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PubMed1977

Methoxytyrosine formation as an indicator of catechol-O-methyltransferase activity in rat liver in vivo.

The O-methyl derivative methoxytyrosine accumulated rapidly in rat liver after an intraperitoneal injection of L-dopa (50 mg/kg) in combination with 3-hydroxybenzylhydrazine, an inhibitor of the aromatic amino acid decarboxylase. Methoxytyrosine levels reached a plateau 40--60 min after i.p. injection of L-dopa, of which the tissue concentration declined monoexponentially. Injection of various doses of L-dopa revealed that methoxytyrosine formation was saturable and followed enzyme kinetics in rat liver. The catechol-O-methyltransferase inhibitors pyrogallol, tropolone and alpha-propyldopacetamide as well as the inhibitor of the aromatic amino acid decarboxylase benserazide inhibited the formation of methoxytyrosine dose-dependently and concomitantly increased the tissue concentration of dopa. The accumulation of methoxytyrosine from exogeneously applied L-dopa appears to be a reliable indicator of the in vivo activity of catechol-O-methyltransferase.

Amino Acids↗
PubMed1978

Iron hydroxide: model for enzymes that oxidize proteins.

The particles of an iron hydroxide sol were found to be a suitable model for protein-oxidizing enzymes such as peroxidase and polyphenol oxidase. In addition to small molecules such as pyrogallol, human serum proteins, albumin and gamma-globulin, are shown to be substrates of the oxidizing model. The activity is markedly increased by the addition of small amounts of copper to the iron in the particles of the sol. The size and molecular weight of the enzyme model, as well as the number of active centers were determined.

Blood Proteins↗
PubMed1981

Comparative studies of the effects of 5-hydroxytryptamine and noradrenaline on the rat anococcygeus muscle.

The effects of 5-hydroxytryptamine (5HT) and noradrenaline (NA) have been studied on rat anococcygeus muscle. 1. 5HT and NA produced a dose-dependent contraction of rat anococcygeus muscle. Cyproheptadine (1.0 X 10(-6) M), a specific 5HT receptor blocker, failed to inhibit the responses to either 5HT or NA. 2. However, phentolamine, a specific alpha receptor antagonist competitively blocked the responses to 5HT and NA. 3. The responses to 5HT were inhibited in the reserpinized (5 mg/kg i.p. 24 h) and 6-hydroxydopamine (6-OHDA) pre-treated preparations. 6-OHDA produced a leftward shift of the dose-response curve of NA. Reserpine pre-treatment potentiated lower doses of NA and the threshold dose of NA was significantly decreased. 4. Nialamide (2.2 x 10(-6) M), the mono-amine oxidase inhibitor produced a significant leftward shift of the dose-response curve of both 5HT and NA. Pyrogallol (2.3 x 10(-5) M), the catechol-o-methyl transferase inhibitor also potentiated the responses to both 5HT and NA, but the potentiation was significant at lower doses of 5HT and NA. 5. Our data suggest that 5HT- and NA-induced contractions in rat anococcygeus muscle are mediated through common alpha adrenoceptors. 5HT actions are probably indirect, mediated through the release of NA.

Animals↗
PubMed2003

High glucose impairs superoxide production from isolated blood neutrophils.

OBJECTIVE: Superoxide (O(2)(-)), a key antimicrobial agent in phagocytes, is produced by the activity of NADPH oxidase. High glucose concentrations may, however, impair the production of O(2)(-) through inhibition of glucose-6-phosphate dehydrogenase (G6PD), which catalyzes the formation of NADPH. This study measured the acute effects of high glucose or the G6PD inhibitor dehydroepiandrosterone (DHEA) on the production of O(2)(-) from isolated human neutrophils. DESIGN: Laboratory studies of short-term cultures of neutrophil granulocytes. PARTICIPANTS: Healthy subjects. INTERVENTIONS: Neutrophils were isolated from peripheral blood and incubated for 1 h in Krebs-Ringer buffer containing 5, 10, or 25 mM glucose, 5 mM glucose with 0, 5, or 20 mM mannitol, or 5 mM glucose with 0, 1, 10, or 100 micro M DHEA. O(2)(-) production was induced by N-formyl-methionyl-leucyl-phenylalanine and measured by the cytochrome c reduction assay. Potential scavenging of O(2)(-) by glucose, mannitol, or DHEA was assessed in a cell free system using the pyrogallol assay. MEASUREMENTS AND RESULTS: Incubation of neutrophils with glucose dose-dependently reduced O(2)(-) production, which was 50% decreased at 25 mM glucose. Also DHEA reduced the production of O(2)(-) dose-dependently, whereas production rates were unaffected by mannitol. Neither glucose, mannitol, nor DHEA scavenged O(2)(-). CONCLUSIONS: High extracellular glucose concentrations acutely reduce O(2)(-) production from activated neutrophils possibly through inhibition of G6PD. If this occurs in vivo, microbial killing by neutrophils may be impaired during acute hyperglycemia, as observed after major surgery, trauma, or severe infection.

