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  • Articles: DFG German National Licenses  (17)
  • 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
    Uptake of horseradish peroxidase (HRP) by the endothelium of the short-term stored rabbit cornea (1976)
    Springer
    Graefe's archive for clinical and experimental ophthalmology 199 (1976), S. 157-166 
    Details
    ISSN: 1435-702X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Die Aufnahme der Meerrettich-Peroxidase (MPO) durch das Endothel der Kaninchenhornhaut wurde in vitro untersucht. Die Hornhäute waren in einem Konservierungsmedium verschiedene Zeiten gelagert worden. Diese konservierten Hornhäute wurden in der MPO-Lösung mit oder ohne Adenosintriphosphat (ATP) inkubiert. Die Zahl der Pinocytosevesikel nahm bei Verlängerung der Lagerungszeit ab. Wurde ATP zur MPO-Lösung zugegeben nahm die Zahl der Pinocytosevesikel bei allen Lagerungszeiten zu. Bei Hornhäuten, die 12 Tage konserviert worden waren, konnte eine Pinocytose nur beobachtet werden, wenn das Gewebe in einer ATP-haltigen MPO-Lösung inkubiert worden war. Auf Grund dieser Ergebnisse kann die Lebensfähigkeit des konservierten Hornhautendothels durch die Aufnahme der Meerrettich-Peroxidase beurteilt werden.
    Notes: Summary In vitro study of the uptake of horseradish peroxidase (HRP) by the corneal endothelium was carried out on rabbit corneae which were stored in a preserving medium for various periods. The stored corneae were incubated in HRP solution with or without adenosine triphosphate (ATP). The number of pinocytotic vesicles decreased as the storage time was prolonged. Addition of ATP to the HRP solution led to an increase in the pinocytotic vesicles in all storage periods. The pinocytosis in the 12-day stored corneal endothelium was only observed when the tissue was incubated in an HRP solution containing ATP. From these results, it was concluded that the viability of the stored cornea can be evaluated with uptake of HRP by the endothelial cell, and that the addition of ATP leads to an enhancement of pinocytotic activity in the endothelial cell.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02385212
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  • 4
    Electronic Resource
    Electronic Resource
    Histochemical evaluation of enzymes in the rabbit corneal endothelium after short-term storage (1976)
    Springer
    Graefe's archive for clinical and experimental ophthalmology 200 (1976), S. 59-69 
    Details
    ISSN: 1435-702X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Description / Table of Contents: Zusammenfassung Isolierte Kaninchenhornhäute wurden in modifiziertem McCoy 5a-Medium mit 5% Dextran T 40 und Gentamycinsulfat (250 μg/ml) gelagert. Die Konservierungsdauer betrug 1, 3, 6, 8, 10, 12 und 18 Tage bei + 4°C. Die Enzymaktivitäten des Hornhautendothels (ATPase, TPPase und SDH) wurden licht- und elektronenmikroskopisch untersucht. Die Aktivität jedes einzelnen Enzyms in Hornhäuten, die bis zu 6 Tagen gelagert worden waren, glichen den Enzymaktivitäten in frischen Endothelzellen. Nach 8 Tagen Konservierungsdauer war die SDH-Aktivität erniedrigt, die spezifische Anfärbbarkeit für ATPase und TPPase war vermindert. Nach 12-tägiger Lagerung konnte für SDH und TPPase keine spezifische Aktivität mehr entdeckt werden. Auf Grund dieser Ergebnisse kann eine Hornhaut, die 6 Tage bei + 4°C in dem Medium gelagert worden war, für eine erfolgreiche perforierende Keratoplastik verwendet werden.
    Notes: Summary Isolated rabbit corneae were stored at a temperature of 4° C in McCoy's 5a medium (modified) containing 5% dextran T 40 and gentamycin sulphate (250 μg/ml) for a varied number of days. The endothelium of the corneae was examined by light- and electron-microscopic histochemical methods for ATPase, TPPase, and SDH. The activity of each enzyme in the endothelia, stored for 6 days, was found to resemble the enzyme activities in the fresh corneal endothelium. By 8 days, the SDH activity was lowered and specific staining for ATPase and TPPase was decreased. In the 12 day-stored endothelium, the SDH and TPPase activities could not be detected. From these results, it was gathered that the isolated cornea stored in the medium for 6 days may be used in keratoplasty.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00411433
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    Paper (German National Licenses)
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  • 5
    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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  • 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
    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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  • 8
    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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  • 9
    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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  • 10
    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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