Reactive species and their accumulation on radical-damaged proteins

Dean, Roger T.; Gieseg, Steven P.; Davies, Michael J.

doi:10.1016/0968-0004(93)90145-d

Cited by 223 publications

(113 citation statements)

References 35 publications

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“…The possibility also exists that the increase of the intensity around 1,413 cm -~ absorption is due, at least in part, to the increase in the C-N bonds, which might results from oxidative processes leading to the formation of additional ring structures. All these alterations are consistent with protein oxidation according to the mechanism proposed by others [33].…”

Section: Resultssupporting

confidence: 76%

“…It is likely that the released iron is bound by the cation binding sites on proteins and that oxygen radicals are formed at those specific sites inducing damage primarily in the amino acid residues. The results of our IR spectroscopy studies are compatible with the scheme suggested by Dean et al [33] for metal catalyzed oxidation of proteinbound 3,4-dihydroxyphenylalanine (DOPA), which is formed by hydroxyl radical-induced hydroxylation of tyrosine. An additional comment is needed for the results obtained with ferrozine.…”

Section: Discussionsupporting

confidence: 79%

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Iron release, membrane protein oxidation and erythrocyte ageing

et al. 1995

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The aerobic incubation of erythroeytes in phosphate buffer for 24-60 h (a model of rapid in vitro ageing) induced progressive iron release and methemoglobin formation. Membrane proteins showed electrophoretic alterations and increase in carbonyl groups (as documented by IR spectroscopy). None of these phenomena were seen when the erythrocytes were incubated under anaerobic conditions. The membranes from aerobically incubated cells bound a much higher amount of autologous IgG than those from anaerobically incubated ones, suggesting that the aerobic incubation gives rise to the senescent antigen. The addition of ferrozine during the aerobic incubation prevented both the IgG binding and the protein alterations seen in the IR spectra, suggesting an intracellular chelation of the released iron by ferrozine.

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Section: Resultssupporting

confidence: 76%

Section: Discussionsupporting

confidence: 79%

Iron release, membrane protein oxidation and erythrocyte ageing

et al. 1995

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“…En el Tabla 4, se muestra el Sandoval et al (2002a), evaluaron la actividad antioxidante de la maca (Lepidium meyenii), frente al radical peroxilo obteniendo un valor de IC 50 de 430 µg.mL -1 destacándose una mayor eficiencia de las muestras de cáscara de camu-camu, indicando que las muestras en experimento contribuyen a la disminución de la formación de radicales peroxilo (DEAN;GIESEG;DAVIES, 1993;SANDOVAL et al, 2002a), presentando una correlación lineal con el contenido de ácido ascórbico (r = 0,926) y polifenoles (r = 0,923); destacando que en las muestras de cáscara de fruto maduro y verde (Figura 1, Tabla 2), la acción de inhibición, está influenciado por otros componentes presentes en la muestra (PRIOR et al, 1998;KAHKOMEN et al, 1999;ZHENG y WANG, 2001). …”

Section: A) Coeficiente De Inhibición (Ic 50 )unclassified

Antocianinas, ácido ascórbico, polifenoles totales y actividad antioxidante, en la cáscara de camu-camu (Myrciaria dubia (H.B.K) McVaugh)

Villanueva-Tiburcio¹,

Condezo-Hoyos²,

Asquieri³

2010

Ciênc. Tecnol. Aliment.

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“…Perhaps more interesting is that when the frequencies of Cys, Met, and His are added to the frequencies of the above-mentioned aromatic residues, the r value of the correlation with the position of the sequences along the third axis is higher (r ‫ס‬ 0.71). These six residues have in common the property of being the preferential targets of reactive oxygen species and can act as sinks for radical fluxes through electron transfer between amino acids on the protein (Dean et al 1993;Berlett and Stadtman 1997). It has been suggested that these residues could confer some resistance to reactive oxygen species in the anaerobic unicellular eukaryote G. lamblia (Garat and Musto 2000).…”

Section: Amino Acid Frequenciesmentioning

confidence: 99%

Trends in Codon and Amino Acid Usage in Thermotoga maritima

Zavala

Naya

Romero

et al. 2002

Journal of Molecular Evolution

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Abstract. The usage of synonymous codons and the frequencies of amino acids were investigated in the complete genome of the bacterium Thermotoga maritima using a multivariate statistical approach. The GC3 content of each gene was the most prominent source of variation of codon usage. Surprisingly the usage of UGU and UGC (synonymous triplets coding for Cys, the least frequent amino acid in this species) was detected as the second most prominent source of variation. However, this result is probably an artifact due to the very low frequency of Cys together with the nonbiased composition of this genome. The third trend was related to the preferential usage of a subset of codons among highly expressed genes, and these triplets are presumed to be translationally optimal. Concerning the amino acid usage, the hydropathy level of each protein (and therefore the frequency of charged residues) was the main trend, while the second factor was related to the frequency of usage of the smaller residues, suggesting that the cell economy strongly influences the architecture of the proteins. The third axis of the analysis discriminated the usage of Phe, Tyr, Trp (aromatic residues) plus Cys, Met, and His. These six residues have in common the property of being the preferential targets of reactive oxygen species, and therefore the anaerobic condition of T. maritima is an important factor for the amino acid frequencies. Finally, the Cys content of each protein was the fourth trend.

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Reactive species and their accumulation on radical-damaged proteins

Cited by 223 publications

References 35 publications

Iron release, membrane protein oxidation and erythrocyte ageing

Iron release, membrane protein oxidation and erythrocyte ageing

Antocianinas, ácido ascórbico, polifenoles totales y actividad antioxidante, en la cáscara de camu-camu (Myrciaria dubia (H.B.K) McVaugh)

Trends in Codon and Amino Acid Usage in Thermotoga maritima

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