Analysis of Variance↗
PubMed1997

Desulfovibrio inopinatus, sp. nov., a new sulfate-reducing bacterium that degrades hydroxyhydroquinone.

A new sulfate-reducing bacterium was isolated from marine sediment with hydroxyhydroquinone (1,2,4-trihydroxybenzene) as the sole electron and carbon source. Strain HHQ 20 grew slowly with doubling times of > 20 h and oxidized hydroxyhydroquinone, lactate, pyruvate, ethanol, fructose, and ribose incompletely to acetate and carbon dioxide, with concomitant reduction of sulfate to sulfide. Cells were large, vibrio-shaped, and gram-negative with a G+C content of 49.7 mol%, and contained desulfoviridin. Based on analysis of the 16S rRNA sequence, strain HHQ 20 was found to be related to the genus Desulfovibrio but formed a separate line, thus justifying the establishment of a new species within this genus. Hydroxyhydroquinone was the only aromatic compound utilized among numerous hydroxybenzoates, hydroxybenzenes, methoxybenzoates, and methoxybenzenes tested, suggesting that phloroglucinol and resorcinol are not degradation intermediates. Cell-free extracts of strain HHQ 20 did not contain pyrogallol-phloroglucinol transhydroxylase activity. First experiments indicated that this strain uses a new reductive pathway for anaerobic hydroxyhydroquinone degradation.

Acetates↗
PubMed2002

Purification and characterization of an extracellular laccase from the edible mushroom Lentinula edodes, and decolorization of chemically different dyes.

A laccase (EC 1.10.3.2) was isolated from the culture filtrate of Lentinula edodes. The enzyme was purified to a homogeneous preparation using hydrophobic, anion-exchange, and size-exclusion chromatographies. SDS-PAGE analysis showed the purified laccase, Lcc 1, to be a monomeric protein of 72.2 kDa. The enzyme had an isoelectric point of around pH 3.0. The optimum pH for enzyme activity was around 4.0, and it was most active at 40 degrees C and stable up to 35 degrees C. The enzyme contained 23.8% carbohydrate and some copper atoms. The enzyme oxidized 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) diammonium salt, p-phenylendiamine, pyrogallol, guaiacol, 2,6-dimethoxyphenol, catechol, and ferulic acid, but not veratryl alcohol, tyrosine, and beta-(3,4-dihydroxyphenyl) alanine. The N-terminal amino acid sequence of Lcc 1 showed close homology to the N-terminal sequences determined for laccases from Phlebia radiata, Trametes villosa, and Trametes versicolor, but only low similarity was observed to a previously reported laccase from L. edodes. Lcc 1 was effective in the decolorization of chemically different dyes - Remazole Brilliant Blue R, Bromophenol Blue, methyl red, and Naphtol Blue Black - without any mediators, but the decolorization of two dyes - red poly(vinylamine)sulfonate-anthrapyridone dye and Reactive Orange 16 - did require some redox mediators.

Color↗
PubMed1996

Nitric oxide donors suppress erythropoietin production in vitro.

