Ultrastructural localization of xanthine oxidase activity in the digestive tract of the rat

Munckhof, R. J. M. Van Den; Vreeling-Sindelárová, Helena; Schellens, J. P. M.; Noorden, C. J. F. Van; Frederiks, Wilma M.

doi:10.1007/bf00173844

Cited by 25 publications

(8 citation statements)

References 36 publications

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“…3 and 4). Frederiks and colleagues (Van den Munckhof, Vreeling-Sindelarova, Schellens, Van Noorden, & Frederiks, 1995) have provided convincing visual evidence for the role of XOR in this process. In electron microscopic studies, the enzyme was detected in enterocytes, in goblet cells and in the mucous of the duodenum.…”

Section: Article In Pressmentioning

confidence: 92%

Milk xanthine oxidase: Properties and physiological roles

Harrison

2006

International Dairy Journal

108

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Section: Article In Pressmentioning

confidence: 92%

Milk xanthine oxidase: Properties and physiological roles

Harrison

2006

International Dairy Journal

108

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“…In some studies, only a very mild fixation with 0.25% glutaraldehyde is used (Meijer, 1972;Yamamoto & Ogawa, 1983;Litwin, 1984;Angermiiller & Fahimi 1986Angermiiller et al, 1986a,b;Angerm~iller, 1989). Most peroxisomal oxidases, such as Damino acid oxidase, L-c~-hydroxy acid oxidase and polyamine oxidase, can be incubated in an aqueous incubation medium since they are bound rather firmly and therefore do not diffuse during incubation (Schellens et al, 1992;Van den Munckhof et al, 1994;, but leakage is a serious problem for loosely bound enzymes, such as cytoplasmic xanthine oxidase ( Van den Munckhof et al, 1992Frederiks et al, 1994). However, omission of fixation might lead to leakage of enzyme molecules during incubation (Fa- himi & Amarasingham, 1964;Altman & Chayen, 1966;Meijer, 1972).…”

Section: Localization Of Catalase Actwitymentioning

confidence: 99%

“…However, leakage of enzyme molecules into the incubation medium is not always prevented completely (Ritter et al, 1971;Meijer, 1972). Recently, this technique was also used for the ultrastructural localization of oxidase activities (Schellens et al, 1992;Van den Munckhof et al, 1992, 1993 and glycogen phosphorylase activity (Schellens et al, 1995) in unfixed cryostat sections since an acceptable subcellular morphology is preserved when using a semipermeable membrane. 4).…”

Section: Localization Of Catalase Actwitymentioning

confidence: 99%

In situ heterogeneity of peroxisomal oxidase activities: An update

Munchof

1996

Histochem J

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Oxidases are a widespread group of enzymes. They are present in numerous organisms and organs and in various tissues, cells, and subcellular compartments, such as mitochondria. An important source of oxidases, which is investigated and discussed in this study, are the (micro)peroxisomes. Oxidases share the ability to reduce molecular oxygen during oxidation of their substrate, yielding an oxidized product and hydrogen peroxide. Besides the hydrogen peroxide-catabolizing enzyme catalase, peroxisomes contain one or more hydrogen peroxide-generating oxidases, which participate in different metabolic pathways. During the last four decades, various methods have been developed and elaborated for the histochemical localization of the activities of these oxidases. These methods are based either on the reduction of soluble electron acceptors by oxidase activity or on the capture of hydrogen peroxide. Both methods yield a coloured and/or electron dense precipitate. The most reliable technique in peroxisomal oxidase histochemistry is the cerium salt capture method. This method is based on the direct capture of hydrogen peroxide by cerium ions to form a fine crystalline, insoluble, electron dense reaction product, cerium perhydroxide, which can be visualized for light microscopy with diaminobenzidine. With the use of this technique, it became clear that oxidase activities not only vary between different organisms, organs, and tissues, but that heterogeneity also exists between different cells and within cells, i.e. between individual peroxisomes. A literature review, and recent studies performed in our laboratory, show that peroxisomes are highly differentiated organelles with respect to the presence of active enzymes. This study gives an overview of the in situ distribution and heterogeneity of peroxisomal enzyme activities as detected by histochemical assays of the activities of catalase, and the peroxisomal oxidases D-amino acid oxidase, L-alpha-hydroxy acid oxidase, polyamine oxidase and uric acid oxidase.

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“…In broilers, this enzyme is mainly expressed in the liver, but also in the intestine (60% of the amount in the liver) and other organs but in a lower amount [25]. The intestine requires an efficient immune defense at the epithelial surface, and among other factors, XOR is secreted by the enterocytes of the small intestine [26].…”

Section: Introductionmentioning

confidence: 99%

Deoxynivalenol Impairs Hepatic and Intestinal Gene Expression of Selected Oxidative Stress, Tight Junction and Inflammation Proteins in Broiler Chickens, but Addition of an Adsorbing Agent Shifts the Effects to the Distal Parts of the Small Intestine

Osselaere

Santos

Hautekiet³

et al. 2013

PLoS ONE

141

127

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Broiler chickens are rather resistant to deoxynivalenol and thus, clinical signs are rarely seen. However, effects of subclinical concentrations of deoxynivalenol on both the intestine and the liver are less frequently studied at the molecular level. During our study, we investigated the effects of three weeks of feeding deoxynivalenol on the gut wall morphology, intestinal barrier function and inflammation in broiler chickens. In addition, oxidative stress was evaluated in both the liver and intestine. Besides, the effect of a clay-based mycotoxin adsorbing agent on these different aspects was also studied. Our results show that feeding deoxynivalenol affects the gut wall morphology both in duodenum and jejenum of broiler chickens. A qRT-PCR analysis revealed that deoxynivalenol acts in a very specific way on the intestinal barrier, since only an up-regulation in mRNA expression of claudin 5 in jejunum was observed, while no effects were seen on claudin 1, zona occludens 1 and 2. Addition of an adsorbing agent resulted in an up-regulation of all the investigated genes coding for the intestinal barrier in the ileum. Up-regulation of Toll-like receptor 4 and two markers of oxidative stress (heme-oxigenase or HMOX and xanthine oxidoreductase or XOR) were mainly seen in the jejunum and to a lesser extent in the ileum in response to deoxynivalenol, while in combination with an adsorbing agent main effect was seen in the ileum. These results suggest that an adsorbing agent may lead to higher concentrations of deoxynivalenol in the more distal parts of the small intestine. In the liver, XOR was up-regulated due to DON exposure. HMOX and HIF-1α (hypoxia-inducible factor 1α) were down-regulated due to feeding DON but also due to feeding the adsorbing agent alone or in combination with DON.

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Ultrastructural localization of xanthine oxidase activity in the digestive tract of the rat

Cited by 25 publications

References 36 publications

Milk xanthine oxidase: Properties and physiological roles

Milk xanthine oxidase: Properties and physiological roles

In situ heterogeneity of peroxisomal oxidase activities: An update

Deoxynivalenol Impairs Hepatic and Intestinal Gene Expression of Selected Oxidative Stress, Tight Junction and Inflammation Proteins in Broiler Chickens, but Addition of an Adsorbing Agent Shifts the Effects to the Distal Parts of the Small Intestine

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