C, Miller N J. Total antioxidant status in plasma and body fluids.  Meth Enzymol. 1994;  234 279-293
    PubMedSearch in Google Scholar
  • 37 Wayner D D, Burton G W, Ingold K U, Locke S. Quantitative measurement of the total, peroxyl radical-trapping antioxidant capacity of human blood plasma by controlled peroxidation.  FEBS Lett. 1985;  187 33-37
    CrossrefPubMedSearch in Google Scholar
  • 38 Alho H, Leinonen J. Total antioxidant activity measured by chemiluminescence methods.  Meth Enzymol. 1999;  299 3-14
    PubMedSearch in Google Scholar
  • 39 Glazer A N. Phycoerythrin fluorescence-based assay for reactive oxygen species.  Meth Enzymol. 1990;  186 161-168
    PubMedSearch in Google Scholar
  • 40 Cao G, Booth S L, Sadowski J A, Prior R L. Increases in human plasma antioxidant capacity following consumption of controlled diets high in fruits and vegetables.  Am J Clin Nutr. 1998;  68 1081-1087
    PubMedSearch in Google Scholar
  • 41 Cao G, Prior R L. Comparison of different analytical methods for assessing total antioxidant capacity of human serum.  Clin Chem. 1998;  44 1309-1315
    PubMedSearch in Google Scholar
  • 42 Jackson P, Loughrey C M, Leghtbody J H, McNamee P T, Young I S. Effect of hemodialysis on total antioxidant capacity and serum antioxidants in patients with chronic renal failure.  Clin Chem. 1995;  41 1135-1138
    PubMedSearch in Google Scholar
  • 43 Gerardi G M, Usberti M, Martini G, Alberini A, Sugherini L, Pompella A, Lorenzo D Di. Plasma total antioxidant capacity in hemodialyzed patients and its relationships to other biomarkers of oxidative stress and lipid peroxidation.  Clin Chem Lab Med. 2002;  40 104-110
    CrossrefPubMedSearch in Google Scholar
  • 44 Cao G, Shukitt-Hale B, Bichford P C, Joseph J A, McEwen J, Prior R L. Hyperoxida-induced changes in antioxidant capacity and the effect of dietary antioxidants.  J Appl Physiol. 1999;  86 1817-1822
    PubMedSearch in Google Scholar
  • 45 Farinati F, Cardin R, Degan P, Maria N De, Floyd R A, Thiel D H Van, Naccarato R. Oxidative DNA damage in circulating leukocytes occurs as an early event in chronic HCV infection.  Free Radic Biol Med. 1999;  27 1284-1291
    CrossrefPubMedSearch in Google Scholar
  • 46 O'Byrne K F, Dalgleish A G. Chronic immune activation and inflammation as the cause of malignancy.  Brit J Cancer. 2001;  85 473-483
    PubMedSearch in Google Scholar
  • 47 Nathan C F. Peroxide and pteridine: a hypothesis on the regulation of macrophage antimicrobial activity by interferon gamma.  Interferon. 1986;  7 125-143
    PubMedSearch in Google Scholar
  • 48 Huber C, Batchelor J R, Fuchs D, Hausen A, Lang A, Niederwieser D, Reibnegger G, Swetly P, Troppmair J, Wachter H. Immune response-associated production of neopterin. Release from macrophages primarily under control of interferon-gamma.  J Exp Med. 1984;  160 310-316
    CrossrefPubMedSearch in Google Scholar
  • 49 Reibnegger G, Auhuber I, Fuchs D, Hausen A, Judmaier G, Prior C, Werner E R, Wachter H. Urinary neopterin levels in acute viral hepatitis.  Hepatology. 1988;  8 771-774
    PubMedSearch in Google Scholar
  • 50 Fuchs D, Hausen A, Reibnegger G, Werner E R, Dierich M P, Wachter H. Neopterin as a marker for activated cell-mediated immunity: application in HIV infection.  Immunol Today. 1988;  9 150-155
    CrossrefPubMedSearch in Google Scholar
  • 51 Lim K L, Jones A C, Brown N S, Powell R J. Urine neopterin as a parameter of disease activity in patients with systemic lupus erythematosus: comparisons with serum sIL-2R and antibodies to dsDNA, erythrocyte sedimentation rate, and plasma C3, C4, and C3 degradation products.  Ann Rheum Dis. 1993;  52 429-435
    PubMedSearch in Google Scholar
  • 52 Hausen A, Fuchs D, Grunewald K, Huber H, Koenig K, Wachter H. Urinary neopterine as marker for haematological neoplasias.  Clin Chim Acta. 1981;  117 297-305
    CrossrefPubMedSearch in Google Scholar
  • 53 Murr C, Bergant A, Widschwendter M, Heim K, Schröcksnadel H, Fuchs D. Neopterin is an independent prognostic variable in females with breast cancer.  Clin Chem. 1999;  45 1998-2004
    PubMedSearch in Google Scholar
