Wyniki wyszukiwania

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Oxidative modification of type II collagen differentially affects its arthritogenic and tolerogenic capacity in experimental arthritis

100%

Marcinkiewicz J., Biedron R., Maresz K., Kwasny-Krochin B., Bobek M., Kontny E., Maslinski W., Chain B.

Archivum Immunologiae et Therapiae Experimentalis

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2004

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tom 52

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nr 4

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Oxidative modification of ovalbumin

100%

Olszowski S., Olszowska E., Stelmaszynska T., Krawczyk A., Marcinkiewicz J., Baczek N.

Acta Biochimica Polonica

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1996

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tom 43

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nr 4

Stimulated neutrophils (PMNL) are a source of the active oxygen species: O2, H2O2 and HOCl/OCT which in turn can act on proteins yielding a variety of mixed oxidation products. A system is proposed in which a model protein — ovalbumin (OVA) first undergoes chlorination by HOC1/OCT and next is oxidised by H2O2. The modification of functional groups (-NH2, -SH, -S-S-, >C=0, Tyr and Trp) in OVA was monitored as well as their accessibility to promote aggregation. Chlorination resulted in additional inter- or intra -S-S- bond formation followed by a decrease in the total sulfhydryl group content. Amino groups were oxidised to carbonyl moieties with a concomitant acidic shift of pi. Formation of chlorotyrosine at the chlorination step was confirmed and its further H202-mediated transformation to bityrosine was demonstrated. It has also been confirmed that tryptophan, and not tyrosine, is the first target for chlorination. SDS/PAGE and HPLC profiles revealed that HOCiyOCl" chlorination promotes formation of aggregates stabilised by non covalent bonds. In conclusion, we suggest that a dramatic change in the OVA molecule structure begins when the molar excess of HOC1/OC1 is about 2 per one reactive group in OVA.

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Mitochondrial protease AtFtsH4 affects the level of oxidatively modified proteins in seeds and mitochondria of A. thaliana

84%

Czarna M., Smakowska E., Janska H.

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

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Aggregation of LS Rubisco in response to exposure of plants to low irradiance

84%

Grabsztunowicz M., Jackowski G.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2013

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tom 94

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nr 3

5

ROS production and redox control in response to abiotic stress in seeds and seedlings

84%

Kranner I.

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

6

Flavonoids and the aging brain

67%

Schmitt-Schillig S., Schaffer S., Weber C. C., Eckert G. P., Muller W. E.

Journal of Physiology and Pharmacology. Supplement

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2005

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tom 56

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nr 1

23-36

Like in all other organs, the functional capacity of the human brain deteriorates over time. Pathological events such as oxidative stress, due to the elevated release of free radicals and reactive oxygen or nitrogen species, the subsequently enhanced oxidative modification of lipids, protein, and nucleic acids, and the modulation of apoptotic signaling pathways contribute to loss of brain function. The identification of neuroprotective food components is one strategy to facilitate healthy brain aging. Flavonoids were shown to activate key enzymes in mitochondrial respiration and to protect neuronal cells by acting as antioxidants, thus breaking the vicious cycle of oxidative stress and tissue damage. Furthermore, recent data indicate a favorable effect of flavonoids on neuro-inflammatory events. Whereas most of these effects have been shown in vitro, limited data in vivo are available, suggesting a rather low penetration of flavonoids into the brain. Nevertheless, several reports support the concept that flavonoid intake inhibits certain biochemical processes of brain aging, and might thus prevent to some extent the decline of cognitive functions with aging as well as the development or the course of neurodegenerative diseases. However, more data are needed to assess the true impact of flavonoids on brain aging.

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Single-dose versus two-dose dexamethasone effects on lung inflammation and airway reactivity in meconium-instilled rabbits

67%

Mokra D., Mokry J., Drgova A., Bulikova J., Petraskova M., Calkovska A.

Journal of Physiology and Pharmacology. Supplement

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2007

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tom 58

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nr 5

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The detection of food components capable of preventing DNA oxidative damage by restriction analysis

67%

Kolodziejski D., Brillowska-Dabrowska A., Bartoszek A.

Polish Journal of Food and Nutrition Sciences

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2011

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tom 61

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nr Suppl.1

9

Involvement of ascorbate, glutathione and protein S-thiolation in benzothiadiazole-inducible defense response of cucumber against Pseudomonas syringae pv. lachrymans

67%

Kuzniak E., Kopczewski T., Glowacki R., Chwatko G., Gajewska E., Wielanek M., Sklodowska M.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2013

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tom 94

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nr 3

10

Collagen type II modification by hypochlorite

67%

Olszowski S., Mak P., Olszowska E., Marcinkiewicz J.

Acta Biochimica Polonica

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2003

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tom 50

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nr 2

Oxidation of proteins is a common phenomenon in the inflammatory process mediated by highly reactive agents such as hypochlorite (HOCl/OCl-) produced by activated neutrophils. For instance, in rheumatoid arthritis hypochlorite plays an important role in joint destruction. One of the major targets for HOCl/OCl- is collagen type II (CII) — the primary cartilage protein. In our study, HOCl/OCl- mediated collagen II modifications were tested using various methods: circular dichroism (CD), HPLC, ELISA, dynamic light scattering (DLS), fluorimetry and spectrophotometry. It was shown that hypochlorite action causes deamination with consecutive carbonyl group formation and transformation of tyrosine residues to dichlorotyrosine. Moreover, it was shown that ammonium chloramine (NH^Cl) formed in the reaction mixture reacts with CII. However, in this case the yield of carbonyl groups and dichlorotyrosine is lower than that observed for HOCl/OCl- by 50%. CD data revealed that collagen II exists as a random coil in the samples and that chlorination is followed by CII fragmentation. In the range of low HOCl/OCl- concentrations (up to 1 mM) 10-90 kDa peptides are predominant whereas massive production of shorter peptides was observed for high (5 mM) hypochlorite concentration. DLS measurements showed that chlorina- tion with HOCl/OCl- decreases the radius of collagen II aggregates from 30 to 6.8 nm. Taking into account the fact that chlorinated collagen is partially degraded, the DLS results suggest that smaller micelles are formed of the 10-90 kDa peptide fraction. Moreover, collagen chlorination results in epitope modification which affects CII recognition by anti-CII antibodies. Finally, since in the synovial fluid the plausible hypochlorite concentration is smaller than that used in the model the change of size of molecular aggregates seems to be the best marker of hypochlorite-mediated collagen oxidation.

Ograniczanie wyników

Oxidative modification of type II collagen differentially affects its arthritogenic and tolerogenic capacity in experimental arthritis

Oxidative modification of ovalbumin

Mitochondrial protease AtFtsH4 affects the level of oxidatively modified proteins in seeds and mitochondria of A. thaliana

Aggregation of LS Rubisco in response to exposure of plants to low irradiance

ROS production and redox control in response to abiotic stress in seeds and seedlings

Flavonoids and the aging brain

Single-dose versus two-dose dexamethasone effects on lung inflammation and airway reactivity in meconium-instilled rabbits

The detection of food components capable of preventing DNA oxidative damage by restriction analysis

Involvement of ascorbate, glutathione and protein S-thiolation in benzothiadiazole-inducible defense response of cucumber against Pseudomonas syringae pv. lachrymans

Collagen type II modification by hypochlorite