Cloning and expression pattern of peroxisomal β-oxidation genes palmitoyl-CoA oxidase, multifunctional protein and 3-ketoacyl-CoA thiolase in mussel Mytilus galloprovincialis and thicklip grey mullet Chelon labrosus

Gene

Volumn 443, Issue 1-2, 2009, Pages 132-142

  Bilbao, Eider ^a   Cajaraville, Miren P ^a   Cancio, Ibon ^a  

^a School of Science and Technology   (Spain)

Author keywords

Chelon labrosus; Mytilus galloprovincialis; Peroxisomal oxidation; Peroxisome proliferation; Peroxisome proliferator response elements

Indexed keywords

ACETYL COENZYME A ACYLTRANSFERASE; PALMITOYL COENZYME A; PEROXISOME PROLIFERATOR; STEROL CARRIER PROTEIN; STEROL CARRIER PROTEIN X; UNCLASSIFIED DRUG; UNSATURATED FATTY ACID; XENOBIOTIC AGENT;

ARTICLE; COMPUTER MODEL; CONTROLLED STUDY; EXOCRINE GLAND; FATTY ACID OXIDATION; FISH; FISH GENETICS; GENE EXPRESSION REGULATION; GENE SEQUENCE; GENETIC CONSERVATION; GENOME ANALYSIS; METAZOON; MOLECULAR CLONING; MOLECULAR MECHANICS; MOLLUSC; MUSSEL; MYTILUS GALLOPROVINCIALIS; NONHUMAN; NUCLEOTIDE SEQUENCE; OPEN READING FRAME; PARALOGY; PEROXISOME; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN DOMAIN; PROTEIN MOTIF; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION;

ACETYL-COA C-ACYLTRANSFERASE; AMINO ACID SEQUENCE; ANIMALS; CLONING, MOLECULAR; FISHES; GENE EXPRESSION; MOLECULAR SEQUENCE DATA; MYTILUS; OXIDOREDUCTASES; PHYLOGENY; SEQUENCE ALIGNMENT; SMEGMAMORPHA;

AMPHIBIA; AVES; CHELON LABROSUS; MAMMALIA; METAZOA; MOLLUSCA; MUGILIDAE; MYTILUS GALLOPROVINCIALIS; PISCES;

EID: 67449084222     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2009.05.008     Document Type: Article

References (71)

