Biogenesis of peroxisomes: immunocytochemical investigation of peroxisomal membrane proteins in proliferating rat liver peroxisomes and in catalase-negative membrane loops.

Baumgart, Eveline; Völkl, Alfred; Hashimoto, Takashi; Fahimi, H. Dariush

doi:10.1083/jcb.108.6.2221

Cited by 61 publications

(37 citation statements)

References 66 publications

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“…Serial section analysis revealed the presence of apparent "peroxisomes" physically continuous to the double-membraned loop. Such a structural transition has been reported in the hepatocytes of rats treated with a peroxisome proliferator (BM 15766;Baumgart et al, 1989). Area 4, the space between two double membranes, had an electron den- sity similar to that of the cytosol, and sometimes a singlemembraned structure was found inside ( Figure 5D, closed circle).…”

Section: Peroxisomal Ghosts In the Pex6-deficient Mutant Are Complex mentioning

confidence: 83%

“…They had no segmentation, and the space between the two membrane layers was smaller than that in ER. They probably corresponded to the structures reported as "double-membraned loops" in the hepatocytes of the rat treated with an inhibitor of cholesterol biosynthesis (BM15766; Baumgart et al, 1989) or in the hepatocytes of the PEX5 knockout mouse (Baes et al, 1997). Almost always, the double-membraned loops of ZP92 and ZP92/GFPSKL cells were accompanied by another type of structures ( Figure 5B, open triangles).…”

Section: Electron Microscopic Analysis Of Zp92 and Zp92/ Gfpskl Cellsmentioning

confidence: 97%

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Peroxisomes Are Formed from Complex Membrane Structures inPEX6-deficient CHO Cells upon Genetic Complementation

Hashiguchi

Kojidani

Imanaka³

et al. 2002

MBoC

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Pex6p belongs to the AAA family of ATPases. Its CHO mutant, ZP92, lacks normal peroxisomes but contains peroxisomal membrane remnants, so called peroxisomal ghosts, which are detected with anti-70-kDa peroxisomal membrane protein (PMP70) antibody. No peroxisomal matrix proteins were detected inside the ghosts, but exogenously expressed green fluorescent protein (GFP) fused to peroxisome targeting signal-1 (PTS-1) accumulated in the areas adjacent to the ghosts. Electron microscopic examination revealed that PMP70-positive ghosts in ZP92 were complex membrane structures, rather than peroxisomes with reduced matrix protein import ability. In a typical case, a set of one central spherical body and two layers of double-membraned loops were observed, with endoplasmic reticulum present alongside the outer loop. In the early stage of complementation by PEX6 cDNA, catalase and acyl-CoA oxidase accumulated in the lumen of the double-membraned loops. Biochemical analysis revealed that almost all the peroxisomal ghosts were converted into peroxisomes upon complementation. Our results indicate that 1) Peroxisomal ghosts are complex membrane structures; and 2) The complex membrane structures become import competent and are converted into peroxisomes upon complementation with PEX6.

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Section: Peroxisomal Ghosts In the Pex6-deficient Mutant Are Complex mentioning

confidence: 83%

Section: Electron Microscopic Analysis Of Zp92 and Zp92/ Gfpskl Cellsmentioning

confidence: 97%

Peroxisomes Are Formed from Complex Membrane Structures inPEX6-deficient CHO Cells upon Genetic Complementation

Hashiguchi

Kojidani

Imanaka³

et al. 2002

MBoC

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“…The heterogeneous particulate distribution of iNOS was further characterized using the peroxisomal membrane protein PMP70 as a peroxisomal marker. 19,20 Anti-PMP70 labels only the peroxisomal membrane. This additional marker was chosen because catalase is known to be down-regulated under conditions of septic shock.…”

Section: Pattern Of Inos Expression Varies With Timementioning

confidence: 99%

“…This additional marker was chosen because catalase is known to be down-regulated under conditions of septic shock. [20][21][22][23] Moreover, peroxisomes have microdomains devoid of catalase. 20 As early as 4 hours after cytokine stimulation, a small number of cells visibly expressed iNOS, and that expression was predominantly within the peroxisomal matrix (Fig.…”

