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  • 1
    Electronic Resource
    Electronic Resource
    Cytosolic and mitochondrial isoforms of NADP+-dependent isocitrate dehydrogenases are expressed in cultured rat neurons, astrocytes, oligodendrocytes and microglial cells (2003)
    Oxford, UK : Blackwell Science Ltd
    Journal of neurochemistry 86 (2003), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: NADP+-dependent isocitrate dehydrogenases (ICDHs) are enzymes that reduce NADP+ to NADPH using isocitrate as electron donor. Cytosolic and mitochondrial isoforms of ICDH have been described. Little is known on the expression of ICDHs in brain cells. We have cloned the rat mitochondrial ICDH (mICDH) in order to obtain the sequence information necessary to study the expression of ICDHs in brain cells by RT-PCR. The cDNA sequence of rat mICDH was highly homologous to that of mICDH cDNAs from other species. By RT-PCR the presence of mRNAs for both the cytosolic and the mitochondrial ICDHs was demonstrated for cultured rat neurons, astrocytes, oligodendrocytes and microglia. The expression of both ICDH isoenzymes was confirmed by western blot analysis using ICDH-isoenzyme specific antibodies as well as by determination of ICDH activities in cytosolic and mitochondrial fractions of the neural cell cultures. In astroglial and microglial cultures, the total ICDH activity was almost equally distributed between cytosolic and mitochondrial fractions. In contrast, in cultures of neurons and oligodendrocytes about 75% of total ICDH activity was present in the cytosolic fractions. Putative functions of ICDHs in cytosol and mitochondria of brain cells are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1471-4159.2003.01871.x
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  • 2
    Electronic Resource
    Electronic Resource
    THE SHORT- AND LONG-TERM EFFECTS OF BEZAFIBRATE IN THE RAT (1982)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 386 (1982), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1982.tb21410.x
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  • 3
    Electronic Resource
    Electronic Resource
    Peroxisome assembly factor–2, a putative ATPase cloned by functional complementation on a peroxisome–deficient mammalian cell mutant (1995)
    [s.l.] : Nature Publishing Group
    Nature genetics 11 (1995), S. 395-401 
    Details
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Rat peroxisome assembly factor–2 (PAF–2) cDNA was isolated by functional complementation of peroxisome deficiency of a mutant CHO cell line, ZP92, using transient transfection assay. This cDNA encodes a 978–amino acid protein with two putative ATP–binding sites. PAF–2 ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/ng1295-395
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  • 4
    Electronic Resource
    Electronic Resource
    Enzyme cytochemical localization of sarcosine oxidase activity in the liver and kidney of several mammals (2000)
    Springer
    Histochemistry and cell biology 113 (2000), S. 489-495 
    Details
    ISSN: 1432-119X
    Keywords: Enzyme cytochemistry Sarcosine oxidase Peroxisomes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. We investigated the enzyme cytochemical localization of sarcosine oxidase (SOX) in the liver and kidney of several mammals using a cerium technique. First we measured the enzyme activities in the liver and kidney of several mammals and in several organs of mice. The highest activity was found in the Chinese hamster, followed by the mouse. Therefore, we used hamster and mouse tissues for enzyme cytochemistry. The liver and kidneys were fixed by perfusion with various concentrations of glutaraldehyde for 10 min. Tissue slices were incubated in reaction medium consisting of 50 mM TRIS-maleate buffer (pH 7.8), 9 mM sodium azide, 9.8 mM sarcosine, 25 µM FAD, 2 mM cerium chloride, 0.002% saponin, and 0.003% Triton X-100 for 0.5–8 h at 37°C. Optimum staining reaction was obtained in tissues fixed with 0.2% glutaraldehyde, followed by incubation for 2–4 h. Electron-dense reaction products were present exclusively in peroxisomes. Within the peroxisomes strong reactions were observed in the matrix subjacent to the limiting membrane decreasing toward the center. The staining reaction was completely inhibited by 2 mM N-bromosuccinimide. These results indicated that SOX is a peroxisomal enzyme and that the enzyme might be associated with the peroxisomal membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180000161
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  • 5
    Electronic Resource
    Electronic Resource
    Aggregate formation and degradation of overexpressed wild-type and mutant urate oxidase proteins. Quality control of organelle-destined proteins by the endoplasmic reticulum (2000)
    Springer
    Histochemistry and cell biology 114 (2000), S. 433-446 
    Details
    ISSN: 1432-119X
    Keywords: Protein quality control Ubiquitination Aggregate formation ER
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. To analyze the cellular response caused by the overexpression of proteins in subcellular compartments, we constructed four expression clones encoding wild-type peroxisomal urate oxidase (UO), truncated UO lacking the peroxisomal targeting signal (UOdC), and chimeric UOs with a mitochondrial targeting signal (MTS) at the N-terminus of UOdC (MUOdC) or UO (MUO). After transfection, we examined COS-1 and HEK293 cells by immunofluorescence and immunoelectron microscopy, transmission electron microscopy, and pulse-chase experiments. The overexpressed UO and UOdC formed large electron-dense aggregates with no limiting membrane in both the cytoplasm and the nucleus. The UO aggregates exhibited the crystalloid structure quite similar to that of rat liver peroxisomal cores, whereas the UOdC aggregates formed a loose mass consisting of small dense substructures. The overexpressed MUOdC and MUO, on the other hand, formed other types of aggregates which were distributed in the cytoplasm. They consisted of tubular and circular membrane structures, which were morphologically confirmed to be derived from the endoplasmic reticulum (ER). No immunolabeling signals for MUOdC and MUO were present free in the cytoplasm and most of them were associated with membrane structures, suggesting that overexpressed UO containing the MTS attached to the ER membranes soon after synthesis and segregated from the cytosolic compartment. All the UO aggregates were stained for ubiquitin antigen. Pulse-chase experiments in combination with proteasome inhibitors suggested that proteasomes did not contribute to the degradation of these products.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180000208
