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1
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Content available

Cysteine-rich receptor-like kinases (CRK) in ROS signalling in Arabidopsis thaliana

100%
Gauthier A., Idanheimo N., Salojarvi J., Wrzaczek M., Kangasjarvi J.
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
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2013
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tom 94
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nr 2
2

Enzymatic oxidation of phthalazine with guinea pig liver aldehyde oxidase and liver slices: inhibition by isovanillin

100%
Panoutsopoulos G. I., Beedham C.
Acta Biochimica Polonica
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2004
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tom 51
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nr 4
The enzymes aldehyde oxidase and xanthine oxidase catalyze the oxidation of a wide range of N-heterocycles and aldehydes. These enzymes are widely known for their role in the metabolism of N-heterocyclic xenobiotics where they provide a pro­tective barrier by aiding in the detoxification of ingested nitrogen-containing heterocycles. Isovanillin has been shown to inhibit the metabolism of aromatic alde­hydes by aldehyde oxidase, but its inhibition towards the heterocyclic compounds has not been studied. The present investigation examines the oxidation of phthalazine in the absence and in the presence of the inhibitor isovanillin by partially purified aldehyde oxidase from guinea pig liver. In addition, the interaction of phthalazine with freshly pre­pared guinea pig liver slices, both in the absence and presence of specific inhibitors of several liver oxidizing enzymes, was investigated. Aldehyde oxidase rapidly converted phthalazine into 1-phthalazinone, which was completely inhibited in the presence of isovanillin (a specific inhibitor of aldehyde oxidase). In freshly prepared liver slices, phthalazine was also rapidly converted to 1-phthalazinone. The formation of 1-phthalazinone was completely inhibited by isovanillin, whereas disulfiram (a specific inhibitor of aldehyde dehydrogenase) only inhibited 1-phthalazinone formation by 24% and allopurinol (a specific inhibitor of xanthine oxidase) had little effect. Therefore, isovanillin has been proved as an inhib­itor of the metabolism of heterocyclic substrates, such as phthalazine, by guinea pig liver aldehyde oxidase, since it had not been tested before. Thus it would appear from the inhibitor results that aldehyde oxidase is the pre­dominant enzyme in the oxidation of phthalazine to 1-phthalazinone in freshly pre­pared guinea pig liver slices, whereas xanthine oxidase only contributes to a small extent and aldehyde dehydrogenase does not take any part.
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Content available remote

Effects of activated neutrophils on isolated rings of rat thoracic aorta

80%
Bauer V., Sotnikova R., Drabikova K.
Journal of Physiology and Pharmacology
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2011
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tom 62
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nr 5
4

Repeated recurrence of gastric mucosal lesions in rats after a single treatment with compound 48/80, a mast cell degranulator

80%
Ohta Y., Kobayashi T., Inui K., Yoshino J., Nakazawa S.
Journal of Physiology and Pharmacology. Supplement
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2009
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tom 60
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nr 7
5
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The prevention of ischemia/reperfusion induced oxidative damage by venous blood in rabbit kidneys monitored with biochemical, histopathological and immunohistochemical analysis

80%
Cetin N., Suleyman H., Sener E., Demirci E., Gundogdu C., Akcay F.
Journal of Physiology and Pharmacology
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2014
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tom 65
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nr 3
6

The effects of vitamins A,C,E on the balance of xanthine oxidase [XOD], catalase [CT] and superoxide dismutase [SOD] in neutrophils [PMN] of patients with chronic obstructive pulmonary disease [COPD]

80%
Marcinkowska A., Malarska A., Passowicz-Muszynska E., Jankowska R., Banas T.
Current Topics in Biophysics
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1994
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tom 18
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nr 2
7

The ability of new formamidine sugar-modified derivatives of daunorubicin to stimulate free radical formation in three enzymatic systems: NADH dehydrogenase, NADPH cytochrome p450 reductase and xanthine oxidase

80%
Pawlowska J., Tarasiuk J., Borowski E., Wasowska M., Oszczapowicz I., Wolf C. R.
Acta Biochimica Polonica
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2000
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tom 47
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nr 1
Some sterically hindered N-substituted derivatives of daunorubicin are known to be poor substrates for NADH dehydrogenase, NADPH cytochrome P450 reductase and xanthine oxidase. In consequence, poor oxygen radical generation by these compounds is observed. In this study we examined a new family of sugar-N-substituted derivatives of daunorubicin bearing a bulky substituent introduced on the nitrogen atom through the amidine spacer. These compounds were found to be very active in radical formation catalyzed by all three studied enzymes. Thus, the introduction of a heterocyclic ring, even if it is bulky but flexible, on the nitrogen atom of daunosamine moiety through the one-atom spacer (amidine group), does not induce the steric hindrance effect on the interaction of daunorubicin derivatives with these flavoprotein enzymes.
8
Content available remote

