ArticleJournal of molecular histology2004
Novel oxidative self-anchoring fluorescent substrates for the histochemical localization of endogenous and immunobound peroxidase activity.
Article in Journal of molecular histology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed.
- New Technologies to Image Tumors.Cancer treatment and research · 2020Article
- N,N-Dialkylaminostyryl dyes: specific and highly fluorescent substrates of peroxidase and their application in histochemistry.Journal of molecular histology · 2008Article
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Authors and funding
2 authors.
Funding
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Abstract
Some 2-(2-styryl)-benzothiazole derivatives have been synthesized as novel fluorescent substrates for the localization of peroxidase activity. Excellent localization, high staining sensitivity and exceptionally low background staining were achieved by optimizing the choice of substrate. Multiple step-by-step anchoring of enzymatically-activated individual substrate molecules to surrounding nucleophiles, related to the catalysed reporter deposition (CARD) technique, is discussed. In contrast to tyramine conjugates, as employed in the CARD technique, the separation between reporting and anchoring function is eliminated, thus yielding a new fluorochrome with altered fluorescence properties after enzymatic cross-linking. (E)-2-(2-[4-hydroxyphenyl] vinyl)-3-ethyl-1,3-benzothiazolium iodide has been found to the best substrate so far. This was demonstrated in histochemical applications for the localization of endogenous and immunobound peroxidase activity using fixed cryostat, paraffin or semi-thin Epon sections. The specific final reaction product is efficiently excitable over a wide spectrum from green to violet, providing an outstanding sensitive localization of sites of enzymatic activity with high photo stability. In a comparative study with the Alexa Fluor 546-tyramine conjugate, endogenous and immunobound peroxidase activity was visualized and the results compared using an epi-fluorescence confocal laser scanning microscope. The novel substrate provided an improved specificity and very low background staining whereas the Alexa Fluor-tyramide exhibited a strong overall background staining. FITC-labelled secondary antibodies also yielded very low background staining but the staining was less specific compared with the biotin-based ABC amplification systems labelled with the selected substrate or the Alexa-tyramide. In conclusion, multiple fluorochrome generation close to sites of peroxidase activity, by enzymatic cross-linking of styrene-related substrates, is a promising alternative to the fluorochrome-labelled tyramine ('tyramide') deposition technique.
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