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O₂ sensing by airway chemoreceptor-derived cells -: Protein kinase C activation reveals functional evidence for involvement of NADPH oxidase

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JOURNAL OF BIOLOGICAL CHEMISTRY 2000年第11期275卷 7684-7692页

作者： O'Kelly, I Lewis, A Peers, C Kemp, PJ Univ Leeds Sch Biomed Sci Leeds LS2 9JT W Yorkshire England Univ Leeds Cardiovasc Res Inst Leeds LS2 9JT W Yorkshire England

Accumulating evidence suggests that neuroepithelial bodies are airway O-2 sensors. Recently, we have established the H-146 small cell lung carcinoma line as a suitable model to study the biochemical basis of neuroepithelial body cell chemotransduction. Here we explore the possibility that hypoxic modulation of K+ channels is intimately linked to activity of NADPH oxidase. Graded hypoxia caused graded inhibition of whole cell K+ currents, which correlated well with membrane depolarization. Pretreatment with the phorbol esi;er, O-tetradecanoyl (TPA), inhibited K+ currents at all potentials, Although 4 alpha-phorbol 12,13-didecanoate and TPA in the presence of bisindolyhmaleimide were also able to depress K+ currents, only TPA could significantly ameliorate hypoxic depression of these currents, Thus, protein kinase C (PKC) activation modulates the sensitivity of these cells to changes in pO(2). Furthermore, because the addition of H2O2, a downstream product of NADPH oxidase, could only activate K+ currents during hypoxia (when endogenous H2O2 production is suppressed), if;appears likely that PKC modulates the affinity of NADPN oxidase for O-2 potentially via phosphorylation of the p47(phox) subunit, which is present in these cells. These data show that PKC is an important regulator of the O-2-transduction pathway and suggests that NADPH oxidase represents a significant component of the airway O-2 sensor.

关键词： 4-氨基吡啶/药理学癌小细胞细胞低氧化学感受器细胞/代谢电生理学过氧化氢/代谢离子通道闸门肺/神经支配肺/代谢膜电位/药物作用氧/药理学佛波醇酯类/药理学钾通道/代谢蛋白激酶C/代谢信号传导肿瘤细胞培养的人类

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Unusual oxidative chemistry of N^ω-hydroxyarginine and N-hydroxyguanidine catalyzed at an engineered cavity in a heme peroxidase

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JOURNAL OF BIOLOGICAL CHEMISTRY 2000年第12期275卷 8582-8591页

作者： Hirst, J Goodin, DB Scripps Res Inst Dept Mol Biol La Jolla CA 92037 USA

Heme enzymes are capable of catalyzing a range of oxidative chemistry with high specificity, depending on the surrounding protein environment. We describe here a reaction catalyzed by a mutant of cytochrome c peroxidase, which is similar but distinct from those catalyzed by nitric-oxide synthase, In the R48A mutant, an expanded water-filled cavity was created above the distal heme face. N-Hydroxyguanidine (NHG) but not guanidine was shown to bind in the cavity with K-d = 8.5 mM, and coordinate to the heme to give a low spin state. Reaction of R48A with peroxide produced a Fe(IV)=O/Trp(.+) center capable of oxidizing either NHG or N-omega-hydroxyarginine (NHA), but not arginine or guanidine, by a multi-turnover catalytic process. Oxidation of either NHG or NRA by R48A did not result in the accumulation of NO, NO2-, NO3-, urea, or citrulline, but instead afforded a yellow product with absorption maxima of 257 and 400 nm. Mass spectrometry of the derivatized NHA products identified the yellow species as N-nitrosoarginine, We suggest that a nitrosylating agent, possibly derived from HNO, is produced by the oxidation of one molecule of substrate. This then reacts with a second substrate molecule to form the observed N-nitroso products. This complex chemistry illustrates how the active sites of enzymes such as nitric-oxide synthase may serve to prevent alternative reactions from occurring, in addition to enabling those desired.