1. Andersen O., Eijsink V.G., and Thomassen M. Multiple variants of the peroxisome proliferator-activated receptor (PPAR) gamma are expressed in the liver of Atlantic salmon (Salmo salar). Gene 255 (2000) 411-418
2. Antonenkov V.D., Van Veldhoven P.P., Waelkens E., and Mannaerts G.P. Comparison of the stability and substrate specificity of purified peroxisomal 3-oxoacyl-CoA thiolases A and B from rat liver. Biochim. Biophys. Acta 1437 (1999) 136-141
3. Antonenkov V.D., Croes K., Waelkens E., Van Veldhoven P.P., and Mannaerts G.P. Identification, purification and characterization of an acetoacyl-CoA thiolase from rat liver peroxisomes. Eur. J. Biochem. 267 (2000) 2981-2990
4. Baes M. Inactivation of the peroxisomal multifunctional protein-2 in mice impedes the degradation of not only 2-methyl-branched fatty acids and bile acid intermediates but also of very long chain fatty acids. J. Biol. Chem. 275 (2000) 16329-16336
5. Beier K., and Fahimi H.D. Environmental pollution by common chemicals and peroxisome proliferation: efficient detection by cytochemistry and automatic image analysis. Prog. Histochem. Cytochem. 23 (1991) 150-163
6. Bilbao E., Soto M., Cajaraville M.P., Cancio I., and Marigómez I. Cell and tissue-level biomarkers of pollution in feral pelagic fish, herring (Clupea harengus) and saithe (Pollachius virens), from the North Sea. In: Hylland K., Lang T., and Vethaak D. (Eds). Biological Effects of Contaminants in Marine Pelagic Ecosystems (2006), SETAC Press 121-141
7. Bilbao E., Diaz de Cerio O., Cajaraville M.P., and Cancio I. Cloning and expression pattern of peroxisomal enzymes in the mussel Mytilus galloprovincialis and in the thicklip grey mullet Chelon labrosus: generation of new tools to study peroxisome proliferation. Mar. Environ. Res. 62S (2006) 109-112
8. Bilbao, E., Cajaraville, M.P., Cancio, I., (submitted for publication). Differential expression of genes involved in peroxisome proliferation in thicklip grey mullet Chelon labrosus injected with benzo(a)pyrene.
9. Bodnar A.G., and Rachubinski R.A. Cloning and sequence determination of cDNA encoding a second rat liver peroxisomal 3-ketoacyl-CoA thiolase. Gene 91 (1990) 193-199
10. Boukouvala E., Antonopoulou E., Favre-Krey L., Diez A., Bautista J.M., Leaver M.J., Tocher D.R., and Krey G. Molecular characterization of three peroxisome proliferator-activated receptors from the sea bass (Dicentrarchus labrax). Lipids 39 (2004) 1085-1092
11. Boutet I., Tanguy A., and Moraga D. Response of the Pacific oyster Crassostrea gigas to hydrocarbon contamination under experimental conditions. Gene 329 (2004) 147-157
12. Cajaraville M.P., and Ortiz-Zarragoitia M. Specificity of the peroxisome proliferation response in mussels exposed to environmental pollutants. Aqua. Toxicol. 78S (2006) 117-123
13. Cajaraville M.P., Cancio I., Ibabe A., and Orbea A. Peroxisome proliferation as biomarker in environmental pollution assessment. Microscopy Res. Tech. 61 (2003) 191-202
14. Cancio I., and Cajaraville M.P. Cell biology of peroxisomes and their characteristics in aquatic organisms. Int. Rev. Cytol. 199 (2000) 201-293
15. Cancio I., Ibabe A., and Cajaraville M.P. Seasonal variation of peroxisomal enzyme activities and peroxisomal structure in mussels Mytilus galloprovincialis and its relationship with the lipid content. Comp. Biochem. Physiol. 123C (1999) 135-144
16. Cancio I., Völkl A., Beier K., Fahimi H.D., and Cajaraville M.P. Peroxisomes in molluscs, characterization by subcellular fractionation combined with western blotting, immunohistochemistry, and immunocytochemistry. Histochem. Cell Biol. 113 (2000) 51-60
17. Chevillard G. Molecular cloning, gene structure and expression profile of two mouse peroxisomal 3-ketoacyl-CoA thiolase genes. BMC Biochem. 5 (2004) 3
18. Crockett E.L., and Sidell B.D. Peroxisomal β-oxidation is a significant pathway for catabolism of fatty acids in a marine teleost. J. Physiol. 264R (1993) 1004-1009
19. Crockett E.L., and Sidell B.D. Substrate selectivities differ for hepatic mitochondrial and peroxisomal β-oxidation in an Antarctic fish, Notothenia gibberifrons. Biochem. J 289 (1993) 427-433
20. Deridovich I.I., and Reunova O.V. Prostaglandins: reproduction control in bivalve molluscs. Comp. Biochem. Physiol. 104A (1993) 23-27
21. Dreyer C., Krey G., Keller H., Givel F., Helftenbein G., and Wahli W. Control of the peroxisomal β-oxidation pathway by a novel family of nuclear hormone receptors. Cell 68 (1992) 879-887
22. Emanuelsson O., Elofsson A., Von Heijne G., and Cristóbal S. In silico prediction of the peroxisomal proteome in fungi, plants and animals. J. Mol. Biol. 330 (2003) 443-456