Many inflammatory diseases are associated with a hypoproliferative anaemia. Patients with this anaemia often present with serum erythropoietin (EPO) concentrations that are too low for the degree of their anaemia. Proinflammatory cytokines, in addition to their inhibitory effects on proliferation of erythroid progenitors, could contribute to the pathogenesis of this anaemia by reducing EPO production. Because several cytokines stimulate nitric oxide (NO) synthase we propose that nitric oxide might mediate the suppression of EPO production during inflammation. In order to test this hypothesis we investigated the effects of NO donors on 24-h hypoxia-induced EPO production in the hepatocellular carcinoma cell line HepG2. Following application of the NO donors sodium nitroprusside (SNP), 3-morpholinosydnonimine (SIN-1), and S-nitroso-N-acetyl-D,L-penicillamine (SNAP), EPO production was dose-dependently reduced: compared to the untreated control EPO production was lowered by 89% with SNP (1000 microM), by 66% with SIN-1 (1000 microM), and by 72% with SNAP (500 microM). In contrast, 8-bromo-cGMP did not inhibit EPO formation. Since pyrogallol (300 microM) and H2O2 (250 microM) showed a comparable suppression of EPO synthesis, we propose that NO might affect EPO production either by a similar direct influence on the cellular redox state or via increasing the cellular content of reactive oxygen species.

Carcinoma, Hepatocellular↗
PubMed2004

Heme-copper/dioxygen adduct formation relevant to cytochrome c oxidase: spectroscopic characterization of [(6L)FeIII-(O2(2-))-CuII]+.

In the further development and understanding of heme-copper dioxygen reactivity relevant to cytochrome c oxidase O(2)-reduction chemistry, we describe a high-spin, five-coordinate dioxygen (peroxo) adduct of an iron(II)-copper(I) complex, [((6)L)Fe(II)Cu(I)](BArF(20)) (1), where (6)L is a tetraarylporphyrinate with a tethered tris(2-pyridylmethyl)amine chelate for copper. Reaction of 1 with O(2) in MeCN affords a remarkably stable [t(1/2) (rt; MeCN) approximately 60 min] adduct, [((6)L)Fe(III)-(O(2) (2-))-Cu(II)](+) (2) [EPR silent; lambda(max)=418 (Soret), 561 nm], formulated as a peroxo complex based on manometry (1:O(2)=1:1; spectrophotometric titration, -40 degrees C, MeCN), mass spectrometry {MALDI-TOF-MS: (16)O(2), m/z 1191 ([((6)L)Fe(III)-((16)O(2) (2-))-Cu(II)](+)); (18)O(2), m/z 1195}, and resonance Raman spectroscopy (nu((O-O))=788 cm(-1); Delta(16)O(2)/(18)O(2)=44 cm(-1); Delta(16)O(2)/(16/18)O(2)=22 cm(-1)). (1)H and (2)H NMR spectroscopy (-40 degrees C, MeCN) reveals that 2 is the first heme-copper peroxo complex which is high-spin, with downfield-shifted pyrrole resonances (delta(pyrrole)=75 ppm, s, br) and upfield shifted peaks at delta= -22, -35, and -40 ppm, similar to the pattern observed for the mu-oxo complex [((6)L)Fe(III)-O-Cu(II)](BAr(F)) (3) (known S=2 system, antiferromagnetically coupled high-spin Fe(III) and Cu(II)). The corresponding magnetic moment measurement (Evans method, CD(3)CN, -40 degrees C) also confirms the S=2 spin state, with mu(B)=4.9. Structural insights were obtained from X-ray absorption spectroscopy, showing Fe-O (1.83 A) and Cu-O (1.882 A) bonds, and an Fe...Cu distance of 3.35(2) A, suggestive of a mu-1,2-peroxo ligand present in 2. The reaction of 2 with cobaltocene gives 3, differing from the observed full reduction seen with other heme-Cu peroxo complexes. Finally, thermal decomposition of 2 yields 3, with concomitant release of 0.5 mol O(2) per mol 2, as confirmed quantitatively by an alkaline pyrogallol dioxygen scavenging solution.

Binding Sites↗
PubMed2005

Reactions of peroxynitrite and nitrite with organic molecules and hemoglobin.

