The Oxidation of Tyramine, Tyrosine, and Related Compounds by Peroxidase

Gross, Arthur J.; Sizer, Irwin W.

doi:10.1016/s0021-9258(18)70059-8

Cited by 335 publications

(78 citation statements)

References 8 publications

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“…This method is based on the ability of tyramine to chemically adhere to a solid substrate (e.g., tissue section) following oxidation/radicalization. 45 Adams 2 adapted this system for immunohistochemistry. The procedure is based on the deposition of biotinylated tyramine at the location of the Ag-Ab reaction, catalyzed by horseradish peroxidase (HRP).…”

Section: Detection Systemsmentioning

confidence: 99%

Technical Aspects of Immunohistochemistry

2005

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Abstract.Immunohistochemistry is an integral technique in many veterinary laboratories for diagnostic and research purposes. In the last decade, the ability to detect antigens (Ags) in tissue sections has improved dramatically, mainly by countering the deleterious effects of formaldehyde with antigen retrieval (AR) and increasing sensitivity of the detection systems. In this review, I address these topics and provide an overview of technical aspects of immunohistochemistry, including those related to antibodies (Abs) and Ags, fixation, AR, detection methods, background, and troubleshooting. Microarray technology and the use of rabbit monoclonal Abs in immunohistochemistry are also discussed.

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Section: Detection Systemsmentioning

confidence: 99%

Technical Aspects of Immunohistochemistry

2005

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“…This method is based on the ability of tyramide to adhere to a solid substrate (eg, tissue section) following oxidation/radicalization. 131 The procedure, adapted for IHC, 3 is based on the deposition, catalyzed by horseradish peroxidase (HRP), of biotinylated or FITC-conjugated tyramide at the location of the antigen-antibody reaction. Free radicals formed during the HRP-tyramide reaction bind covalently to electron-rich amino acids (eg, tyrosine) of nearby proteins.…”

Section: Analytical Phase Of Ihcmentioning

confidence: 99%

When Tissue Antigens and Antibodies Get Along

2013

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Once focused mainly on the characterization of neoplasms, immunohistochemistry (IHC) today is used in the investigation of a broad range of disease processes with applications in diagnosis, prognostication, therapeutic decisions to tailor treatment to an individual patient, and investigations into the pathogenesis of disease. This review addresses the technical aspects of immunohistochemistry (and, to a lesser extent, immunocytochemistry) with attention to the antigen-antibody reaction, optimal fixation techniques, tissue processing considerations, antigen retrieval methods, detection systems, selection and use of an autostainer, standardization and validation of IHC tests, preparation of proper tissue and reagent controls, tissue microarrays and other high-throughput systems, quality assurance/quality control measures, interpretation of the IHC reaction, and reporting of results. It is now more important than ever, with these sophisticated applications, to standardize the entire IHC process from tissue collection through interpretation and reporting to minimize variability among laboratories and to facilitate quantification and interlaboratory comparison of IHC results.

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“…The levels of nitrotyrosine and DiY, two products of oxidative modification, have been shown to be significantly increased in the AD brain [18]. The cross-linking of proteins by DiY enhances their stability [19], as demonstrated by the occurrence in tough proteins such as resilin. Indeed, DiY cross-links occur naturally in several elastic and structural proteins including elastin, fibroin, keratin, cuticlin, and collagen [50][51][52][53].…”

Section: Discussionmentioning

confidence: 99%

“…Oxidative stress is one of the earliest sources of damage identified in AD [17] and key markers of oxidative stress, such as nitrotyrosine and DiY levels, are increased in the AD brain [18]. DiY cross-linking results in a stable, irreversible modification of proteins [19]. Aβ and α-synuclein (associated with Parkinson's disease) have both been shown to form DiY cross-links in vitro [20][21][22][23].…”

Section: Introductionmentioning

confidence: 99%

Oxidative Stress Conditions Result in Trapping of PHF-Core Tau (297–391) Intermediates

Maina

Al-Hilaly

Burra

et al. 2021

Cells

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The self-assembly of tau into paired helical filaments (PHFs) in neurofibrillary tangles (NFTs) is a significant event in Alzheimer’s disease (AD) pathogenesis. Numerous post-translational modifications enhance or inhibit tau assembly into NFTs. Oxidative stress, which accompanies AD, induces multiple post-translational modifications in proteins, including the formation of dityrosine (DiY) cross-links. Previous studies have revealed that metal-catalysed oxidation (MCO) using Cu2+ and H2O2 leads to the formation of DiY cross-links in two misfolding proteins, Aβ and α-synuclein, associated with AD and Parkinson’s disease respectively. The effect of MCO on tau remains unknown. Here, we examined the effect of MCO and ultra-violet oxidation to study the influence of DiY cross-linking on the self-assembly of the PHF-core tau fragment. We report that DiY cross-linking facilitates tau assembly into tau oligomers that fail to bind thioflavin S, lack β-sheet structure and prevents their elongation into filaments. At a higher concentration, Cu2+ (without H2O2) also facilitates the formation of these tau oligomers. The DiY cross-linked tau oligomers do not cause cell death. Our findings suggest that DiY cross-linking of pre-assembled tau promotes the formation of soluble tau oligomers that show no acute impact on cell viability.

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The Oxidation of Tyramine, Tyrosine, and Related Compounds by Peroxidase

Cited by 335 publications

References 8 publications

Technical Aspects of Immunohistochemistry

Technical Aspects of Immunohistochemistry

When Tissue Antigens and Antibodies Get Along

Oxidative Stress Conditions Result in Trapping of PHF-Core Tau (297–391) Intermediates

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