Molecular characterization of three peroxisome proliferator-activated receptors from the sea bass (Dicentrarchus labrax).
Peroxisome proliferator-activated receptors (PPAR) are nuclear hormone receptors that control the expression of genes involved in lipid homeostasis in mammals. We searched for PPAR in sea bass, a marine fish of particular interest to aquaculture, after hypothesizing that the physiological and molecular processes that regulate lipid metabolism in fish are similar to those in mammals. Here, we report the identification of complementary DNA and corresponding genomic sequences that encode three distinct PPAR from sea bass. The sea bass PPAR are the structural homologs of the mammalian PPAR alpha, beta/delta, and gamma isotypes. As revealed by RNase protection, the tissue expression profile of the fish PPAR appears to be very similar to that of the mammalian PPAR homologs. Thus, PPAR alpha is mainly expressed in the liver, PPAR gamma in adipose tissue, and PPAR beta in all tissues tested, with its highest levels in the liver, where it is also the dominant isotype expressed. Like mammalian PPAR, the sea bass isotypes recognize and bind to PPAR response elements of both mammalian and piscine origin, as heterodimers with the 9-cis retinoic acid receptor. Through the coactivator-dependent receptor ligand assay, we also demonstrated that natural FA and synthetic hypolipidemic compounds can act as ligands of the sea bass PPAR alpha and beta isotypes. This suggests that the sea bass PPAR act through similar mechanisms and perform the same critical lipid metabolism functions as mammalian PPAR.
Boukouvala
Evridiki
E
National Agricultural Research Foundation-Fisheries Research Institute, Nea Peramos, 64007 Kavala, Greece.
Antonopoulou
Efthimia
E
Favre-Krey
Laurence
L
Diez
Amalia
A
Bautista
José M
JM
Leaver
Michael J
MJ
Tocher
Douglas R
DR
Krey
Grigorios
G
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001492:Bass / Q000235:genetics / Q000378:metabolism*; D018076:DNA, Complementary / Q000235:genetics; D019281:Dimerization; D020869:Gene Expression Profiling; D016678:Genome; D006801:Humans; D008024:Ligands; D008969:Molecular Sequence Data; D047492:Peroxisome Proliferator-Activated Receptors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D018168:Receptors, Retinoic Acid / Q000378:metabolism; D020218:Response Elements / Q000235:genetics; D016415:Sequence Alignment
D018076:DNA, Complementary; D008024:Ligands; D047492:Peroxisome Proliferator-Activated Receptors; D020033:Protein Isoforms; D018168:Receptors, Retinoic Acid
Endocr Rev. 1999 Oct;20(5):649-88
10529898
Endocrinology. 2001 Oct;142(10):4195-202
11564675
Biochem J. 1997 Jan 15;321 ( Pt 2):405-12
9020873
Cell. 2003 Apr 18;113(2):159-70
12705865
EMBO J. 1998 Jan 2;17(1):232-43
9427757
J Steroid Biochem Mol Biol. 1993 Dec;47(1-6):65-73
8274443
Mol Endocrinol. 1997 Jun;11(6):779-91
9171241
Cell. 1995 Dec 1;83(5):813-9
8521498
Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13919-24
11698662
Biol Cell. 1993;77(1):67-76
8390886
Nature. 1998 Sep 10;395(6698):137-43
9744270
Gene. 2000 Sep 19;255(2):411-8
11024302
Genome Res. 2001 May;11(5):781-8
11337474
Cell. 1992 Mar 6;68(5):879-87
1312391
Genes Dev. 1994 May 15;8(10 ):1224-34
7926726
Biochim Biophys Acta. 1996 Jan 19;1299(2):235-44
8555269
Endocrinology. 1998 Jun;139(6):2748-54
9607781
Endocrinology. 1996 Jan;137(1):354-66
8536636
Proc Natl Acad Sci U S A. 1995 Aug 15;92(17):7921-5
7644514
Proc Natl Acad Sci U S A. 1993 Mar 15;90(6):2160-4
8384714
Proc Natl Acad Sci U S A. 1997 Apr 29;94(9):4318-23
9113987
Proc Natl Acad Sci U S A. 1997 Apr 29;94(9):4312-7
9113986
Annu Rev Med. 2002;53:409-35
11818483
J Biol Chem. 1997 Aug 8;272(32):20108-17
9242684