In this work, the reactions of nitrite (NO2-) and peroxynitrite (ONOO-) with organic molecules as well as with hemoglobin (Hb) were examined and the potential interference with the detection of hydrogen peroxide and Hb was investigated. ONOO- at low concentrations (35-140 microM) induced a concentration-dependent oxidation of o-phenylenediamine and guaiacol, and this process can be improved by the addition of Hb in a concentration-dependent manner. This enhancing effect of Hb was possibly due to the formation of such highly reactive species as ferrylHb during the reaction of ONOO- and Hb. NO2- also oxidized the aromatic amine o-phenylenediamine, but its efficiency was much lower than that of ONOO-. A 300-fold excess of NO2- over hydrogen peroxide inhibited the oxidation of Pyrogallol Red mediated by hydrogen peroxide and Hb, which was due in part to the reaction of NO2- with Hb ferryl species compound I and compound II and the phenoxyl radical. These data suggest that ONOO- and NO2- can interfere with the detection of hydrogen peroxide. The overestimation or underestimation of the hydrogen peroxide detected is dependent upon the organic molecule utilized for detection and the relative rate of NO2-, superoxide, and ONOO- generation.

Guaiacol↗
PubMed1995

A comparison between two screening methods for detection of microproteinuria.

OBJECTIVE: We compared two screening tests for microproteinuria with 24-hour quantitative measurements to determine which method is better at predicting clinically significant proteinuria. STUDY DESIGN: We obtained 690 24-hour urine collections from both low- and high-risk patients seen for prenatal care. Qualitative screening for microproteinuria on the basis of the protein-error-of-indicators principle (Ames Multistix 10SG and Micro-bumintest, Miles Diagnostic Division, Elkhart, Ind.) was done by the same investigator (C.S.). Quantitative assay was done by use of pyrogallol red-molybdate for total protein and by radioimmunoassay for albumin. RESULTS: The Micro-bumintest had a sensitivity of 87% compared with 36% for the Multistix 10SG. It also had a higher specificity and higher positive and negative predictive values. The Micro-bumintest was a better screening test in patients with significant protein excretion (> 300 mg/24 hours). CONCLUSION: The Micro-bumintest has a much higher sensitivity and a lower false-negative rate than does the Multistix 10SG. Our data support the Micro-bumintest as a better screening test for clinically significant proteinuria.

Albumins↗
PubMed1983

Reduction of laccase type 1 copper by 3,4-dihydroxyphenylalanine and other catechol derivatives.

3,4-Dihydroxyphenylalanine (DOPA) is not a preferred substrate of Rhus vernicifera laccase, as rate constants for the anaerobic reduction of the type 1 cupric atom by L-DOPA (6.3 X 10(1) M-1 s-1), D-DOPA (2.6 X 10(1) M-1 s-1), and L-DOPA methyl ester (2.6 X 10(1) M-1 s-1) are considerably smaller than k1 (catechol) (7 X 10(2) M-1 s-1) and rate constants characteristic of numerous other nonphysiological organic substrates (25 degrees C, pH 7.0, I = 0.5 M). The reactions of DOPA derivatives with laccase are unique, however, in that a two-term rate law pertains: kobsd = k0 + k1[phenol]; k0(L-DOPA) = 7 X 10(-2) s-1. The reactivities of other catechol derivatives (pyrogallol, gallic acid, and methyl gallate) with laccase type 1 copper were also examined.

Catechols↗
PubMed1992

Purification and characterization of a catalase-peroxidase from the fungus Septoria tritici.

Three classes of heme proteins, commonly designated hydroperoxidases, are involved in the metabolism of hydrogen peroxide: catalases, peroxidases, and catalase-peroxidases. While catalases and peroxidases are widely spread in animals, plants, and microorganisms, catalase-peroxidases were characterized only in prokaryotes. We report here, for the first time, on a catalase-peroxidase in a eukaryotic organism. The enzyme was purified from the fungal wheat pathogen Septoria tritici, and is one of three different hydroperoxidases synthesized by this organism. The S. tritici catalase-peroxidase, designated StCP, is similar to the enzymes previously isolated from the bacteria Rhodobacter capsulatus, Escherichia coli, and Klebsiella pneumoniae, although it is significantly more sensitive to denaturing conditions. In addition to its catalatic activity StCP catalyzes peroxidatic activity with o-dianisidine, diaminobenzidine, pyrogallol, NADH, and NADPH as electron donors. The enzyme is a tetramer with identical subunits of 61,000 Da molecular weight. StCP shows a typical high-spin ferric heme spectrum with a Soret band at 405 nm and a peak at 632 nm, and binding of cyanide causes a shift of the Soret band to 421 nm, the appearance of a peak at 537 nm, and abolition of the peak at 632 nm. Reduction with dithionite results in a decrease in the intensity of the Soret band and its shift to 436 nm, and in the appearance of a peak at 552 nm. The pH optimum is 6-6.5 and 5.4 for the catalatic and peroxidatic activities, respectively. Fifty percent of the apparent maximal activity is reached at 3.4 mM and 0.26 mM for the catalatic and peroxidatic activities, respectively. The enzyme is inactivated by ethanol/chloroform, and is inhibited by KCN and NaN3, but not by the typical catalase inhibitor 3-amino-1,2,4-triazole.

