Oxidation of Proteins by Tyrosinase and Peroxidase

Sizer, Irwin W.

doi:10.1002/9780470122594.ch4

Cited by 30 publications

(8 citation statements)

References 65 publications

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“…Experiments that expose proteins to UV irradiation, g-irradiation, oxygen-free radicals, nitrogen dioxide, peroxynitrite, and lipid hydroperoxides have all demonstrated the formation of dityrosine (Lehrer & Fasman, 1967;Boguta & Dancewicz, 1981;Davies, 1987;Tew & Ortiz de Montellano, 1988;Giulivi & Davies, 1993, 1994a. In addition, the enzymatic formation of dityrosine has been found to promote protein crosslinking after incubation of proteins with peroxidases (Wagley et al, 1950;Sizer, 1953;Aeschbach, Amado, & Neukom, 1976;Foerder & Shapiro, 1977;Giulivi & Davies, 1994a). Tyrosine is oxidized to dityrosine in response to oxidative stress by peroxidase-catalyzed mechanisms in chymotrypsin, myoglobin, hemoglobin, and calmodulin (Aeschbach et al, 1976;Tew & Ortiz de Montellano, 1988;Giulivi & Davies, 1993;Malencik et al, 1996).…”

Section: B Dityrosine As a Biomarker For Oxidative/nitrative Stressmentioning

confidence: 94%

Current analytical methods for the detection of dityrosine, a biomarker of oxidative stress, in biological samples

DiMarco

Giulivi

2006

Mass Spectrometry Reviews

121

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Dityrosine is a fluorescent molecule formed as a result of normal posttranslational processing. In many structural proteins, dityrosine confers resistance to proteolysis and physicochemical trauma as a stabilizing crosslink. Dityrosine has also been found in oxidative/nitrative stress under a variety of conditions and biological systems. In this regard, it has been used as an important biomarker for oxidatively modified proteins during UV and gamma-irradiation, aging, and exposure to oxygen free radicals, nitrogen dioxide, peroxynitrite, and lipid hydroperoxides. Renewed interest in dityrosine and other tyrosine oxidation products as clinical indicators of oxidative modification has driven the development of important techniques for the specific analysis and quantification of these molecules. The presence of elevated levels of dityrosine in mammalian tissue and urine samples has been measured by chromatographic separation followed by mass spectrometry GC-MS and HPLC-MS/MS. Increases in dityrosine levels have been associated with pathologies such as eye cataracts, atherosclerosis, acute inflammation, and Alzheimer's disease. The continued development of, and increased accessibility to, improved mass spectrometric instrumentation will expand the capability, feasibility, and sensitivity with which specific biomarkers like dityrosine can be measured.

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Section: B Dityrosine As a Biomarker For Oxidative/nitrative Stressmentioning

confidence: 94%

Current analytical methods for the detection of dityrosine, a biomarker of oxidative stress, in biological samples

DiMarco

Giulivi

2006

Mass Spectrometry Reviews

121

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“…Peroxidase is one of the most precisely investigated respiratory enzymes in the field of enzymology. It is a heme protein that is widely distributed in plants, animals and microorganisms (Sizer, 1953; Saunders et al , 1964; Bordeleau & Bartha, 1969; Koenigs, 1972). Peroxidase, in the presence of H 2 O 2 , oxidises monophenols, diphenols, monoamines, diamines, aromatic acids, amino acids and ascorbic acid, as well as halides and nitrites (Sizer, 1953; Saunders et al , 1964; Urs & Dunleavy, 1975).…”

Section: Introductionmentioning

confidence: 99%

Localisation of hydrogen peroxide and peroxidase in gametophytes of Ceratopteris richardii (C‐fern) grown in the presence of pathogenic fungi in a gnotobiotic system

Urs

Roberts

Schultz

2006

Annals of Applied Biology

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The endogenous localisation of peroxidase and hydrogen peroxide (H 2 O 2 ) was detected when gametophytes of the fern, Ceratopteris richardii, were exposed to the plant pathogenic fungi Sclerotium rolfsii and Sclerotinia sclerotiorum and Phytophthora infestans, an oomycete, in a gnotobiotic system. This was accomplished by light microscopy using 3,3#-diaminobenzidine, guaiacol and H 2 O 2 and starch potassium iodide (KI) staining procedures, which facilitated the observation of the reaction in vivo and in situ, without physically damaging the tissues. All three staining methods promoted staining at the rhizoid regions. Although most of the cells were destroyed when gametophytes were exposed to S. rolfsii and S. sclerotiorum, there was staining where mycelial growth was confluent with cell walls. A qualitative test confirmed that the colour change in starch KI agar medium, as well as in the histochemical test with starch KI, was because of H 2 O 2 secreted by S. rolfsii or S. sclerotiorum and not because of oxalic acid. When gametophytes were exposed to P. infestans, no infection occurred, but localisation of H 2 O 2 and peroxidase was detected irrespective of staining methods tested. Based on the observation on gametophytes grown in presence of P. infestans, it is possible that the peroxidase in plants coupled with H 2 O 2 may prevent the invasion of nonpathogens by functioning as a barrier. This fern-pathogen model system has potential for application as a tool to study the host-parasite interaction in a gnotobiotic system.

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“…(65,69). It is also involved in oxidative decarboxylation of methionine (53) and biosynthesis of ethylene (81).…”

mentioning

confidence: 99%

The function of peroxidase in plant resistance to bacterial pustule disease of soybeans

Urs

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Oxidation of Proteins by Tyrosinase and Peroxidase

Cited by 30 publications

References 65 publications

Current analytical methods for the detection of dityrosine, a biomarker of oxidative stress, in biological samples

Current analytical methods for the detection of dityrosine, a biomarker of oxidative stress, in biological samples

Localisation of hydrogen peroxide and peroxidase in gametophytes of Ceratopteris richardii (C‐fern) grown in the presence of pathogenic fungi in a gnotobiotic system

The function of peroxidase in plant resistance to bacterial pustule disease of soybeans

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