关键词：精氨酸/类似物和衍生物精氨酸/化学精氨酸/代谢催化域结晶学 X线细胞色素c过氧化物酶/遗传学细胞色素c过氧化物酶/代谢胍/代谢胍类/化学胍类/代谢血红素蛋白类/遗传学血红素蛋白类/代谢过氧化氢/代谢质谱分析法模型分子分子序列数据核磁共振生物分子氧化还原蛋白质工程重组蛋白质类/代谢分光光度法红外线底物特异性

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Evidence that the β-amyloid plaques of Alzheimer's disease represent the redox-silencing and entombment of Aβ by zinc

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JOURNAL OF BIOLOGICAL CHEMISTRY 2000年第26期275卷 19439-19442页

作者： Cuajungco, MP Goldstein, LE Nunomura, A Smith, MA Lim, JT Atwood, CS Huang, XD Farrag, YW Perry, G Bush, AI Massachusetts Gen Hosp Lab Oxidat Biol Genet Aging Unit Charlestown MA 02129 USA Univ Auckland Sch Med Dept Psychiat & Behav Sci Auckland New Zealand Case Western Reserve Univ Dept Pathol Cleveland OH 44106 USA Asahikawa Med Coll Dept Psychiat & Neurol Asahikawa Hokkaido 0788510 Japan

A beta binds Zn2+, Cu2+ and Fe3+ in vitro, and these metals are markedly elevated in the neocortex and especially enriched in amyloid plaque deposits of individuals with Alzheimer's disease (AD). Zn2+ precipitates A beta in vitro, and Cu2+ interaction with A beta promotes its neurotoxicity, correlating with metal reduction and the cell-free generation of H2O2 (A beta 1-42 > A beta 1-40 > ratA beta 1-40). Because Zn2+ is redox-inert, we studied the possibility that it may play an inhibitory role in H2O2-mediated A beta toxicity. In competition to the cytotoxic potentiation caused by coincubation with Cu2+, Zn2+ rescued primary cortical and human embryonic kidney 293 cells that were exposed to A beta 1-42, correlating with the effect of Zn2+ in suppressing Cu2+-dependent H2O2 formation from A beta 1-42. Since plaques contain exceptionally high concentrations of Zn2+, we examined the relationship between oxidation (8-OH guanosine) levels in AD-affected tissue and histological amyloid burden and found a significant negative correlation. These data suggest a protective role for Zn2+ in AD, where plaques form as the result of a more robust Zn2+ antioxidant response to the underlying oxidative attack.

关键词：阿尔茨海默病/代谢淀粉样β蛋白/化学淀粉样β蛋白/代谢脑/代谢细胞系细胞存活无细胞系统细胞培养的铜/代谢鸟苷/代谢过氧化氢/代谢免疫组织化学离子神经元/药物作用氧化还原氧/代谢锌/代谢老年人老年人 80以上动物人类中年人大鼠

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Oxidative stress triggers STAT3 tyrosine phosphorylation and nuclear translocation in human lymphocytes

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JOURNAL OF BIOLOGICAL CHEMISTRY 1999年第25期274卷 17580-17586页

作者： Carballo, M Conde, M El Bekay, R Martín-Nieto, J Camacho, MJ Monteseirín, J Conde, J Bedoya, FJ Sobrino, F Univ Seville Hosp Virgen Macarena Dept Bioquim Med & Biol Mol Fac Med E-41009 Seville Spain Univ Seville Hosp Virgen Macarena Dept Med Serv Reg Inmunol & Alergia E-41009 Seville Spain Univ Alicante Div Genet E-03080 Alicante Spain