Catalase↗
PubMed1988

Inactivation of peroxidases of rat bone marrow by repeated administration of propylthiouracil is accompanied by a change in the heme structure.

Myeloperoxidase and eosinophil peroxidase were isolated from the bone marrow cells of rats treated with or without propylthiouracil (PTU) which caused bone marrow depression. PTU treatment decreased the activity of myeloperoxidase but not of eosinophil peroxidase using guaiacol as the electron donor. However, when KI,N-N'-dimethyl-p-phenylenediamine and pyrogallol were used as the electron donor, the activity of only eosinophil peroxidase was inhibited by PTU treatment. EPR spectra indicated that the structure of myeloperoxidase surrounding the heme iron changed from a rhombic form into an axial one by the repeated administration of PTU. Therefore, the inactivation of peroxidases by PTU treatment was accompanied by an alteration of their structures surrounding the heme.

Animals↗
PubMed1990

High density lipoprotein is a scavenger of superoxide anions.

Present work describes a new property of HDL to act as a scavenger of O2- free radicals in vitro. This lipoprotein prevents both enzymic and non-enzymic generation of O2- anions as evidenced by inhibition of xanthine oxidase, peroxidase, peroxidation of pyrogallol and phenazine methosulphate-NADH reaction. Ascorbate stimulated MDA formation in microsomes has been shown to be suppressed by HDL and these effects are comparable with that of BHA.

Animals↗
PubMed1990

Extragranular storage of the neuron blocking agent meta-iodobenzylguanidine (MIBG) in human neuroblastoma cells.

Human SK-N-SH neuroblastoma cells accumulate and store the adrenal imaging agent metaiodobenzylguanidine (MIBG) with minor involvement of specialized cytoplasmic storage granules (Smets LA et al., Active uptake and extravesicular storage of meta-iodo-benzylguanidine in human neuroblastoma SK-N-SH cells. Cancer Res 49: 2941-2944, 1989). In the present study the mechanism of extravesicular MIBG retention was investigated and compared with granular storage of MIBG and norepinephrine (NE) in PC-12 pheochromocytoma cells. SK-N-SH cells concentrated both MIBG and NE by neuron-specific Uptake-1 but long-term retention was only observed with MIBG. Retention of accumulated NE was, however, promoted by inhibition of intracellular catecholamine degradation with pyrogallol. Drug release by controlled cell permeabilization and by KCl-induced exocytosis indicated that MIBG was mainly stored as freely diffusible, cytoplasmic molecules. SK-N-SH cells were depleted from stored MIBG by the Uptake-1 inhibitor imipramine but poorly so by the granule-depleting drug reserpine. Conversely, PC-12 cells were depleted by reserpine but insensitive to imipramine. The data suggest that extravesicular retention of MIBG in SK-N-SH cells is not based on intracellular sequestration but is solely due to efficient re-uptake of accumulated drug after leaking from the cells. The accumulation of MIBG in SK-N-SH cells, reflecting "pure" Uptake-1, appears to be a powerful system for exploring various cellular and molecular aspects of catecholamine uptake.

3-Iodobenzylguanidine↗
PubMed1992

Molsidomine inhibits the chemoattractant-induced respiratory burst in human neutrophils via a no-independent mechanism.

