Ligand-dependent transcriptional activities of four torafugu pufferfish Takifugu rubripes peroxisome proliferator-activated receptors.

Structural and functional properties were investigated for four peroxisome proliferator-activated receptors (PPARs), PPARalpha1, PPARalpha2, PPARbeta, and PPARgamma, from torafugu pufferfish Takifugu rubripes and determined for their transcriptional activity by the reporter assay using reporter plasmids containing three copies of the acyl-CoA oxidase PPAR response element. Although torafugu PPARs showed a high similarity in the primary structure to other vertebrate counterparts, torafugu PPARalpha2 and gamma contained additional sequences of 21 and 28 amino acids, respectively, as in the case of other teleost fish species when compared with African clawed frog counterparts. The transcriptional activity of torafugu PPARalpha1 was enhanced 4.

Identification of three isoforms for mitochondrial adenine nucleotide translocator in the pufferfish Takifugu rubripes.

Three adenine nucleotide translocator (ANT) genes were identified through in silico data mining of the Fugu genome database along with isolation of their corresponding cDNAs in vivo from the pufferfish (Takifugu rubripes). As a result of phylogenetic analysis, the ANT gene on scaffold_254 corresponded to mammalian ANT1, whereas both of those on scaffold_6 and scaffold_598 to mammalian ANT3. The ANT gene encoded by scaffold_6 was expressed ubiquitously in various tissues, whereas the ANT genes encoded by scaffold_254 and scaffold_598 were predominantly expressed in skeletal muscle and heart, respectively.

Characterization of the pufferfish Takifugu rubripes apolipoprotein multigene family.

We have characterized the apolipoprotein multigene family of the pufferfish Takifugu rubripes. The pufferfish mainly contains 28-kDa, 27-kDa, and 14-kDa apolipoproteins in its plasma and was designated apo-28 kDa, apo-27 kDa, and apo-14 kDa, respectively. N-terminal amino acid sequencing revealed that pufferfish apo-28 kDa and apo-27 kDa have an identical amino acid sequence except an additional propeptide in the former; and both are homologues of apoA-I from other animals.