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  • 6
    Electronic Resource
    Electronic Resource
    Immunocytochemical localization of L-α-hydroxyacid oxidase in dense bar of dumb-bell-shaped peroxisomes of monkey kidney (1995)
    Springer
    Histochemistry and cell biology 104 (1995), S. 55-61 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Localization of the B of L-αhydroxyacid oxidase (HOX-B) in monkey kidney peroxisomes was investigated by immunoelectron microscopic techniques. Kidneys of Japanese monkeys,Macaca fuscata, were fixed with 4% paraformaldehyde+0.25% glutaraldehyde and embedded in LR White resin. Thin sections were stained for HOX-B and catalase by the immunogold technique. HOX-B was localized in the marginal plates of normal peroxisomes and the dense bar of dumb-bellshaped peroxisomes. Catalase was detected in the matrix of normal peroxisomes and in the terminal dilatations of dumb-bell-shaped peroxisomes. There were no gold particles indicating presence of catalase associated with the marginal plates or with the dense bars. Immunoblot analysis of monkey kidney homogenate showed that HOX-B has a molecular mass of 42 kDa that was slightly larger than that of rat kidney HOX-B (39 kDa). The results show that the dense bar of dumb-bell-shaped peroxisomes in monkey kidney is composed of at least HOX-B and is a variation of the marginal plates.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01464786
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  • 7
    Electronic Resource
    Electronic Resource
    Studies on mouse liver urate oxidase (1973)
    Springer
    Histochemistry and cell biology 36 (1973), S. 21-27 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The localization of urate oxidase in mouse liver was investigated by fluorescent antibody technique. The fluorescence was observed in the cytoplasm and fine granules scattering throughout the cytoplasm of liver cells. The diffuse cytoplasmic fluorescence around the central vein was somewhat stronger than that of the medial and outer zone of hepatic lobule. Nuclei of the liver cell and stellate cell of Kuppfer were not stained.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00310117
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  • 8
    Electronic Resource
    Electronic Resource
    Immunolocalization of cellular glutathione peroxidase in adult rat lungs and quantitative analysis after postembedding immunogold labeling (1996)
    Springer
    Histochemistry and cell biology 105 (1996), S. 383-389 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract To determine the distribution of cellular glutathione peroxidase in rat lungs, the tissues were stained immunohistochemically. Quantitative analysis was performed in certain cell types of alveolar linings, after the ultrathin sections were stained by a postembedding immunogold technique. Immunoblot analysis revealed that homogenates of rat liver, heart, and lungs all gave a single band. Under the light microscope, the following tissues were stained intensely: epithelial cells, smooth muscle cells and glands of bronchi and bronchioles, type II alveolar cells, and alveolar macrophages. Under immunoelectron microscopy, type II alveolar cells and macrophages were abundant in mitochondria. The mitochondria, nucleus, and cytoplasm of macrophages were labeled almost twice as densely as the respective compartments of type II alveolar cells. Within cell types, the mitochondria were labeled twice as densely as the nuclei. The other particles were less than half as densely labeled as the nuclei. The labeling was slightly less dense in the cytoplasm than in the nucleus. The present study revealed that glutathione peroxidase occurred predominantly in the epithelial linings and metabolically active sites in rat lungs. The tissues that were previously found to be rich in superoxide dismutases were also rich in glutathione peroxidase.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01463659
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  • 9
    Electronic Resource
    Electronic Resource
    Studies on mouse liver urate oxidase (1974)
    Springer
    Histochemistry and cell biology 39 (1974), S. 243-250 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The fine localization of urate oxidase was investigated with immunoferritin technique directly applied to ultrathin sections of fixed and frozen mouse liver tissue. The ferritin particles indicating the urate oxidase antigen were localized in microbodies, cisternae of rough- and smooth-surfaced endoplasmic reticulum (ER), and Golgi vacuoles and vesicles. In ER the particles were abundantly observed in dilated terminal portions. In addition, Golgi lamellae were slightly stained comparing with the vacuoles and vesicles. The staining with ferritin particles was inhibited by the treatment of unconjugated anti-urate oxidase before ferritin conjugate staining. From these results, the formation of microbody was discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00493309
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  • 10
    Electronic Resource
    Electronic Resource
    Ultrastructural localization of catalase on ultracryotomic sections of mouse liver by ferritin-conjugated antibody technique (1974)
    Springer
    Histochemistry and cell biology 40 (1974), S. 165-174 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Ferritin labeled antibody to mouse liver catalase was applied to ultracryotomic sections of mouse liver tissue. The ferritin particles indicating a catalase antigen were localized in microbodies, membran-ebound ribosomes, cisternae of endoplasmic reticulum, Golgi vacuoles and vesicles, and cytoplasmic matrix of liver cell. Infrequently, the ferritin particles were observed in a few lysosomes of the hepatic cell and the stellate cell of Kupffer and in perichromatin of the hepatic cell nucleus. To the contray, mitochondria, Golgi lamellae, plasma membranes, and most of nuclei and lysosomes were not stained by ferritin conjugate. The results were discussed with regard to enzymecytochemical and biochemical results described by several investigators.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00495964
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