Cerium as Capturing Agent in Phosphatase and Oxidase Histochemistry

Kj, Halbhuber; Hulstaert, C.E.; Feuerstein, H; Zimmermann, Norbert

doi:10.1016/s0079-6336(11)80041-0

Cited by 18 publications

(16 citation statements)

References 291 publications

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“…The little cerium deposition that occurred in CFs and vascular tissues did not appear to be much affected by the presence or absence of putrescine. One limitation to using Ce3+ on intact tissues is that these ions diffuse relatively slowly through biological samples (Van Noorden and Frederiks, 1993;Halbhuber et al, 1994); for instance, Kausch (1987) reported that they penetrate only 70 to 15 cell layers beyond the cut surface of tissue samples. Seria1 sections taken from pea epicotyl segments incubated with Ce3+ and putrescine, as well as from segments incubated in Ce3+ alone, showed fairly constant staining to depths between 100 and 200 pm (L. Liu, K.-E.L.…”

Section: Resultsmentioning

confidence: 99%

“…The inability of epi-polarization microscopy to distinguish between cerium deposits and crystalline cellulose in secondary cell walls makes study of H 2 O 2 production for lignin biosynthesis difficult with this technique. This problem is even more pronounced in mature plant tissues, and appropriate experimental controls are critical for interpreting results (Halbhuber et al, 1994). However, in such cases, mapping the distribution of elemental Ce with SE/XRMA can be used to clarify observations.…”

Section: Dlscusslonmentioning

confidence: 99%

“…However, these techniques are indirect measurements of H,O, production and are limited to detection of H202 produced at the cut surface of tissue sections. Briggs et al (1975) introduced the use of Ce3+ as a reagent for specific detection of H,Oz production, and this technique is now widely used for the histochemical detection of various oxidases and phosphatases (Kausch, 1987;Van Noorden and Frederiks, 1993;Halbhuber et al, 1994). Ce3+ penetrates into tissues, albeit slowly, and reacts directly with H,O, to form insoluble, finely divided deposits of Ce(1V) perhydroxide.…”

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confidence: 99%

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Localization of Hydrogen Peroxide Production in Pisum sativum L. Using Epi-Polarization Microscopy to Follow Cerium Perhydroxide Deposition

1995

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Cerium is becoming an increasingly popular reagent for histochemical localization of oxidases and phosphatases because it combines directly with reaction products to form fine precipitates of electron-dense materials that can be easily detected using transmission electron microscopy or laser confocal scanning microscopy. We used epi-polarization microscopy to detect cerium perhydroxide deposits formed when H,O, was produced by diamine oxidase in pea (Pisum sativum L.) epicotyls exposed to exogenous putrescine. Diamine oxidase activity was abundant in cortical cell walls but showed little, if any, association with vascular tissues. Maps of cerium deposition generated using scanning electron microscopy/x-ray microanalysis verified these observations. This study demonstrates the use of epi-polarization microscopy to follow cerium deposition, and the ready accessibility of this microscopy technique should facilitate more widespread use of cerium for plant histochemistry and cytochemistry.

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Section: Resultsmentioning

confidence: 99%

Section: Dlscusslonmentioning

confidence: 99%

mentioning

confidence: 99%

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Localization of Hydrogen Peroxide Production in Pisum sativum L. Using Epi-Polarization Microscopy to Follow Cerium Perhydroxide Deposition

1995

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“…Due to the catalase-like activity of CDNs, the free hydrogen peroxide cannot be released in SOD-mimetic (Scheme 1(B)) or hydroxyl radical scavenging (Scheme 2(B)) cycles because H 2 O 2 is immediately decomposed by CeO 2 , according to Scheme 4(C). Cerium perhydroxide formation was observed during the interaction of cerium compounds and O 2 -radicals [39].…”

Section: Cdn Is Catalase Mimeticmentioning

confidence: 99%

Cerium dioxide nanoparticles as third-generation enzymes (nanozymes)

Попов¹,

Shcherbakov²,

Zholobak³

et al. 2017

Nanosystems: Phys. Chem. Math.

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Ceria nanoparticles are capable of performing the function of some enzymes (such as oxidoreductases, phosphatase) and can be classified as nanozymes. In this review, the actual data on the enzymatic activity of ceria were critically analyzed and specific conditions under which the cerium dioxide nanoparticles can act as enzymes were defined. The presented analysis may be useful in the planning, design and synthesis of ceria nanoparticles having the desired enzymatic functions required for various processes, including the development of the nanodrugs, which exhibit the therapeutic effect depending on their composition and pH of media, development of molecular sensors and biosensors, etc.

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“…These methods provide a new aspect into the ATPase cytochemistry because they are highly reproducible for enzyme demonstration, generate very small primary cerium reaction product precipitates, and are highly sensitive for enzyme determinations (Halbhuber et al 1994). The ceriumbased methodology has been also employed for both Na,K-ATPase and H,K-ATPase (Kobayashi and Seguchi 1990;Kobayashi et al 1987).…”

mentioning

confidence: 99%

Biochemical Properties and Cytochemical Localization of Ouabain-insensitive, Potassium-dependentp-Nitrophenylphosphatase Activity in Rat Atrial Myocytes

Zinchuk¹,

Kobayashi²,

Saz³

et al. 1997

J Histochem Cytochem.

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Enzyme activity that represents ouabain-insensitive, potassium-dependent p-nitrophenylphosphatase (p-NPPase) was assessed in rat atrial myocytes by biochemical and cytochemical procedures. No activity was detected in parallel experiments with ventricular myocytes. Fixed tissues were incubated in a reaction medium containing Tricine buffer, p-nitrophenylphosphate (p-NPP), KCl, MgCl2, CaCl2, CeCl3, Triton X-100, levamisole, and ouabain. Final pH was adjusted to 7.5. Biochemical studies showed that accumulation of p-nitrophenol in the medium was increased proportionally in accordance with the amount of incubated tissue. This activity was optimal with incubation at pH 7.5 and in the presence of KCl. Approximately 70% of the enzyme was inhibited by 2 mM CeCl3. Electron microscopic observations revealed reaction product (RP) at sites of ouabain-insensitive, potassium-dependent p-NPPase activity as electron-dense precipitate localized at the inner surface of the plasma membrane and at the T-tubules of atrial myocytes. Control experiments indicated that the activity was strongly inhibited by sodium orthovanadate and was repressed by omeprazole and 1,3-dicyclohexylcarbodiimide. X-ray microanalysis confirmed the presence of cerium within the cytochemical RP. The ouabain-insensitive, K-dependent p-NPPase activity detected in the present study is considered to be an isoform of a P-type, H-transporting, K-dependent adenosine triphosphatase (H,K-ATPase).

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Cerium as Capturing Agent in Phosphatase and Oxidase Histochemistry

Cited by 18 publications

References 291 publications

Localization of Hydrogen Peroxide Production in Pisum sativum L. Using Epi-Polarization Microscopy to Follow Cerium Perhydroxide Deposition

Localization of Hydrogen Peroxide Production in Pisum sativum L. Using Epi-Polarization Microscopy to Follow Cerium Perhydroxide Deposition

Cerium dioxide nanoparticles as third-generation enzymes (nanozymes)

Biochemical Properties and Cytochemical Localization of Ouabain-insensitive, Potassium-dependentp-Nitrophenylphosphatase Activity in Rat Atrial Myocytes

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