Antioxidant Enzymatic Activities in Human Blood Cells after an Allergic Reaction to Pollen or House Dust Mite

Matés, José M.; Segura, José; Pérez‐Gómez, Cristina; Rosado, Rafael Rayo; Olalla, Lucı́a; Blanca, Miguel; Sánchez‐Jiménez, Francisca

doi:10.1006/bcmd.1999.0234

Cited by 62 publications

(41 citation statements)

References 33 publications

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“…The activity of glutathione peroxidase (GPx) was measured as described elsewhere [19]. Briefly, MTB-infected monocytes were co-cultured for 24 h with or without 10 mmol/l NAC, 100 lg/ml SN50, 100 lg/ml SN50/M and 500 ng/ml allicin in the presence or absence of 10 nmol/l H 2 O 2 .…”

Section: Glutathione Peroxidase Assaymentioning

confidence: 99%

“…Briefly, MTB-infected monocytes were co-cultured for 24 h with or without 10 mmol/l NAC, 100 lg/ml SN50, 100 lg/ml SN50/M and 500 ng/ml allicin in the presence or absence of 10 nmol/l H 2 O 2 . Thereafter, cells were scrapped, sonicated and centrifuged as described earlier [19], and the supernatants were subjected to GPx activity determination. The GPx activity was quantified in 100 ll of each sample, with continuous photometric monitoring of oxidized glutathione (GSSG) at 37°C.…”

Section: Glutathione Peroxidase Assaymentioning

confidence: 99%

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Suppression of Mycobacterium tuberculosis induced reactive oxygen species (ROS) and TNF‐α mRNA expression in human monocytes by allicin

et al. 2006

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Chronic inflammation associated with tumor necrosis factor (TNF)-a and reactive oxygen species (ROS) is the hallmark of tuberculosis. Mycobacterium tuberculosis (MTB) directly stimulates human monocytes to secrete TNF-a. We show the augmented expression of TNF-a mRNA in MTB-infected monocytes by cellular activation and ROS was suppressed by allicin in a dose-dependent manner. Also, allicin enhanced the glutathione peroxidase activity, which correlated inversely with the downregulation of ROS and TNF-a in MTB-infected monocytes. Hence, allicin may prove to be a valuable natural antioxidant in combating tuberculosis.

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Section: Glutathione Peroxidase Assaymentioning

confidence: 99%

Section: Glutathione Peroxidase Assaymentioning

confidence: 99%

Suppression of Mycobacterium tuberculosis induced reactive oxygen species (ROS) and TNF‐α mRNA expression in human monocytes by allicin

et al. 2006

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“…[1] These ROS can cause severe metabolic malfunctions and damage biological macromolecules like DNA by peroxidation. [2] Superoxide dismutases (SODs; EC 1.15.1.1) destroy the superoxide anion radical by converting it into hydrogen peroxide and oxygen with a rate near the diffusion limit (k cat > 2 10 9 m À1 s À1 ). [3][4][5] Initially, two independent classes of SODs were identified.…”

Section: Introductionmentioning

confidence: 99%

“…They contain either a dinuclear Cu or Zn cofactor or a mononuclear Fe or Mn cofactor. [2] Later, the third class of nickel-containing SODs was discovered in Streptomyces by Youn et al [6][7][8] NiSOD, as a mononuclear Ni-containing metalloenzyme, cycles between the Ni II and Ni III oxidation states during catalysis. [4,9,10] Two crystallographic and several spectroscopic studies have given an impression of the structure of the whole enzyme and the geometry of its active site.…”

Section: Introductionmentioning

confidence: 99%

New Insight into the Mode of Action of Nickel Superoxide Dismutase by Investigating Metallopeptide Substrate Models

Tietze

Breitzke

Imhof³

et al. 2008

Chemistry A European J

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For the first time, the existence of a substrate adduct of a nickel superoxide dismutase (NiSOD) model, based on the first nine residues from the N terminus of the active form of Streptomyces coelicolor NiSOD, has been proven and the adduct has been isolated. This adduct is based on the cyanide anion (CN(-)), as a substrate analogue of the superoxide anion (O(2)(*-)), and the nickel metallopeptide H-HCDLPCGVY-NH(2)-Ni. Spectroscopic studies, including IR, UV/Vis, and liquid- and solid-state NMR spectroscopy, show a single nickel-bound cyanide anion, which is embedded in the metallopeptide structure. This complex sheds new light on the question of whether the mode of action of the NiSOD enzyme is an inner- or outer-sphere mechanism. Whereas discussion was previously biased in favor of an outer-sphere electron-transfer mechanism due to the fact that binding of cyanide or azide moieties to the nickel active site had never been observed, our results are a clear indication in favor of the inner-sphere electron-transfer mechanism for the disproportionation of the O(2)(*-) ion, whereby the substrate is attached to the Ni atom in the active site of the NiSOD.

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“…Monitoring the status of glutathione peroxidase (GPx) in mononuclear cells : GPx activity in control and test samples was determined as described by others and us previously (7,8).…”

Section: Methodsmentioning

confidence: 99%

Normal delivery induced stress alters glutathione peroxidase and TNF-α in elderly primigravidas mononuclear cells

Nasreen

Islam

Moin

et al. 2008

Indian J Clin Biochem

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Antioxidant Enzymatic Activities in Human Blood Cells after an Allergic Reaction to Pollen or House Dust Mite

Cited by 62 publications

References 33 publications

Suppression of Mycobacterium tuberculosis induced reactive oxygen species (ROS) and TNF‐α mRNA expression in human monocytes by allicin

Suppression of Mycobacterium tuberculosis induced reactive oxygen species (ROS) and TNF‐α mRNA expression in human monocytes by allicin

New Insight into the Mode of Action of Nickel Superoxide Dismutase by Investigating Metallopeptide Substrate Models

Normal delivery induced stress alters glutathione peroxidase and TNF-α in elderly primigravidas mononuclear cells

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