Localization of immunoreactive transthyretin (prealbumin) and of transthyretin mRNA in fetal and adult rat brain

Kato, Michimasa; Soprano, Dianne Robert; Makover, Adina; Kato, K; Herbert, Joseph; Goodman, DeWitt S.

doi:10.1111/j.1432-0436.1986.tb00402.x

Cited by 49 publications

(17 citation statements)

References 29 publications

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“…It appears that the choroid plexus epithelium synthesizes transthyretin and secretes it into the cerebrospinal fluid. We have also observed immunoreactive transthyretin in the tela choroidea (at 11 days of gestation) and in the choroid plexus (at 14 and 18 days of gestation) of the developing rat brain (45). In addition, we have detected transthyretin mRNA in the brains of rat fetuses of 16, 18, and 20 days of gestation (45).…”

Section: Discussionmentioning

confidence: 55%

“…We have also observed immunoreactive transthyretin in the tela choroidea (at 11 days of gestation) and in the choroid plexus (at 14 and 18 days of gestation) of the developing rat brain (45). In addition, we have detected transthyretin mRNA in the brains of rat fetuses of 16, 18, and 20 days of gestation (45). The relative levels of transthyretin mRNA in the fetal brain averaged about 40% of the adult brain or about 10%-15% of the adult liver.…”

Section: Discussionmentioning

confidence: 75%

“…High levels of transthyretin mRNA have been found in the adult rat brain, specifically localized in the choroid plexus epithelium (14,44,45). It appears that the choroid plexus epithelium synthesizes transthyretin and secretes it into the cerebrospinal fluid.…”

Section: Discussionmentioning

confidence: 98%

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Retinol-binding protein and transthyretin mRNA levels in visceral yolk sac and liver during fetal development in the rat.

Soprano¹,

Soprano²,

Goodman³

1986

Proc. Natl. Acad. Sci. U.S.A.

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Studies were conducted to explore the synthesis of retinol-binding protein and transthyretin by embryonic and extraembryonic tissues during fetal development in the rat. The levels of retinol-binding protein mRNA and transthyretin mRNA were measured in fetal liver and in extraembryonic tissues by RNA gel blot analysis and hybridization with specific cDNA probes. Retinol-binding protein mRNA and transthyretin mRNA were both detected in the liver of fetuses at 14 days of gestation. The relative levels of these two transcripts increased during later fetal development; by the 20th day of gestation retinol-binding protein mRNA levels were comparable to those of the adult liver, while the levels of transthyretin mRNA were only 46% of those of the adult liver. Examination of the extraembryonic membranes for retinolbinding protein mRNA and transthyretin mRNA showed that these two transcripts were present specifically and only in the visceral yolk sac. The relative levels of retinol-binding protein mRNA and transthyretin mRNA in visceral yolk sac were constant from 14 to 20 days of gestation, averaging 58% and 51 %, respectively, of the adult liver levels of these two transcripts. Both retinol-binding protein mRNA and transthyretin mRNA in the visceral yolk sac were found to be specifically localized in the endodermal layer. Finally, both immunoprecipitable retinol-binding protein and transthyretin were found to be synthesized and secreted by explant cultures of visceral yolk sac tissue. These data show that the visceral yolk sac is a major source of both retinol-binding protein and transthyretin in the developing fetus. Since the visceral yolk sac is a site of true placentation and nutrient transfer in the rodent, this raises the possibility that visceral yolk sac-derived retinolbinding protein and transthyretin may play important roles in the transport and delivery of retinol from the maternal blood to the developing fetus.Vitamin A is an indispensable nutrient for normal fetal growth and development in many different species of animals (1-4). Although there is a large amount of information concerning the plasma transport of retinol (for review, see ref. 5), the mechanism of transplacental transport of retinol from maternal blood to the developing fetus is not well understood.In plasma, two proteins are involved in the transport of retinol from the liver to extrahepatic tissues. Retinol-binding protein is a 20-to 21-kDa protein that has one binding site for one molecule of retinol (5-7). Holo-retinol-binding protein strongly interacts in the plasma with transthyretin (previously referred to as prealbumin) and normally circulates as a 1:1 molar retinol-binding protein-transthyretin complex (8, 9). Plasma transthyretin is a 54.9-kDa tetrameric protein composed of four identical subunits (10). In addition to having binding sites for retinol-binding protein, transthyretin also possesses binding sites for thyroid hormones (11, 12). The liver serves as a major site of synthesis ofboth retinol-binding protein and tran...