23. Galay-Burgos M., Gealy C., Navarro-Martín L., Piferrer F., Zanuy S., and Sweeney G.E. Cloning of the promoter from the gonadal aromatase gene of the European sea bass and identification of single nucleotide polymorphisms. Comp. Biochem. Physiol. 145A (2006) 47-53
24. Gardner L., Anderson T., Place A.R., Dixon B., and Elizur A. Sex change strategy and the aromatase genes. J. Steroid Biochem. Mol. Biol. 94 (2005) 395-404
25. Goldberg E.D. The mussel watch. A first step in global marine monitoring. Mar. Pollut. Bull. 6 (1975) 111
26. Hansmannel F., Clèmencet M.C., Le Jossic Corcos C., Osumi T., Latruffe N., and Nicolas-Francés V. Functional characterization of a peroxisome proliferator response-element located in the intron 3 of rat peroxisomal thiolase B gene. Biochem. Biophys. Res. Commun. 311 (2003) 149-155
27. Hashimoto T. Peroxisomal β-oxidation enzymes. Neurochem. Res. 24 (1999) 551-563
28. Hijikata M., Wen J.K., Osumi T., and Hashimoto T. Rat peroxisomal 3-ketoacyl-CoA thiolase gene. Occurrence of two closely related but differentially regulated genes. J. Biol. Chem. 265 (1990) 4600-4606
29. Hiltunen J.K., and Qin Y.M. β-oxidation strategies for the metabolism of a wide variety of acyl-CoA esters. Biochim. Biophys. Acta 1484 (2000) 117-128
30. Hooks M.A., Kellas F., and Graham I.A. Long-chain acyl-CoA oxidases of Arabidopsis. Plant J. 20 (1999) 1-13
31. Huyghe S., Mannaerts G.P., Baes M., and Van Veldhoven P.P. Peroxisomal multifunctional protein-2: the enzyme, the patients and the knockout mouse model. Biochim. Biophys. Acta 1761 (2006) 973-994
32. Ibabe A., Granbenbauer M., Baumgart E., Völkl A., Fahimi H.D., and Cajaraville M.P. Expression of peroxisome proliferator-activated receptors in the liver of gray mullet (Mugil cephalus). Acta Histochem. 106 (2004) 11-19
33. Inoue H. Endogenous ligands for PPARs. Nippon Rinsho Jpn. J. Clin. Med. 63 (2005) 578-583
34. Keller H., and Wahli W. Peroxisome proliferator-activated receptors. A link between endocrinology and nutrition?. Trends Endocrinol. Metab. 4 (1993) 291-296
35. Keller J.M. Implications of peroxisome proliferator-activated receptors (PPARs) in development, cell life status and disease. Inter. J. Dev. Biol. 44 (2000) 429-442
36. Kiema T.R., Taskinen J.K., Pirilä P.L., Koivuranta K.T., Wierenga R.K., and Hiltunen J.K. Organization of the multifunctional enzyme type 1: interaction between N-and C-terminal domains is required for the hydrates-1/isomerase activity. Biochem. J. 367 (2002) 433-441
37. Kim J.J., and Battaile K.P. Burning fat: the structural basis of fatty acid beta-oxidation. Curr. Opin. Struct. Biol. 12 (2002) 721-728
38. Kunau W.H., Dommes V., and Schulz H. Beta-oxidation of fatty acids in mitochondria, peroxisomes and bacteria: a century of continued progress. Prog. Lipid Res 34 (1995) 267-342
39. Leaver M.J., Wright J., and George S.G. Structure and expression of a cluster of glutathione S-transferase genes from a marine fish, the plaice (Pleuronectes platessa). Biochem. J. 321 (1997) 405-412
40. Leaver M.J. Three peroxisomal proliferator-activated receptor isotypes from each of two species of marine fish. Endocrinology 146 (2005) 3150-3162
41. Lei Z., Chen W., Zhang M., and Napoli J.L. Reduction of all-trans-retinal in the mouse liver peroxisome fraction by the short-chain dehydrogenase/reductase RRD: induction by the PPARα ligand clofibrate. Biochemistry 42 (2003) 4190-4196
42. Lukyanova O.N., and Khotimchenko Y.S. Lipid peroxidation in organs of the scallop Mizuhopecten yessoensis and sea-urchin Strongylocentrotus intermedius during the reproductice cycle. Comp. Biochem. Physiol. 110B (1995) 371-377
43. Mandard S., Müller M., and Kersten S. Peroxisome proliferator-activated receptor α target genes. Cell. Mol. Life Sci. 61 (2004) 393-416
44. Mannaerts G.P., and Van Veldhoven P.P. Metabolic pathways in mammalian peroxisomes. Biochimie 75 (1993) 145-158
45. Mannaerts G.P., Van Veldhoven P.P., and Casteels M. Peroxisomal lipid degradation via β-and α-oxidation in mammals. Cell Biochem. Biophys. 32 (2000) 73-87
46. Masters C.J. On the role of the peroxisome in the metabolism of drugs and xenobiotics. Biochem. Pharmacol. 56 (1998) 667-673
47. Miyata K.S., McCaw S.E., Marcus S.L., Rachubinski R.A., and Capone J.P. The peroxisome proliferator-activated receptor interacts with the retinoid X receptor in vivo. Gene 148 (1994) 327-330
48. Miyazawa S. Complete nucleotide sequence of cDNA and predicted amino acid sequence of rat acyl-CoA oxidase. J. Biol. Chem. 262 (1987) 8131-8137