Oxidizing agents are powerful activators of factors responsible for the transcriptional activation of cytokine-encoding genes involved in tissue injury. In this study we show evidence that STAT3 is a transcription factor whose activity is modulated by H2O2 in human lymphocytes, in which endogenous catalase had previously been inhibited. H2O2-induced nuclear translocation of STAT3 to form sequence-specific DNA-bound complexes was evidenced by immunoblotting of nuclear fractions and electrophoretic mobility shift assays, and vanadate was found to strongly synergize with H2O2. Moreover, anti-STAT3 antibodies specifically precipitated a protein of 92 kDa that becomes phosphorylated on tyrosine upon lymphocyte treatment with H2O2. Phenylarsine oxide, a tyrosine phosphatase inhibitor, and genistein, a tyrosine kinase inhibitor, cooperated and cancelled, respectively, the H2O2-promoted STAT3 nuclear translocation, Evidence is also presented, using Fe2+/Cu2+ ions, that 'OH generated from H2O2 through Fenton reactions could be a candidate oxygen reactive species to directly activate STAT3, Present data suggest that H2O2 and vanadate are likely to inhibit the activity of intracellular tyrosine phosphatase(s), leading to enhanced STAT3 tyrosine phosphorylation and hence its translocation to the nucleus, These results demonstrate that the DNA binding activity of STAT3 can be modulated by oxidizing agents and provide a framework to understand the effects of oxidative stress on the JAK-STAT signaling pathway.

关键词：砷剂/药理学细胞核/代谢铜/药理学 DNA结合蛋白质类/代谢二酰胺/药理学酶抑制剂/药理学染料木黄酮/药理学过氧化氢/代谢铁/药理学淋巴细胞/代谢氧化性应激菲绕啉类/药理学磷酰化磷酸酪氨酸/分析植物血凝素类/药理学蛋白质酪氨酸磷酸酶类/拮抗剂和抑制剂活性氧 STAT3转录因子反式激活因子类/代谢酪氨酸/代谢钒酸盐类/药理学人类

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Stable overexpression of manganese superoxide dismutase in mitochondria identifies hydrogen peroxide as a major oxidant in the AP-1-mediated induction of matrix-degrading metalloprotease-1

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JOURNAL OF BIOLOGICAL CHEMISTRY 1999年第36期274卷 25869-25876页

作者： Wenk, J Brenneisen, P Wlaschek, M Poswig, A Briviba, K Oberley, TD Scharffetter-Kochanek, K Univ Cologne Dept Dermatol D-50931 Cologne Germany Univ Dusseldorf Dept Physiol Chem D-40225 Dusseldorf Germany Univ Wisconsin Dept Pathol Madison WI 53705 USA

Reactive oxygen species (ROS) are important second messengers for the induction of several genes in a variety of physiological and pathological conditions. Here we addressed the question of whether isolated, unbalanced overexpression of the antioxidant enzyme manganese superoxide dismutase (Mn-SOD) may modulate signal transduction cascades, finally leading to connective tissue degradation, a hallmark in carcinogenesis and aging, Therefore, we generated stably Mn-SOD-overexpressing fibroblasts with an up to 4.6-fold increase in Mn-SOD activity. The Mn-SOD-overexpressing cells revealed specific resistance to the superoxide anion (O-2 radical anion)-generating agent paraquat, whereas no resistance to UVA-generated oxidative stress was found. Treatment of the Mn-SOD overexpressing cells with various ROS-generating systems resulted (due to the enhanced dismutation of superoxide anion to hydrogen peroxide) in an up to 9.5-fold increase in matrix-degrading metalloprotease-1 (MMP-1) mRNA levels, A similar increase in MMP-1 mRNA was also seen when the intracellular H2O2 concentration was increased by the inhibition of different H2O2-detoxifying pathways, Furthermore, prooxidant conditions led to a strong induction of c-jun and c-fos mRNA levels resulting in a 4-fold higher transactivation of the transcription factor AP-1 in the Mn-SOD-overexpressing cells. Collectively, we have found that enhanced Mn-SOD activity, via an unbalanced H2O2 overproduction and detoxification, induces MMP-1 mRNA levels, and this effect is at least partly mediated by the DNA recognition sequence AP-1.

