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1.
J Food Prot ; 71(3): 595-601, 2008 Mar.
Article in English | MEDLINE | ID: mdl-18389706

ABSTRACT

Substantial amounts of mercury are usually present in tuna muscle, with levels in excess of 10 times the standard safety value present in some individuals. Inspection of individual fish for mercury content would be desirable but may not be cost-effective. In this study, we tried to establish a low-cost system for checking the mercury content of tuna by using a tail muscle that is usually discarded. The samples used in this experiment were bluefin tuna, cultured in the Fisheries Laboratory of Kinki University (Oshima Experimental Station, Wakayama, Japan). They were raised from eggs spawned in 2002. Ninety-eight individuals, weighing 22.3 to 61.6 kg, were selected between December 2004 and November 2005. In nine individuals, the mercury content of the tail was compared with that of the whole body. The total mercury level was measured using the reduction vaporizing atomic absorption method after acid digestion. Except for the front of the abdomen, where the mercury content was lower (0.490 ppm), the mercury content of other parts of the fish did not differ from that of the tail muscle (0.631 ppm). Therefore, the overall mercury concentration in bluefin tuna could be estimated to be almost the same and/or lower than that of the tail muscle. On the basis of these results, for 1 year we investigated the quantity of mercury in full-cycle cultured bluefin tuna that were shipped. The mercury concentration showed no increase irrespective of increases of body weight.


Subject(s)
Food Contamination/analysis , Mercury/analysis , Seafood/analysis , Tuna/metabolism , Water Pollutants, Chemical/analysis , Animals , Consumer Product Safety , Environmental Monitoring/methods , Food Analysis , Humans , Muscle, Skeletal/chemistry , Quality Control , Seafood/standards , Tail/chemistry , Tissue Distribution
2.
Gen Comp Endocrinol ; 155(3): 597-606, 2008 Feb 01.
Article in English | MEDLINE | ID: mdl-17988667

ABSTRACT

We studied the profiles of 3,5,3'-l-triiodothyronine (T3), thyroxine (T4), and thyroid hormone receptors (TRs) in Pacific bluefin tuna (Thunnus orientalis) during embryonic and post-embryonic development. Both T3 and T4 were detected in embryos just before hatching, and it was found that the levels of both were increased in postflexion fish. The thyroid follicles were increased in both size and number in postflexion fish compared with preflexion fish. A TRbeta cDNA clone was generated by RACE. Two TRalpha cDNA clones were also partially identified and analyzed by real-time RT-PCR in this study. The TR mRNA levels in embryos were determined, and these were found to be lower than those in preflexion fish. Therefore, we considered that thyroid hormones function during early post-embryonic development as well as during embryonic development. Moreover, there was a peak in the TR mRNA level during postflexion stages, as seen during metamorphosis in Japanese flounder and Japanese conger eel. It is possible that thyroid hormones control the early development of scombrid fish through TRs, as they do for Pluronectiformes and Anguilliformes.


Subject(s)
Receptors, Thyroid Hormone/genetics , Thyroid Hormones/metabolism , Tuna/growth & development , Tuna/genetics , Amino Acid Sequence , Animals , Base Sequence , DNA, Complementary/isolation & purification , DNA, Complementary/metabolism , Embryo, Nonmammalian , Gene Expression Regulation, Developmental , Life Cycle Stages/genetics , Life Cycle Stages/physiology , Models, Biological , Molecular Sequence Data , Phylogeny , Sequence Homology, Amino Acid , Thyroid Gland/anatomy & histology , Thyroid Gland/embryology , Thyroid Gland/growth & development , Time Factors , Tuna/embryology , Tuna/metabolism
3.
Zoolog Sci ; 23(5): 443-8, 2006 May.
Article in English | MEDLINE | ID: mdl-16766863

ABSTRACT

A cDNA encoding transthyretin was cloned from the Pacific bluefin tuna (Thunnus orientalis). This cDNA contains a complete open reading frame encoding 151 amino acid residues. The deduced amino acid sequence is 81% and 55% identical to the gilthead seabream and common carp forms, respectively, and 33-39% to mammalian, reptilian, and amphibian forms. A 1.0-kb transcript was found in the the liver and ovary; the liver is the main source of this protein. Analysis of triiodo-L-thyronine (T(3)) and L-thyroxine (T(4)) binding demonstrated that both T(3) and T(4) bind to bluefin transthyretin. The binding activity of T(3) for bluefin transthyretin is higher than that of T(4). These results indicate that bluefin transthyretin acts as a transporter of thyroid hormones (THs) in the plasma, and plays an important role in the function of THs in target cells.


Subject(s)
DNA, Complementary/analysis , Liver/metabolism , Prealbumin/genetics , Prealbumin/isolation & purification , Thyroid Hormones/metabolism , Tuna/metabolism , Amino Acid Sequence , Animals , Base Sequence , DNA, Complementary/chemistry , Female , Gene Expression , Male , Molecular Sequence Data , Open Reading Frames , Ovary/metabolism , Prealbumin/chemistry , RNA, Messenger/biosynthesis , Reverse Transcriptase Polymerase Chain Reaction/veterinary , Sequence Alignment , Sequence Homology, Nucleic Acid , Thyroxine/metabolism , Triiodothyronine/metabolism , Tuna/blood
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