  • 54 Margreiter R, Fuchs D, Hausen A, Huber C, Reibnegger G, Spielberger M, Wachter H. Neopterin as a new biochemical marker for diagnosis of allograft rejection. Experience based upon evaluation of 100 consecutive cases.  Transplantation. 1983;  36 650-653
    PubMedSearch in Google Scholar
  • 55 Tatzber F, Rabl H, Koriska K, Erhart U, Puhl H, Waeg G, Krebs A, Esterauer H. Elevated serum neopterin levels in atherosclerosis.  Atherosclerosis. 1991;  89 203-208
    PubMedSearch in Google Scholar
  • 56 Leblhuber F, Walli J, Demel U, Tilz G P, Widner B, Fuchs D. Increased serum neopterin concentrations in patients with Alzheimer's disease.  Clin Chem Lab Med. 1999;  37 429-431
    CrossrefPubMedSearch in Google Scholar
  • 57 Widner B, Leblhuber F, Fuchs D. Increased neopterin production and tryptophan degradation in advanced Parkinson's disease.  J Neural Transm. 2002;  109 181-189
    CrossrefPubMedSearch in Google Scholar
  • 58 Murr C, Fuchs D, Gossler W, Hausen A, Reibnegger G, Werner E R, Werner-Felmayer G, Esterbauer H, Wachter H. Enhancement of hydrogen peroxide-induced luminol-dependent chemiluminescence by neopterin depends on the presence of iron chelator complexes.  FEBS Lett. 1994;  338 223-226
    CrossrefPubMedSearch in Google Scholar
  • 59 Herpfer I, Greilberger J, Ledinski G, Widner B, Fuchs D, Jurgens G. Neopterin and 7,8-dihydroneopterin interfere with low density lipoprotein oxidation mediated by peroxynitrite and/or copper.  Free Radic Res. 2002;  36 509-520
    CrossrefPubMedSearch in Google Scholar
  • 60 Widner B, Baier-Bitterlich G, Wede I, Wirleitner B, Fuchs D. Neopterin derivatives modulate the nitration of tyrosine by peroxynitrite.  Biochem Biophys Res Commun. 1998;  248 341-346
    CrossrefPubMedSearch in Google Scholar
  • 61 Kojima S, Icho T, Mori H, Arai T. Enhancing potency of neopterin toward B-16 melanoma cell damage induced by UV-A irradiation and its possible application for skin tumor treatment.  Anticancer Res. 1995;  15 1975-1980
    PubMedSearch in Google Scholar
  • 62 Weiss G, Fuchs D, Hausen A, Reibnegger G, Werner E R, Werner-Felmayer G, Semenitz E, Dierich M P, Wachter H. Neopterin modulates toxicity mediated by reactive oxygen and chloride species.  FEBS Lett. 1993;  321 89-92
    CrossrefPubMedSearch in Google Scholar
  • 63 Reibnegger G, Fuchs D, Murr C, Dierich M P, Pfleiderer W, Wachter H. Effects of pteridines on luminol-dependent chemiluminescence induced by chloramine-T.  Free Radic Biol Med. 1995;  18 515-523
    CrossrefPubMedSearch in Google Scholar
  • 64 Gieseg S P, Reibnegger G, Wachter H, Esterbauer H. 7,8 -dihydroneopterin inhibits low density lipoprotein oxidation in vitro. Evidence that this macrophage secreted pteridine is an anti-oxidant.  Free Radic Res. 1995;  23 123-136
    PubMedSearch in Google Scholar
  • 65 Baier-Bitterlich G, Fuchs D, Murr C, Reibnegger G, Werner-Felmayer G, Sgonc R, Bock G, Dierich M P, Wachter H. Effect of neopterin and 7,8-dihydroneopterin on tumor necrosis factor-alpha induced programmed cell death.  FEBS Lett. 1995;  364 234-238
    CrossrefPubMedSearch in Google Scholar
  • 66 Oettl K, Dikalov S, Freisleben H J, Mlekusch W, Reibnegger G. Spin trapping study of antioxidant properties of neopterin and 7,8-dihydroneopterin.  Biochem Biophys Res Commun. 1997;  234 774-778
    CrossrefPubMedSearch in Google Scholar
  • 67 Thomas A H, Lorente C, Capparelli A L, Martinez C G, Braun A M, Oliveros E. Singlet oxygen (1deltag) production by pterin derivatives in aqueous solutions.  Photochem Photobiol Sci. 2003;  2 245-250
    CrossrefPubMedSearch in Google Scholar
  • 68 Razumovitchi J A, Semenkova G N, Fuchs D, Cherenkevich S N. Influence of neopterin on the generation of reactive oxygen species in human neutrophils under the action of neopterin. FEBS Lett 2003, in press
    Search in Google Scholar
  • 69 Witko-Sarsat V, Friedlander M, Capeillere-Blandin C, Nguyen-Khoa T, Nguyen A T, Zingraff J, Jungers P, Descamps-Latscha B. Advanced oxidation protein products as a novel marker of oxidative stress in uremia.  Kidney Int. 1996;  49 1304-1313
    CrossrefPubMedSearch in Google Scholar