关键词：细胞系胶原酶类/代谢成纤维细胞/代谢成纤维细胞/超微结构自由基清除剂/代谢过氧化氢/代谢免疫组织化学基质金属蛋白酶1 线粒体/代谢线粒体/超微结构超氧化物歧化酶/生物合成转录因子AP-1/代谢人类

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Synthesis and purification of 3-hydroxykynurenine-O-β-glucoside, a primate lens ultraviolet filter, and its application in a two-step assay for β-glucosidase activity

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ANALYTICAL BIOCHEMISTRY 2001年第1期299卷 78-83页

作者： Heckathorn, RC Dillon, J Gaillard, ER No Illinois Univ Dept Chem & Biochem De Kalb IL 60115 USA Columbia Univ Dept Ophthalmol New York NY 10032 USA

3-Hydroxykynurenine-3-O-beta -glucoside (3-HKG) functions in the primate lens as a filter of 295- 400-nm light, thereby protecting the retina from damaging UV radiation. Although extensive studies have been conducted to determine the functional role of 3-HKG in the primate lens, an efficient method for its synthesis and purification has yet to be developed. Several procedures have been reported for the synthesis of 3-HKG;however, these procedures either result in low yields or require numerous sequential reactions and purification steps. In this study, we report a two-step synthesis of 3-HKG with a one-step purification and a two- to eightfold increase in yield over previously reported methods. Additionally, an assay was developed to confirm the presence of a beta -glycosidic linkage in the purified reaction product and we propose a method by which 3-HKG can be used as a general probe of B-glucosidase activity. The assay consists of adding glucose oxidase to the 3-HKG/glucosidase solution and then allowing the hydrogen peroxide, generated from the interaction of glucose with glucose oxidase, to oxidize 3-hydroxykynurenine to xanthomattin (XAN) and 4,6-dihydroxyquinolinequinone carboxylic acid (DHQCA). Both XAN and DHQCA absorb strongly between 400 and 500 nm and the color change of the solution can be seen by eye. In addition, XAN fluoresces in the visible region with lambda (max) = 527 nm. (C) 2001 Elsevier Science Elsevier Science.

关键词：葡萄糖/代谢葡糖氧化酶/代谢葡糖苷类/化学合成葡糖苷类/化学葡糖苷类/分离和提纯过氧化氢/化学过氧化氢/代谢晶体/解剖学和组织学恶嗪类/化学氧化还原色素类生物学/化学灵长目醌类/化学紫外线呫吨类 β葡糖苷酶类/分析动物人类

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Ethanol and arachidonic acid increase α2(I) collagen expression in rat hepatic stellate cells overexpressing cytochrome P450 2E1 -: Role of H₂O₂ and cyclooxygenase-2

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JOURNAL OF BIOLOGICAL CHEMISTRY 2000年第26期275卷 20136-20145页

作者： Nieto, N Greenwel, P Friedman, SL Zhang, F Dannenberg, AJ Cederbaum, AI Mt Sinai Sch Med Dept Biochem & Mol Biol New York NY 10029 USA Mt Sinai Sch Med Dept Med & Liver Dis New York NY 10029 USA Cornell Univ Weill Med Coll Dept Cardiothorac Surg New York NY 10021 USA Cornell Univ Weill Med Coll Dept Med New York NY 10021 USA Strang Canc Prevent Ctr New York NY 10021 USA

The ability of ethanol and arachidonic acid (AA), as inducers of oxidative stress and key factors in alcoholic liver disease, to up-regulate alpha 2 collagen type I (COL1A2) gene expression was studied in a hepatic stellate cell line overexpressing the ethanol-inducible cytochrome P450 2E1 (CYP2E1) (E5 cells). A time- and dose-dependent induction in COL1A2 mRNA by ethanol or AA was observed that was prevented by diallylsulfide, a CYP2E1 inhibitor, Nuclear run-on experiments showed transcriptional activation of the COL1A2 gene by ethanol and Ak Catalase abrogated the increase in COL1A2 mRNA suggesting an H2O2-dependent mechanism. Cyclooxygenase-2 (COX-2) levels and production of prostaglandin E-2 upon addition of AA were elevated in the E5 cells. Incubation with NS-398, a COX-2 inhibitor, blocked the effect of AA, but not of ethanol, on COL1A2 expression suggesting that CYP2E1 activates COX-2 expression, and the oxidation of AA by COX-2 is responsible for the increase in COL1A2. Activity of a reporter construct driven by -378 base pairs of the proximal promoter region of the COL1A2 gene increased in E5 but not control cells and was further increased by ethanol or AA. These experiments link CYP2E1-dependent oxidative stress to induction of COX-2 and the actions of ethanol and AA on activation of collagen gene expression in hepatic stellate cells.

