Ontogenesis of transthyretin gene expression in chicken choroid plexus and liver

Southwell, Bridget R.; Duan, Wei; Tu, Guo-Fen; Schreiber, Gerhard

doi:10.1016/0305-0491(91)90383-o

Cited by 27 publications

(20 citation statements)

References 45 publications

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“…We suggest that the first and probably still the most important function of transthyretin is to create an extracellular thyroxine pool in the central nervous system . Expression of the transthyretin gene in the liver of birds Southwell et al, 1991;Richardson et al, 1994) -YWKALGISPE * * * s * * * * * * * * * * * * * * * * ********** ***T****** ******v*** ******v*** **pJ***v*** ******v*** I ***TF***** ***G**L*** (Tu et al, 1989), rat (Dickson et al, 1985b;Duan et al, 1989), mouse (Wakasugi et al, 1985), Tammar wallaby (M. eugenii, Brack et al, 1994), the lizard Tiliqua rugosa (Achen et al, 1993) and the sequences for the sugar glider P. breviceps, the dunnart S. rnacrouru and the opossum M. dornestica, described in this paper, are aligned with the deduced amino acid sequence of human transthyretin (Mita et al, 1984). The N-terminal residue of mature transthyretin (designated + I ) has been identified for human (Kanda et al, 1974), rabbit (Sundelin et al, 1985), rat (Navab et al, 1977), chicken and M. dornesticu (this paper), but has been inferred for mouse, sugar glider, dunnart and sheep from this alignment.…”

Section: Resultsmentioning

confidence: 99%

Evolution of Transthyretin in Marsupials

Duan

Richardson

Babon

et al. 1995

European Journal of Biochemistry

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The evolution of the expression and the structure of the gene for transthyretin, a thyroxine-binding plasma protein formerly called prealbumin, was studied in three marsupial species : the South American polyprotodont Monodelphis domestica, the Australian polyprotodont Sminthopsis macroura and the Australian diprotodont Petaurus breviceps. The transthyretin gene was found to be expressed in the choroid plexus of all three species. In liver it was expressed in P. breviceps and in M. domestica, but not in S.macroura. This, together with previous studies [Richardson, S. J., Bradley, A. J., Duan, W., Wettenhall, R. E. H., Harms, P. J., Babon, J. J., Southwell, B. R., Nicol, S., Donnellan, S. C. & Schreiber, G. (1994) Am. .I. Physiol. 266, R1359 -R1370], suggests the independent evolution of transthyretin synthesis in the liver of the American Polyprotodonta and the Australian Diprotodonta.The results obtained from cloning and sequencing of the cDNA for transthyretin from the three species suggested that, in the evolution of the structure of transthyretin in vertebrates, marsupial transthyretin structures are intermediate between birdreptile and eutherian transthyretin structures. In marsupials, as in birds and reptiles, a hydrophobic tripeptide beginning with valine and ending with histidine was found in transthyretin at a position which has been identified in eutherians as the border between exon 1 and intron 1. In humans, rats and mice, the nine nucleotides, coding for this tripeptide in marsupials/reptiles/ birds, are found at the 5' end of intron 1. They are no longer present in mature transthyretin mRNA. This results in a change in character of the N-termini of the subunits of transthyretin from hydrophobic to hydrophilic. This change might affect the accessibility of the thyroxine-binding site in the central channel of tr,ansthyretin, since, at least in humans, the N-termini of the subunits of transthyretin are located in the vicinity of the channel entrance [Hamilton,

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Section: Resultsmentioning

confidence: 99%

Evolution of Transthyretin in Marsupials

Duan

Richardson

Babon

et al. 1995

European Journal of Biochemistry

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“…TTR has a fairly restricted gene expression, being demonstrated principally in the liver and choroid plexus of rat Fung et al, 1988;Schreiber et al, 1990), human (Dickson and Schreiber, 1986), sheep (Schreiber et al, 1990), pig , and chicken (Southwell et al, 1991) and in the liver of marsupials (Richardson et al, 1994). In two reptiles, the turtle (Trachemys scripta) and lizard (Tiliqua rugosa), TTR is present in the brain but little or no expression has been detected in the liver (Achen et al, 1993;Richardson et al, 1997).…”

