On the topology of the catalase biosynthesis and-degradation in the guinea pig liver

Geerts, Albert; Prest, B. De; Roels, Frank

doi:10.1007/bf00495414

Cited by 27 publications

(13 citation statements)

References 26 publications

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“…Catalase was initially thought to primarily be a peroxisomal protein, but subsequent studies indicated a significant cytosolic pool as well (11,43-46). A number of studies have focused on understanding catalase maturation with respect to its sub-cellular compartmentalization.…”

Section: Discussionmentioning

confidence: 99%

Novel insights in mammalian catalase heme maturation: Effect of NO and thioredoxin-1

Chakravarti

Gupta

Majors

et al. 2015

Free Radical Biology and Medicine

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Catalase is a tetrameric heme-containing enzyme with essential antioxidant functions in biology. Multiple factors including nitric oxide (NO) have been shown to attenuate its activity. However, the possible impact of NO in relation to the maturation of active catalase, including its heme acquisition and tetramer formation, has not been investigated. We found that NO attenuates heme insertion into catalase in both short-term and long-term incubations. The NO inhibition in catalase heme incorporation was associated with defective oligomerization of catalase, such that inactive catalase monomers and dimers accumulated in place of the mature tetrameric enzyme. We also found that GAPDH plays a key role in mediating these NO effects on the structure and activity of catalase. Moreover, the NO sensitivity of catalase maturation could be altered up or down by manipulating the cellular expression level or activity of thioredoxin-1, a known protein-SNO denitrosylase enzyme. In a mouse model of allergic inflammatory asthma, we found that lungs from allergen-challenged mice contained a greater percentage of dimeric catalase relative to tetrameric catalase in the unchallenged control, suggesting that the mechanisms described here are in play in the allergic asthma model. Together, our study shows how maturation of active catalase can be influenced by NO, S-nitrosylated GAPDH, and thioredoxin-1, and how maturation may become compromised in inflammatory conditions such as asthma.

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Section: Discussionmentioning

confidence: 99%

Novel insights in mammalian catalase heme maturation: Effect of NO and thioredoxin-1

Chakravarti

Gupta

Majors

et al. 2015

Free Radical Biology and Medicine

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“…This observation suggests that densitometric analysis of immunostained light microscopic sections could provide similar information as the more elaborate and timeconsuming quantitative immunoelectron microscopy. Indeed, densitometry has been used for detection of catalase concentration in DAB-stained light microscopic sections (Geerts and Roels, 1981;Geerts et al, 1984;Kerckaert et al, 1989). The immunohistochemistry, however, is more versatile because it can be used for the investigation of a larger number of enzyme proteins against which an antibody is available.…”

Section: Effect Of Bezafibrate Treatment On Labeling Density Of Peroxmentioning

confidence: 99%

Application of automatic image analysis for quantitative morphological studies of peroxisomes in rat liver in conjunction with cytochemical staining with 3‐3′‐diaminobenzidine and immunocytochemistry

Beier

Fahimi

1992

Microscopy Res & Technique

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We describe the application of automatic image analysis for quantitative morphological studies of peroxisomes in rat liver. For automatic detection by light and electron microscopy peroxisomes must be stained with the alkaline DAB procedure for catalase. There is a good agreement between the results obtained by conventional morphometric techniques and by automatic image analysis of DAB-stained electron microscopic preparations. Moreover, the image analyzer may be used in conjunction with a light microscope for evaluation of semithin sections (1-0.25 microns), provided the section thickness factor is taken into consideration. This latter approach has proven highly efficient in estimation of peroxisome proliferation. The limitations of this method and the relevance of volume density as a reliable morphometric parameter for evaluation of peroxisome proliferation are discussed. In the second part of this study we present the application of image analysis for quantitation of alterations of individual peroxisomal enzyme proteins after treatment with bezafibrate in immunogold stained ultrathin sections. There is good agreement between the results of quantitative immunocytochemistry and Western (immuno) blot analysis of highly purified peroxisomal fractions. In our experience quantitative immunoelectron microscopy provides a versatile, highly sensitive, and efficient method for detection of modulations of various proteins in peroxisomes. Finally the limitations and prospects of quantitative immunocytochemistry for investigation of peroxisomal proteins are discussed.

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“…However, there is also the possibility that the turnover of catalase is increased while synthesis remains unaffected. In the liver, the half-life of catalase is species-dependent and varies from 1.5 to 5 days (Price et al 1962;Jones and Masters 1976;Geerts et al 1984). Degradation of peroxisomes in toto via autophagocytosis was not observed, and inhibition of the enzyme can be ruled out because the antigen is equally disappearing, as detected by the decreasing ␣-catalase immunofluorescence signal.…”

Section: Discussionmentioning

confidence: 98%

“…Granulosa sheets were rinsed twice in homogenization buffer [imidazol-HCl 0.01 M, pH 7.2, containing sucrose (8.5%), EDTA (1 mM), and ethanol (22 mM)] (Geerts et al 1984). Sheets were resuspended in 500-1000 l homogenization buffer and disrupted by sonication (six times for 15 sec) on ice using a Vibracell VC-130 sonicator resulting in an output of 4 W. Protein concentrations were measured according to Bradford (1976) using the BioRad (Hercules, CA) protein assay kit.…”

Section: Staining Of Peroxisomesmentioning

confidence: 99%

Inverse Expression of Peroxisomes and Connexin-43 in the Granulosa Cells of the Quail Follicle

Farioli-Vecchioli

Raes

Espeel

et al. 2000

J Histochem Cytochem.

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SUMMARY Studying the regulation of peroxisome (Px) expression could improve our understanding of human peroxisomal disorders. The granulosa of the largest preovulatory quail follicles proved to be a relevant model because (a) Px expression changes according to the follicular maturation stage and (b) Px expression varies regionally according to the distance of the granulosa relative to the germinal disc region containing the female gamete (oocyte). The question was asked whether Px expression is related to the extent of metabolic cell coupling and whether zonal Px variation is causally related to oocytal factors. This was evaluated by the presence of catalase and Cx-43 (marker proteins for peroxisomes and gap junctions, respectively) and by in vitro experiments with granulosa explants. The data obtained show that the expression of Cx-43 and Px is inversely correlated both temporally and spatially. Uncoupling of gap junctions results in an upregulation of ␣ -catalase immunofluorescence. This is in agreement with reports that gap junctions are often negatively affected by Px proliferators. The zonal gradient in Px expression appears to be imposed by the oocyte, as is the case for steroidogenesis and proliferative capacity in the granulosa epithelium.

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On the topology of the catalase biosynthesis and-degradation in the guinea pig liver

Cited by 27 publications

References 26 publications

Novel insights in mammalian catalase heme maturation: Effect of NO and thioredoxin-1

Novel insights in mammalian catalase heme maturation: Effect of NO and thioredoxin-1

Application of automatic image analysis for quantitative morphological studies of peroxisomes in rat liver in conjunction with cytochemical staining with 3‐3′‐diaminobenzidine and immunocytochemistry

Inverse Expression of Peroxisomes and Connexin-43 in the Granulosa Cells of the Quail Follicle

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