关键词：烯丙化合物/药理学抗氧化剂/药理学花生四烯酸/药理学印迹法 RNA 印迹法蛋白质细胞系胶原/生物合成环氧化酶2 环氧化酶2抑制剂环加氧酶抑制药/药理学细胞色素P450CYP2E1/拮抗剂和抑制剂细胞色素P450CYP2E1/代谢剂量效应关系药物电泳聚丙烯酰氨凝胶乙醇/药理学基因报告过氧化氢/代谢同工酶类/代谢肝/药物作用模型生物学硝基苯甲酸盐/药理学氧化性应激前列腺素内过氧化物合酶类/代谢前列腺素E类/生物合成 RNA 信使/药物作用重组蛋白质类/代谢硫化物/药理学磺胺类/药理学时间因素转录遗传/药物作用动物大鼠

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Reactive oxygen species activate p90 ribosomal S6 kinase via Fyn and Ras

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JOURNAL OF BIOLOGICAL CHEMISTRY 2000年第3期275卷 1739-1748页

作者： Abe, JI Okuda, M Huang, QH Yoshizumi, M Berk, BC Univ Rochester Sch Med & Dent Cardiol Unit Cardiovasc Res Ctr Rochester NY 14642 USA Kobe Univ Sch Med Dept Internal Med Div 1 Kobe Hyogo 6500017 Japan

Reactive oxygen species and growth factors stimulate similar intracellular signal transduction events including activation of Src kinase family members and extracellular signal-regulated kinases (ERK1/2), A potentially important downstream effector of Src and ERK1/2 is p90 ribosomal S6 kinase (p90RSK), which plays an important role in cell growth by activating several transcription factors as well as the Na+/H+ exchanger. In the present study, we determined whether H2O2 activates p90RSK to gain insight into signal transduction mechanisms activated by reactive oxygen species. H2O2 (200 mu M) Stimulated ERK1/2 and p90RSK activity in lymphocytes, endothelial cells, and fibroblasts. The MEK-1 inhibitor, PD98059 (30 mu M), inhibited H2O2-mediated activation of ERK1/2 but not of p90RSK, An essential role for Fyn and Ras in p90RSK activation was suggested by five findings. 1) The tyrosine kinase inhibitor, herbimycin A and the specific Src kinase family inhibitor, PP1, blocked p90RSK activation by H2O2 in a concentration-dependent manner. 2) p90RSK activation by H2O2 was significantly reduced in fibroblasts derived from transgenic mice deficient in Fyn, but not c-Src. 3) H2O2 rapidly activated Ras (peak at 2-5 min), which preceded p90RSK activation (peak at 20 min). 4) Dominant negative Res completely blocked H2O2-induced activation of p90RSK. 5) In Fyn-/- fibroblasts, activation of Ras by H2O2 was significantly attenuated. These results show essential roles for Fyn and Ras in H2O2-mediated activation of p90RSK and establish redox-sensitive regulation of Ras and p90RSK as a new function for Fyn.

关键词：钙/代谢细胞培养的剂量效应关系药物酶抑制剂/药理学成纤维细胞/代谢过氧化氢/代谢 Jurkat细胞丝裂原活化蛋白激酶1/代谢丝裂原活化蛋白激酶3 丝裂原激活蛋白激酶类/代谢氧化性应激磷酰化原癌基因蛋白质类/代谢原癌基因蛋白质c-fyn 活性氧/代谢核糖体蛋白质S6激酶类/代谢信号传导 ras蛋白质类/代谢 src族激酶类/拮抗剂和抑制剂动物人类小鼠

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Laccase-catalyzed oxidation of Mn²⁺ in the presence of natural Mn³⁺ chelators as a novel source of extracellular H₂O₂ production and its impact on manganese peroxidase

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APPLIED AND ENVIRONMENTAL MICROBIOLOGY 2002年第7期68卷 3514-3521页