Section: Transthyretin Gene Expressionmentioning

confidence: 99%

Evolution of the Thyroid Hormone-Binding Protein, Transthyretin

Power

Elias

Richardson

et al. 2000

General and Comparative Endocrinology

193

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Transthyretin (TTR) belongs to a group of proteins, which includes thyroxine-binding globulin and albumin, that bind to and transport thyroid hormones in the blood. TTR is also indirectly implicated in the carriage of vitamin A through the mediation of retinol-binding protein (RBP). It was first identified in 1942 in human serum and cerebrospinal fluid and was formerly called prealbumin for its ability to migrate faster than serum albumin on electrophoresis of whole plasma. It is a single polypeptide chain of 127 amino acids (14,000 Da) and is present in the plasma as a tetramer of noncovalently bound monomers. The major sites of synthesis of TTR in eutherian mammals, marsupials, and birds are the liver and choroid plexus but in reptiles it is synthesised only in the choroid plexus. The observation that TTR is strongly expressed in the choroid plexus but not in the liver of the stumpy-tailed lizard and the strong conservation of expression in the choroid plexus from reptiles to mammals have been taken as evidence to suggest that extrahepatic synthesis of TTR evolved first. The identification and cloning of TTR from the liver of an amphibian, Rana catesbeiana, and a teleost fish, Sparus aurata, and its absence from the choroid plexus of both species suggest an alternative model for its evolution. Protein modelling studies are presented that demonstrate differences in the electrostatic characteristics of the molecule in human, rat, chicken, and fish, which may explain why, in contrast to TTR from human and rat, TTR from fish and birds preferentially binds triiodo-L-thyronine.

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“…The tissue pattern and the timing of transthyretin and lipocalin gene expression during ontogenesis in the bullfrog (this report) greatly differ from those in eutherian [61,62] or avian species [63]. The expression of the transthyretin gene in the early stages of development, and its cessation during further development and differentiation, described here, is seen in no other vertebrate class studied to date.…”

Section: Discussionmentioning

confidence: 59%

“…In the rat, a eutherian altricial species, the transthyretin gene begins to be expressed in the fetal liver during midgestation, and transthyretin mRNA levels steadily increase thereafter to reach 40% of the adult levels by birth [61]. In sheep and chicken, precocial eutherian species, transthyretin mRNA appears in the embryonic liver after the first third of the prenatal period and reaches adult levels at birth [63,64]. Expression of the transthyretin gene in the developing rat choroid plexus is initiated at approximately the same time as in the fetal liver [61].…”

Section: Discussionmentioning

confidence: 99%

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Structural characteristics of bullfrog (Rana catesbeiana) transthyretin and its cDNA

Yamauchi

Takeuchi

Overall

et al. 1998

European Journal of Biochemistry

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Transthyretin, an extracellular thyroid-hormone-binding protein (THBP) in higher vertebrates, is synthesized and secreted by the choroid plexus of all classes of vertebrates, except fish and amphibians, and synthesized in the liver of endothermic animals. Here, we report the nucleotide sequence of the cDNA for a THBP found in plasma of bullfrog (Rana catesbeiana) tadpoles before the climax of metamorphosis.The amino acid sequence clearly shows this protein to be an amphibian transthyretin. The three-dimensional structure of bullfrog transthyretin was derived using homology modeling. Compared with transthyretins from other vertebrate species, bullfrog transthyretin is highly conserved at the thyroid hormonebinding sites and other important structural regions of the subunits. Bullfrog transthyretin mRNA was found in tadpole liver, but not in tadpole choroid plexus. Thus, during evolution, synthesis of transthyretin in the liver of metamorphosing amphibians preceded that in the choroid plexus of reptiles, birds and mammals. It was previously observed that the protein most abundantly synthesized and secreted by the choroid plexus in adult amphibians is a lipocalin [Achen, M. G., Harms, P. J., Thomas, T., Richardson, S. J., Wettenhall, R. E. H. & Schreiber, G. (1992) J. Biol. Chem. 267, 23170Ϫ23 174], in contrast to transthyretin being the most abundantly synthesized and secreted protein in the choroid plexus of mammals, birds and reptiles. Lipocalin mRNA was found in large amounts in tadpole choroid plexus, but not livers. Keywords : transthyretin; lipocalin ; metamorphosis; bullfrog (Rana catesbeiana).Amphibian metamorphosis can be induced by both thyroxine and 3,3′,5-triiodothyronine [1], and is regulated via the hypothalamus-pituitary-thyroid gland axis, which is established just before the onset of metamorphosis [2]. The concentration of thyroid hormones in the blood increases gradually during prometamorphosis, reaches a maximum level at the beginning of metamorphic climax, and then decreases and ceases to be detectable at the end of metamorphosis [3,4]. Thyroid hormone receptors, the genes of which are thought to be among the earliest genes responding to the elevation of thyroid hormone concentration in blood plasma, are upregulated in several tissues during both spontaneous and induced metamorphosis [5,6], and in cell-culture systems [7,8]. Thus, amphibian metamorphosis has provided a good model for analyzing the control of gene expression by thyroid hormones [9Ϫ11]. However, it is still unclear how thyroid hormones are delivered to target cells. Previously, the presence of a thyroid hormone-binding protein (THBP) in blood plasma from metamorphosing Rana catesbeiana (bullfrog) tadpoles had been described [12]. This THBP had a higher affinity Correspondence to K. Yamauchi,

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Ontogenesis of transthyretin gene expression in chicken choroid plexus and liver

Cited by 27 publications

References 45 publications

Evolution of Transthyretin in Marsupials

Evolution of Transthyretin in Marsupials

Evolution of the Thyroid Hormone-Binding Protein, Transthyretin

Structural characteristics of bullfrog (Rana catesbeiana) transthyretin and its cDNA

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