Paradoxical augmentation of bradykinin-induced vasodilatation by xanthine-xanthine oxidase-derived free radicals in isolated guinea pig heart

80%
Olszanecki R., Kozlovski V. I., Chlopicki S., Gryglewski R. J.
Journal of Physiology and Pharmacology
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2002
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tom 53
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nr 4,1
Increased generation of reactive oxygen species contribute to endothelial dysfunction in atherosclerosis, hypertension and heart failure. Recently, it was suggested that bursts of superoxide anions may inactivate endothelial surface-bound enzymes such as angiotensin converting enzyme (ACE). Here, we tested effects of xanthine/xanthine oxidase-derived superoxide anions on vascular responses and ACE activity in the isolated guinea pig heart. We analysed effects of intracoronary infusion of low concentration of xanthine oxidase (10 mU/ml) in the presence of xanthine (0,5 mM) (X/XO) on bradykinin, other endothelium-dependent and independent vasodilators (acetylcholine, ADP, SNAP), as well as vasoconstrictor responses to angiotensin I and angiotensin II. Surprisingly, X/XO significantly augmented coronary response to bradykinin without an effect on responses to ADP, acetylcholine, SNAP, angiotensin I and angiotensin II. In contrast, inhibition of ACE by perindoprilate (100 nM) resulted in augmentation of bradykinin-induced vasodilatation as well as diminution of angiotensin I-evoked vasoconstriction without an influence on other responses. In summary, in the isolated guinea pig heart, X/XO-derived free radicals selectively augmented coronary vasodilator response to bradykinin, which cannot be explained by X/XO- induced derangement of ACE. The mechanism of this paradoxical phenomenon, which might represent a defensive response of the coronary circulation to oxidative stress requires further investigations.
9

Kinetics and specificity of guinea pig liver aldehyde oxidase and bovine milk xanthine oxidase towards substituted benzaldehydes

80%
Panoutsopoulos G. I., Beedham C.
Acta Biochimica Polonica
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2004
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tom 51
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nr 3
Molybdenum-containing enzymes, aldehyde oxidase and xanthine oxidase, are im­portant in the oxidation of N-heterocyclic xenobiotics. However, the role of these en­zymes in the oxidation of drug-derived aldehydes has not been established. The present investigation describes the interaction of eleven structurally related benzaldehydes with guinea pig liver aldehyde oxidase and bovine milk xanthine oxidase, since they have similar substrate specificity to human molybdenum hydroxylases. The compounds under test included mono-hydroxy and mono-methoxy benzaldehydes as well as 3,4-dihydroxy-, 3-hydroxy-4-methoxy-, 4-hydroxy-3-metho- xy-, and 3,4-dimethoxy-benzaldehydes. In addition, various amines and catechols were tested with the molybdenum hydroxylases as inhibitors of benzaldehyde oxida­tion. The kinetic constants have shown that hydroxy-, and methoxy-benzaldehydes are excellent substrates for aldehyde oxidase (Km values 5*10 M to 1^10 M) with lower affinities for xanthine oxidase (Km values around 10- M). Therefore, alde­hyde oxidase activity may be a significant factor in the oxidation of the aromatic alde­hydes generated from amines and alkyl benzenes during drug metabolism. Com­pounds with a 3-methoxy group showed relatively high Vmax values with aldehyde oxidase, whereas the presence of a 3-hydroxy group resulted in minimal Vmax values or no reaction. In addition, amines acted as weak inhibitors, whereas catechols had a more pronounced inhibitory effect on the aldehyde oxidase activity. It is therefore possible that aldehyde oxidase may be critical in the oxidation of the analogous phenylacetaldehydes derived from dopamine and noradrenaline.
10
Content available remote

Alcoholic beverages and gastric epithelial cell viability: effect on oxidative stress-induced damage

71%
Loguercio C., Tuccillo C., Federico A., Fogliano V., Del Vecchio Blanco C., Romano M.
Journal of Physiology and Pharmacology. Supplement
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2009
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tom 60
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nr 7
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