作者： Schlosser, D Höfer, C UFZ Helmholtz Ctr Environm Res Ctr Environm Res Leipzig Halle Microbiol Subterr Aquact Syst Grp D-06120 Halle An Der Saale Germany Biotype Gesell Mol Biol Analyt AG D-01109 Dresden Germany

A purified and electrophoretically homogeneous blue laccase from the litter-decaying basidiomycete Stropharia rugosoannulata with a molecular mass of approximately 66 kDa oxidized Mn2+ to Mn3+, as assessed in the presence of the Mn chelators oxalate, malonate, and pyrophosphate. At rate-saturating concentrations (100 mM) of these chelators and at pH 5.0, Mn3+ complexes were produced at 0.15, 0.05, and 0.10 mumol/min/mg of protein, respectively. Concomitantly, application of oxalate and malonate, but not pyrophosphate, led to H2O2 formation and tetranitromethane (TNM) reduction indicative for the presence of superoxide anion radical. Employing oxalate, H2O2 production, and TNM reduction significantly exceeded those found for malonate. Evidence is provided that, in the presence of oxalate or malonate, laccase reactions involve enzyme-catalyzed Mn2+ oxidation and abiotic decomposition of these organic chelators by the resulting Mn3+, which leads to formation of superoxide and its subsequent reduction to H2O2. A partially purified manganese peroxidase (MnP) from the same organism did not produce Mn 31 complexes in assays containing 1 mM Mn2+ and 100 mM oxalate or malonate, but omitting an additional H2O2 source. However, addition of laccase initiated MnP reactions. The results are in support of a physiological role of laccase-catalyzed Mn2+ oxidation in providing H2O2 for extracellular oxidation reactions and demonstrate a novel type of laccase-MnP cooperation relevant to biodegradation of lignin and xenobiotics.

关键词：伞菌目/酶学催化作用螯合剂/代谢过氧化氢/代谢漆酶锰/代谢氧化还原氧化还原酶类/代谢氧/代谢过氧化物酶类/代谢

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Overexpression of catalase in cytosolic or mitochondrial compartment protects HepG2 cells against oxidative injury

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JOURNAL OF BIOLOGICAL CHEMISTRY 1999年第37期274卷 26217-26224页

作者： Bai, JX Rodriguez, AM Melendez, JA Cederbaum, AI Mt Sinai Sch Med Dept Biochem & Mol Biol New York NY 10029 USA Albany Med Coll Dept Biochem & Mol Biol Albany NY 12208 USA

HepG2 cells were transfected with vectors containing human catalase cDNA and catalase cDNA with a mitochondrial leader sequence to allow comparison of the effectiveness of catalase overexpressed in the cytosolic or mitochondrial compartments to protect against oxidant-induced injury. Overexpression of catalase in cytosol and in mitochondria was confirmed by Western blot, and activity measurement and stable cell lines were established. The intracellular level of H2O, induced by exogenously added H2O2 or antimycin A was lower in C33 cell lines overexpressing catalase in the cytosol and mC5 cell lines overexpressing catalase in the mitochondria as compared with Hp cell lines transfected with empty vector. Cell death caused by H2O2, antimycin A, and menadione was considerably suppressed in both the mC5 and C33 cell lines. C33 and mC5 cells were also more resistant to apoptosis induced by H2O2 and to the loss of mitochondrial membrane potential induced by H2O2 and antimycin A. In view of the comparable protection by catalase overexpressed in the cytosol versus the mitochondria, catalase produced in both cellular compartments might act as a sink to decompose H2O2 and move diffusable H2O2 down its concentration gradient. The present study suggests that catalase in cytosol and catalase in mitochondria are capable of protecting HepG2 cells against cytotoxicity or apoptosis induced by oxidative stress.

关键词：抗霉素A/药理学过氧化氢酶/代谢胞质溶胶/酶学 DNA碎片裂过氧化氢/代谢膜电位线粒体/酶学线粒体/生理学氧化性应激肿瘤细胞培养的维生素K/药理学人类

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