49. Morais S., Knoll-Gellida A., Andrè M., Barthe C., and Babin P.J. Conserved expression of alternative splicing variants of peroxisomal acyl-CoA oxidase I in vertebrates and developmental and nutritional regulation in fish. Physiol. Genomics 28 (2007) 239-252
50. Moroz L.L. Neuronal Transcriptome of Aplysia: neuronal compartments and circuitry. Cell 127 (2006) 1453-1467
51. Nevejan N., Saez I., Gajardo G., and Sorgeloos P. Energy vs. essential fatty acids: what do scallop larvae (Argopecten purpuratus) need most?. Comp. Biochem. Physiol. 134B (2003) 599-613
52. Ngo S.N., Mckinnon R.A., and Stupans I. Identification and cloning of two forms of liver peroxisomal fatty acyl CoA oxidase from the koala (Phascolarctos cinereus). Gene 309 (2003) 91-99
53. Nocillado J.N., Elizur A., Avitan A., Carrick F., and Levavi-Sivan B. Cytochrome P450 aromatase in grey mullet: cDNA and promoter isolation; brain, pituitary and ovarian expression during puberty. Mol. Cell. Endocrinol. 263 (2007) 65-78
54. Nöhammer C. cDNA cloning and analysis of tissue-specific expression of mouse peroxisomal straight-chain acyl-CoA oxidase. Eur. J. Biochem. 267 (2000) 1254-1260
55. Orbea A., and Cajaraville M.P. Peroxisome proliferation and antioxidant enzymes in transplanted mussels of four basque estuaries with different levels of polycyclic aromatic hydrocarbon and polychlorinated biphenyl pollution. Environ. Toxicol. Chem. 25 (2006) 1616-1626
56. Orbea A., Beier K., Völkl A., Fahimi H.D., and Cajaraville M.P. Ultraestructural, immunocytochemical and morphometric chracterization of liver peroxisomes in gray mullet, Mugil cephalus. Cell Tiss. Res. 297 (1999) 493-502
57. Ortiz-Zarragoitia M., and Cajaraville M.P. Effects of selected xenoestrogens on liver peroxisomes, vitellogenin levels and spermatogenic cell proliferation in male zebrafish. Comp. Biochem. Physiol. 141C (2005) 133-144
58. Osumi T., Hashimoto T., and Ui N. Purification and properties of acyl CoA oxidase from rat liver. J. Biochem. 87 (1980) 1735-1746
59. Raingeard D., Cancio I., and Cajaraville M.P. Cloning and expression pattern of peroxisome proliferator-activated receptor alpha in the thicklip grey mullet Chelon labrosus. Mar. Environ. Res. 62S (2006) 113-117
60. Raingeard D., Cancio I., and Cajaraville M.P. Cloning and expression pattern of peroxisome proliferator-activated receptors, retinoid X receptor α and estrogen receptor α in the thicklip grey mullet Chelon labrosus. Comp. Biochem. Physiol. Toxicol. Pharmacol. 149 (2009) 26-35
61. Raingeard, D., 2008. Peroxisome proliferator-activated receptors (PPARs) and other nuclear receptors in aquatic organisms: cloning and gene expression studies in relation to environmental contamination. European PhD Thesis, University of the Basque Country, pp. 477.
62. Reddy J.K., and Hashimoto T. Peroxisomal β-oxidation and peroxisome proliferator-activated receptor α: an adaptive metabolic system. Annu. Rev. Nutr. 21 (2001) 193-230
63. Rocha E., Lobo-Da-Cunha A., Monteiro R.A.F., Silva M.W., and Oliveira M.H. A stereological study along the year on the hepatocytic peroxisomes of brown trout (Salmo trutta). J. Submicrosc. Cytol. Pathol. 31 (1999) 91-105
64. Sampath H., and Ntambi J.M. Polyunsaturated fatty acid regulation of genes of lipid metabolism. Annu. Rev. Nutr. 25 (2005) 317-340
65. Scarano L.J., Calabrese E.J., Kostecki P.T., Baldwin L.A., and Laonard D.A. Evaluation of a rodent peroxisome proliferator in two species of freshwater fish: rainbow trout (Onchorynchus mykiss) and Japanese medaka (Oryzias latipes). Ecotoxicol. Environ. Saf. 29 (1994) 13-19
66. Schulz H. Regulation of fatty acid oxidation in heart. J. Nutr. 124 (1994) 165-171
67. Setoyama C., Tamaoki H., Nishina Y., Shiga K., and Miura R. Functional expression of two forms of rat acyl-CoA oxidase and their substrate specificities. Biochem. Biophys. Res. Commun. 217 (1995) 482-487
68. Tocher D.R. Metabolism and functions of lipids and fatty acids in teleost fish. Rev. Fish. Sci. 11 (2003) 107-184
69. Williams T.D. Development of the GENIPOL European Flounder (Platichthys flesus) microarray and determination of the temporal transcriptional responses to cadmium at low dose. Environ. Sci. Technol. 40 (2006) 6479-6488
70. Yang J.H., Kostecki P.T., Calabrese E.J., and Baldwin L.A. Induction of peroxisome proliferation in rainbow trout exposed to ciprofibrate. Toxicol. Appl. Pharmacol. 104 (1990) 476-482
71. Zhang B. Identification of a peroxisome proliferator-responsive element upstream of the gene encoding rat peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 7541-7545