Section: Pattern Of Inos Expression Varies With Timementioning

confidence: 99%

Peroxisomal localization of inducible nitric oxide synthase in hepatocytes

et al. 2002

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Shock states induce the expression of inducible nitric oxide synthase (iNOS) in both Kupffer cells and hepatocytes in the liver, but little is known about its subcellular localization in these cells. Studies were undertaken to characterize the subcellular location of iNOS in hepatocytes in response to sepsis. By immunofluorescence analysis, intraperitoneal challenge with bacterial lipopolysaccharide induced cytosolic iNOS in Kupffer cells but punctate labeling in hepatocytes. Cultured rat hepatocytes exposed to interferon gamma, interleukin 1, and tumor necrosis factor ␣ showed iNOS protein expression within peroxisomes as early as 4 hours after stimulation, as determined by colabeling for catalase or PMP70. To a lesser extent, iNOS was also observed associated with the plasma membrane and in undefined intracellular aggregates. S tudies in the past decade have shown that all nitric oxide synthases (NOS), whether constitutive or inducible, are regulated at transcriptional, posttranscriptional, translational, and posttranslational levels. 1 One important aspect of NOS regulation is its subcellular localization. For example, endothelial NOS is localized to the caveolae of endothelial cells, where direct association with caveolin I regulates enzyme activity. 2 Such localization may enhance NO function by concentrating NO release close to the cell surface. The inducible NOS (iNOS; NOS2) isoform, which contributes to inflammatory processes through high NO output, is regulated positively and negatively by cytokines but can also be controlled posttranslationally by NO and/or its reaction products. 1,3,4 Furthermore, this enzyme is found in both particulate and cytosolic cellular pools. 5 Our interest has focused on the regulation and function of iNOS in the liver. This enzyme is readily upregulated in hepatocytes, 6 and human iNOS expression was first detected in hepatocytes. 7 In vivo studies have shown that the consequences of iNOS up-regulation in liver are dependent on the physiologic or pathologic circumstances. Following conditions associated with severe redox stress, iNOS contributes to hepatocellular damage during hemorrhagic shock or hepatic ischemia/reperfusion. 8,9 In contrast, iNOS-generated NO suppresses hepatocyte apoptosis in endotoxemia 10 and following cytokine exposure. 11 To better understand how iNOS functions within hepatocytes as well as factors that might determine the fate of NO in the liver, we undertook a study to characterize its subcellular localization. We show that iNOS localizes to the peroxisome, plasma membrane, and cytoplasm. Interestingly, increased expression of iNOS is associated with decreased catalase expression.

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“…Adequately perfused tissue was immersed for 30 min (4°C) in freshly prepared fixative. Sections 50-100 pm thick, cut with an Oxford Vibratome, were either postfixed by the reduced osmium procedure of Karnovsky (1971), dehydrated and embedded in Epon 812, or embedded in LR White (Newman et al, 1983) as described by Baumgart et al (1989).…”

Section: Immunohisto-and Cytochemical Studiesmentioning

confidence: 99%

Light and electron microscopic localization of D-aspartate oxidase in peroxisomes of bovine kidney and liver: an immunocytochemical study.

Zaar

1996

J Histochem Cytochem.

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D-Aspartate oxidase (EC 1.4.3.1; D-ASPOX) specifically oxidizes the D-isomers of dicarboxylic amino acids such as aspartic or glutamic acid. Subcellular fractionation experiments in the past showed its association with peroxisome preparations in kidney cortex and liver. However, no information exists on the in situ localization and distribution of the enzyme in different cell types. We have purified the enzyme from the bovine kidney and raised an antibody against it in rabbits. The monospecificity of the antibody has been confirmed by Western blotting and it does not crossreact with D-amino, acid oxidase. Immunohistochemical localization of the antigen in bovine kidney and liver with the streptavidin-biotin-peroxidase technique revealed a punctate localization in the epithelial cells of proximal nephron tubules, particularly in the straight P-3 segment, as well as in hepatocytes. This is consistent with a localization in peroxisomes. Best results have been obtained with Carnoy-fixed material after paraffin embedding or after fixation with formaldehyde-glutaraldehyde in cryostat sections. Immunoelectron microscopy with protein A-gold confirms the peroxisomal localization of D-ASPOX. Gold particles are distributed over the matrix, suggestive of a peroxisomal matrix enzyme. This is the first report on the localization of D-ASPOX, a little-known peroxisomal enzyme. The techniques described and the antibody prepared will now allow systematic investigation of its tissue distribution.

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Biogenesis of peroxisomes: immunocytochemical investigation of peroxisomal membrane proteins in proliferating rat liver peroxisomes and in catalase-negative membrane loops.

Cited by 61 publications

References 66 publications

Peroxisomes Are Formed from Complex Membrane Structures inPEX6-deficient CHO Cells upon Genetic Complementation

Peroxisomes Are Formed from Complex Membrane Structures inPEX6-deficient CHO Cells upon Genetic Complementation

Peroxisomal localization of inducible nitric oxide synthase in hepatocytes

Light and electron microscopic localization of D-aspartate oxidase in peroxisomes of bovine kidney and liver: an immunocytochemical study.

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