  • 70 Witko-Sarsat V, Friedlander M, Nguyen K hoa, Capeillere-Blandin C, Nguyen A T, Canteloup S, Dayer J M, Jungers P, Drueke T, Descamps-Latscha B. Advanced oxidation protein products as novel mediators of inflammation and monocyte activation in chronic renal failure.  J Immunol. 1998;  161 2524-2532
    PubMedSearch in Google Scholar
  • 71 Sattler W, Leblhuber F, Walli J, Widner B, Fuchs D. Cerebrospinal fluid levels of α-tocopherol and neopterin in patients with dementia.  Pteridines. 1999;  10 220-224
    PubMedSearch in Google Scholar
  • 72 Solichova D, Melichar B, Blaha V, Klejna M, Vavrova J, Palicka V, Zadak Z. Biochemical profile and survival in nonagenarians.  Clin Biochem. 2001;  34 563-569
    PubMedSearch in Google Scholar
  • 73 Hronek M, Zadak Z, Solichova D, Jandik P, Melichar B. The association between specific nutritional antioxidants and manifestation of colorectal cancer.  Nutrition. 2000;  16 189-191
    CrossrefPubMedSearch in Google Scholar
  • 74 Zvetkova E, Wirleitner B, Tram N T, Schennach H, Fuchs D. Aqueous extracts of Crinum latifolium (L.) and Camellia sinensis show immunomodulatory properties in human peripheral blood mononuclear cells.  Int Immunopharmacol. 2001;  1 2143-2150
    PubMedSearch in Google Scholar
  • 75 Neurauter G, Wirleitner B, Schroecksnadel K, Schennach H, Fuchs D. Red and white wine as well as grape juice modulate interferon-γ-induced neopterin production and tryptophan degradation in human PBMC.  Pteridines. 2003;  14 52
    PubMedSearch in Google Scholar
  • 76 Heyden S. Das Ende der Supplementierung mit antioxidantiven Vitaminen.  Aktuel Ernaehr Med. 2003;  28 113-120
    PubMedSearch in Google Scholar
  • 77 El-Khairy L, Vollset S E, Refsum H, Ueland P M. Plasma total cysteine, mortality, and cardiovascular disease hospitalizations: The Hordaland homocysteine study.  Clin Chem. 2003;  49 895-900
    PubMedSearch in Google Scholar
  • 78 Wede I, Altindag Z Z, Widner B, Wachter H, Fuchs D. Inhibition of xanthine oxidase by pterins.  Free Radic Res. 1998;  29 331-338
    PubMedSearch in Google Scholar
  • 79 Baier-Bitterlich G, Fuchs D, Zangerle R, Baeuerle P A, Werner E R, Fresser F, Überall F, Baier G, Wachter H. Trans-Activation of the HIV type 1 promoter by 7,8-dihydroneopterin in vitro.  AIDS Res Hum Retroviruses. 1997;  13 173-178
    PubMedSearch in Google Scholar
  • 80 Überall F, Werner-Felmayer G, Schubert C, Grunicke H H, Wachter H, Fuchs D. Neopterin derivatives together with cyclic guanosine monophosphate induce c-fos gene expression.  FEBS Lett. 1994;  352 11-14
    CrossrefPubMedSearch in Google Scholar
  • 81 Baier-Bitterlich G, Fuchs D, Wachter H. 7,8-dihydroneopterin upregulates interferon-gamma promoter in T cells.  Immunobiology. 1996;  196 350-355
    PubMedSearch in Google Scholar
  • 82 Hoffmann G, Frede S, Kenn S, Smolny M, Wachter H, Fuchs D, Grote J, Rieder J, Schobersberger W. Neopterin-induced tumor necrosis factor-alpha synthesis in vascular smooth muscle cells in vitro.  Int Arch Allergy Immunol. 1998;  116 240-245
    CrossrefPubMedSearch in Google Scholar
  • 83 Hoffmann G, Rieder J, Smolny M, Seibel M, Wirleitner B, Fuchs D, Schobersberger W. Neopterin-induced expression of intercellular adhesion molecule-1 (ICAM-1) in type II-like alveolar epithelial cells.  Clin Exp Immunol. 1999;  118 435-440
    CrossrefPubMedSearch in Google Scholar
  • 84 Schobersberger W, Hoffmann G, Grote J, Wachter H, Fuchs D. Induction of inducible nitric oxide synthase expression by neopterin in vascular smooth muscle cells.  FEBS Lett. 1995;  377 461-464
    CrossrefPubMedSearch in Google Scholar
  • 85 Baier-Bitterlich G, Baier G, Fuchs D, Bock G, Hausen A, Utermann G, Pavelka M, Wachter H. Role of 7,8-dihydroneopterin in T-cell apoptosis and HTLV-1 transcription in vitro.  Oncogene. 1996;  13 2281-2285
    PubMedSearch in Google Scholar

Dr. Dietmar Fuchs

Institut für medizinische Chemie und Biochemie · Leopold-Franzens-Universität Innsbruck · Boltzmann-Institut für AIDS-Forschung

Fritz-Pregl-Straße 3

6020 Innsbruck · Austria

Phone: ++ 43/512/507-3519

Fax: ++ 43/512/507-2865

Email: dietmar.fuchs@uibk.ac.at