3-Morpholino-sydnonimine (SIN-1) is a NO-releasing compound which mimics the effects of cGMP through activation of soluble guanylyl cyclase. Its prodrug, molsidomine (SIN-10), does not release NO but does modulate various cell functions. These findings prompted us to study the effects of SIN-10 and SIN-1 on the respiratory burst in human neutrophils. SIN-10 was more effective than SIN-1 in inhibiting superoxide anion (O2-) formation induced by N-formyl-L-methionyl-L-leucyl-L-phenylalanine (fMet-Leu-Phe) and by C5a. The effects of SIN-1 and SIN-10 on O2- formation were additive or less than additive, indicating the sydnonimines acted through a common mechanism. The sydnonimines showed no effect on O2- formations induced by gamma-hexachlorocyclohexane, arachidonic acid and a phorbol ester. They did not inhibit O2- formation induced by xanthine oxidase, by autoxidation of pyrogallol and in a cell-free system from HL-60 leukemic cells. Neutrophils did not convert SIN-10 to SIN-1 as assessed by O2 consumption which accompanies NO release from SIN-1. The cell-permeant analogue of cGMP, N2,2'-O-dibutyryl guanosine 3':5'-monophosphate (Bt2cGMP), and SIN-10 but not SIN-1 inhibited fMet-Leu-Phe-induced O2 consumption. SIN-1 and SIN-10 slightly enhanced agonist binding to formyl peptide receptors, whereas Bt2cGMP was inhibitory. The sydnonimines did not affect GTP hydrolysis of heterotrimeric regulatory guanine nucleotide-binding proteins in HL-60 membranes. SIN-1 but not SIN-10 stimulated ADP-ribosylation of a 39-kDa protein in the cytosol of HL-60 cells. SIN-10 reduced fMet-Leu-Phe-induced rises in cytosolic Ca2+ concentration in neutrophils. These data suggest that SIN-10 inhibits the respiratory burst via a NO-independent mechanism which may involve inhibition of rises in cytosolic Ca2+ concentration.

Acetates↗
PubMed1995

A new synthetic flavonoid protects endothelium-derived relaxing factor-induced relaxation in rabbit arteries in vitro: evidence for superoxide scavenging.

A new synthetic flavone derivative, 6,7-dimethoxy-8-methyl-3',4',5-trihydroxyflavone, was studied for its capacity to protect the acetylcholine-induced relaxation of rabbit ear and cerebral arteries from inhibition by superoxide anion. This property was evaluated via two types of in vitro experiments, using rabbit ear or basilar arteries mounted in organ baths equipped for isometric tension measurement. When a high level of superoxide anion was generated by adding 3 x 10(-4) M pyrogallol to the bath, the relaxation to acetylcholine was substantially inhibited. This inhibition was significantly reversed by both superoxide dismutase (25 and/or 50 U/mL) and the flavonoid (3 x 10(-6) M and/or 10(-5) M) in both types of arteries. In the presence of the basal level of superoxide anion, the responses to acetylcholine were significantly potentiated by the flavonoid (10(-5) M) in the ear but not the basilar artery. Thus this flavonoid protects endothelium-dependent relaxation from high levels of superoxide anion possibly by scavenging superoxide anion and may have a certain therapeutic value as an agent capable of promoting natural vasodilatation.

Animals↗
PubMed1993

Determination of proteins by a reverse biuret method combined with the copper-bathocuproine chelate reaction.

A method of protein determination has been developed which combines the biuret reaction and the copper(I)-bathocuproine chelate reaction. Protein in the specimen forms a Cu(2+)-protein chelate complex (biuret reaction) during the first step. Excess Cu2+ is reduced to Cu+ by ascrobic acid, allowing the Cu+ to form a Cu(+)-bathocuproine chelate complex during the second step. The amount of Cu(+)-bathocuproine chelate complex formed is inversely proportional to the protein concentration. The sensitivity (epsilon = 1.4 x 10(6) 1.mol-1.cm-1 against human albumin) of this method was higher than that of the original Lowry (9.8 x 10(5)), pyrogallol red (1.0 x 10(6)) and commercially available Coomassie Brilliant Blue G.250 methods (6.7 x 10(5)). The color intensities of human gamma-globulin, human globulin (fractions IV-1 and IV-4), bovine albumin, egg albumin and horse gamma-globulin against human albumin (100%) ranged from 92 to 101%. The results obtained with the present method (y) correlated well with those determined by the biuret method (r = 0.998, y = 0.98 chi - 0.002, x = 1.31, y = 1.29 g/l) in 30 diluted sera. These results confirm that this assay is similar in sensitivity to the original Lowry method, is rapid and has similar reactivity to each of the various proteins in biological fluids.

Ascorbic Acid↗