Difference between Guinea Pig and Rat in the Liver Peroxisomal Response to Equivalent Plasmatic Level of Ciprofibrate

Pacot, Corinne; Petit, Michel; Rollin, Michel; Behechti, Ninoufar; Moisant, Maryvonne; Deslex, Paul; Althoff, J.; Lhuguenot, Jean-Claude; Latruffe, Norbert

doi:10.1006/abbi.1996.0107

Cited by 20 publications

(10 citation statements)

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“…As was the case with ALD [15], we did not see any change in the level of PXMP1‐L mRNA after fenofibrate treatment of rats. This would be in accordance with the absence of PPREs in the putative promoter region of the mouse gene although species differences in the action of peroxisome proliferators have been observed [29–31]. From these data and the analysis of tissue expression it can be concluded that there is no apparent pair of peroxisomal ABC half‐transporters showing coordinate expression so that an obligate exclusive dimerization between any two of the four peroxisomal ABC transporters appears to be unlikely.…”

Section: Discussionsupporting

confidence: 67%

The mouse gene encoding the peroxisomal membrane protein 1‐like protein (PXMP1‐L): cDNA cloning, genomic organization and comparative expression studies¹

et al. 1998

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PXMP1-L (synonyms: PMP69, P70R) is a peroxisomal protein that belongs to the ABC-transporter superfamily. Its closest homolog is the peroxisomal membrane protein 1 (PMP70). We have cloned the mouse PXMP1-L gene. It encodes a 606 amino acid protein. In contrast to the human and the rat, mouse PXMP1-L is predominantly expressed in the liver. The mouse PXMP1-L gene consists of 19 exons and spans 21 kb of genomic sequence. No obvious peroxisome proliferator response element has been found in 1.1 kb of the putative promoter region. No coordination of constitutive or fenofibrateinduced expression of PXMP1-L with other peroxisomal ABC transporters was observed so that an obligate exclusive heterodimer formation is not likely to occur. The data presented will be particularly useful for the generation of a mouse model defective in PXMP1-L in order to elucidate the yet unknown function of this protein.z 1998 Federation of European Biochemical Societies.

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Section: Discussionsupporting

confidence: 67%

The mouse gene encoding the peroxisomal membrane protein 1‐like protein (PXMP1‐L): cDNA cloning, genomic organization and comparative expression studies¹

et al. 1998

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“…This mechanism would be consistent with a concerted and reciprocal regulation of glucose and fatty acid metabolism [33]. Whereas fatty acid P-oxidation Finally, other evidence suggests that the level of ciprofibrate-sensitive thiolase mRNA is markedly decreased when cells are exposed to PKC inhibitors [35]. This finding strongly supports the view that fibrate-modulated PKC activity might be important in the regulation of peroxisomal fatty acid /I-oxidation.…”

Section: Protein Kinase C (Pkc) Mediates Peroxisome Proliferator Effectssupporting

confidence: 76%

“…We thank Dr Jean-Piem Zahnd (Faculty of Medicine, Dijon, France) and Dr Paul Deslex (liiboratoires Sterling-Winthrop, Dijon, France) and their teams for collaboration [35] and for performing electron microscopy of guinea-pig liver; and Dr Salish Surapureddi for critical reading ofthe manuscript. This programme is supported by the Regional Council of Burgundy and the Cancer League of Burgundy.…”

mentioning

confidence: 99%

Peroxisome-proliferator-activated receptors as physiological sensors of fatty acid metabolism: molecular regulation in peroxisomes

Latruffe

Cherkaoui-Malki

Nicolas-Francès

et al. 2001

Biochemical Society Transactions

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The enzymes required for the β-oxidation of fatty acyl-CoA are present in peroxisomes and mitochondria. Administration of hypolipidaemic compounds such as clofibrate to rodents leads to an increase in the volume and density of peroxisomes in liver cells. These proliferators also induce simultaneously the expression of genes encoding acyl-CoA oxidase, enoyl-CoA hydratase-hydroxy-acyl-CoA dehydrogenase (multifunctional enzyme) and thiolase (3-ketoacyl-CoA thiolase). All these enzymes are responsible for long-chain and very-long-chain fatty acid β-oxidation in peroxisomes. Similar results were observed when rat hepatocytes, or liver-derived cell lines, were cultured with a peroxisome proliferator. The increased expression of these genes is due to the stimulation of their transcription rate. These results show that the peroxisome proliferators act on the hepatic cells and regulate the transcription through various cellular components and pathways, including peroxisome-proliferatoractivated receptor α (PPARα). After activation by specific ligands, either fibrates or fatty acid derivatives, PPARα binds to a DNA response element: peroxisome-proliferator-responsive element (PPRE), which is a direct repeat of the following consensus sequence: TGACCTXTGACCT, found in the promoter region of the target genes. PPARα is expressed mainly in liver, intestine and kidney. PPARα is a transcriptional factor, which requires other nuclear proteins for function including retinoic acid X receptor (RXRα) and other regulatory proteins. From our results and others we suggest the role of PPARα in the regulation of the peroxisomal fatty acid β-oxidation. In this regard, we showed that although PPARα binds to thiolase B gene promoter at - 681 to - 669, a better response is observed with hepatic nuclear factor 4 (‘HNf-4’). Moreover, rat liver PPARα regulatory activity is dependent on its phosphorylated state. In contrast, a proteinkinase-C-mediated signal transduction pathway seems to be modified by peroxisome proliferators, leading to an increase in the phosphorylation level of specific proteins, some of which have been shown to be involved in the phosphoinositide metabolism.

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“…Peroxisome proliferation is a highly species-specific process occurring in many rodents but not in several other mammalian organisms including guinea pigs, humans, and non-human primates (Fahimi et al, 1993;Pacot et al, 1996). Similarly, peroxisome proliferators elicit liver carcinogenesis only in responsive organisms such as rodents but not in humans.…”

Section: Peroxisome Proliferation Andmentioning

confidence: 96%

Peroxisome proliferation as a biomarker in environmental pollution assessment

Cajaraville

Cancio

Ibabe

et al. 2003

Microscopy Res & Technique

133

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Peroxisome proliferators comprise a heterogeneous group of compounds known for their ability to cause massive proliferation of peroxisomes and liver carcinogenesis in rodents. In recent years it has become evident that other animals may be threatened by peroxisome proliferators, in particular aquatic organisms living in coastal and estuarine areas. These animals are exposed to a variety of pollutants of industrial, agricultural and urban origin which are potential peroxisome proliferators. Both laboratory and field studies have shown that phthalate ester plasticizers, PAHs and oil derivatives, PCBs, certain pesticides, bleached kraft pulp and paper mill effluents, alkylphenols and estrogens provoke peroxisome proliferation in different fish or bivalve mollusc species. The response appears to be mediated by peroxisome-proliferator activated receptors, members of the nuclear receptor family, recently cloned in fish. Based on these results it is proposed that peroxisome proliferation could be used as a biomarker of exposure to a variety of pollutants in environmental pollution assessment. This is illustrated by a case study in which mussels, used worldwide as sentinels of environmental pollution, were transplanted from reference to contaminated areas and vice versa. In mussels native to an area polluted with PAHs and PCBs, peroxisomal acyl-CoA oxidase (AOX) activity and peroxisomal volume density were 2-3 fold and 5-fold higher, respectively, compared to the reference site. When animals were transplanted to the polluted station, with increased concentration of organic xenobiotics, a concomitant significant increase of AOX was recorded. Conversely, in animals transplanted to the cleaner station, AOX activity and peroxisomal volume density decreased significantly. These results indicate that peroxisome proliferation is a rapid (i.e., two days) and reversible response to pollution in mussels. Before peroxisome proliferation can be implemented as a biomarker in biomonitoring programs, a well-defined protocol should be established and validated in intercalibration and quality assurance programmes. Furthermore, the influence of biotic and abiotic factors, some of which are known to affect peroxisome proliferation (season, tide level, interpopulation and interindividual variability), should be taken into consideration. The possible hepatocarcinogenic effects as well as the potential adverse effects on reproduction, development, and growth of peroxisome proliferators are unknown in aquatic organisms, thus providing a challenge for future investigations.

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Difference between Guinea Pig and Rat in the Liver Peroxisomal Response to Equivalent Plasmatic Level of Ciprofibrate

Cited by 20 publications

References 0 publications

The mouse gene encoding the peroxisomal membrane protein 1‐like protein (PXMP1‐L): cDNA cloning, genomic organization and comparative expression studies¹

The mouse gene encoding the peroxisomal membrane protein 1‐like protein (PXMP1‐L): cDNA cloning, genomic organization and comparative expression studies¹

Peroxisome-proliferator-activated receptors as physiological sensors of fatty acid metabolism: molecular regulation in peroxisomes

Peroxisome proliferation as a biomarker in environmental pollution assessment

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Difference between Guinea Pig and Rat in the Liver Peroxisomal Response to Equivalent Plasmatic Level of Ciprofibrate

Cited by 20 publications

References 0 publications

The mouse gene encoding the peroxisomal membrane protein 1‐like protein (PXMP1‐L): cDNA cloning, genomic organization and comparative expression studies1

The mouse gene encoding the peroxisomal membrane protein 1‐like protein (PXMP1‐L): cDNA cloning, genomic organization and comparative expression studies1

Peroxisome-proliferator-activated receptors as physiological sensors of fatty acid metabolism: molecular regulation in peroxisomes

Peroxisome proliferation as a biomarker in environmental pollution assessment

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The mouse gene encoding the peroxisomal membrane protein 1‐like protein (PXMP1‐L): cDNA cloning, genomic organization and comparative expression studies¹

The mouse gene encoding the peroxisomal membrane protein 1‐like protein (PXMP1‐L): cDNA cloning, genomic organization and comparative expression studies¹