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Section: Discussionmentioning

confidence: 55%

Section: Discussionmentioning

confidence: 75%

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Retinol-binding protein and transthyretin mRNA levels in visceral yolk sac and liver during fetal development in the rat.

Soprano¹,

Soprano²,

Goodman³

1986

Proc. Natl. Acad. Sci. U.S.A.

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“…Their morphological and functional differences can now be correlated with the presence or absence of two molecular markers; choroidal, but not ependymal, cells transcribe the rIGF-II and transthyretin genes. Transthyretin (prealbumin), a transport protein for retinol and thyroxin, is synthesized de novo in the choroidal epithelium and then secreted into the CSF (36)(37)(38)(39).…”

Section: Resultsmentioning

confidence: 99%

Expression of the insulin-like growth factor II gene in the choroid plexus and the leptomeninges of the adult rat central nervous system.

Stylianopoulou

Herbert

Soares³

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

219

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Expression of the insulin-like growth factor II gene in the choroid plexus and the leptomeninges of the adult rat central nervous system ( (4)(5)(6). Transcription from P1 generates the 5' noncoding exon E1(1) (1125 nucleotides; nt), whereas transcription from P2 generates an alternate 5' noncoding exon, E1(2) (94 nt). The two predominant mature mRNAs [4.5 and 3.5 kilobases (kb)] consist of either E1(1) or E1(2), respectively, connected to three additional exons (E2, 163 nt; E3, 149 nt; and E4, 3.1 kb). Among the several other transcripts, a P2-specific mRNA (1.1 kb) includes only a portion of E4 (the first 650 nt) and is generated by differential polyadenylylation.The rIGF-II gene transcripts are present in all fetal or neonatal tissues that we have examined, but they are extremely rare or undetectable in adult tissues, with the exception of the brain and the spinal cord (4). Similar observations have been made by other investigators (5,(7)(8)(9) (10). For RNA blot hybridization, RNA was electrophoresed on formaldehyde/1% agarose gels and then transferred onto nylon membranes. Prehybridization and hybridization were as described (11). The hybridization probes were either uniformly 32P-labeled, mRNA-complementary, singlestranded DNA synthesized on M13 templates (12) or DNA fragments labeled by randomly primed synthesis using pd(N)6 primers, [a-32P]dNTPs, and Klenow enzyme as described (13). S1 nuclease-protection analysis was done as described (4).In Situ Hybridization. Tissues from Sprague-Dawley rats were sectioned and prepared for in situ hybridization as described (14). Hybridization, followed by washing under stringent conditions, autoradiography, exposure to photoemulsion, development, and counterstaining with hematoxylin/eosin were as described (15). The RNA hybridization probes were prepared as follows. A 545-base pair (bp) coding region fragment from rIGF-II cDNA clone 27 (4) was isolated. This fragment extends between a BamHI site located one nucleotide downstream from the ATG initiator and an EcoRI linker present at the end of the fragment three nucleotides downstream from the TGA terminator. The fragment was subcloned into the BamHI and EcoRI sites of the pGEM-1 vector polylinker. Transcription with 17 polymerase from BamHI-linearized plasmid generated antisense probe, whereas transcription with SP6 polymerase from EcoRIlinearized plasmid generated sense (control) probe. Transcription reactions with these polymerases (10-,A vol each) were performed according to the manufacturer's specifications, using 25 ,uM 35S-UTP, 500 The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.

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“…Transthyretin is one of the few proteins identified in the cerebrospinal fluid (CSF), that is synthesized in the choroid plexus (Kato et al 1986) and may have a function in the transport of thyroxine through the blood-CSF barrier (Dickson et al 1987). It is possible that chemicals interacting with transthyretin may affect the transport function of the choroid plexus with possible consequences for brain functions.…”

Section: -Sec-butylphenol (Dinoseb)mentioning

confidence: 99%

Interactions of halogenated industrial chemicals with transthyretin and effects on thyroid hormone levels in vivo

Berg¹,

Raaij²,

Bragt³

et al. 1991

Arch Toxicol

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Previous results in experimental systems have suggested that hydroxylated PCBs may decrease thyroid hormone levels through associative interaction with transthyretin. In the present paper it was investigated whether this property was also shared by various industrial chemicals, mainly pesticides. In total, 65 compounds from 12 chemical groups were analyzed for direct interference with the T4 binding site of transthyretin using a competitive binding assay. Sixty per cent of the compounds were competitive at a concentration level of 100 microM. Relatively strong interactions were observed by several chlorophenols, chlorophenoxy acids and nitrophenols, as well as by individual compounds such as hexachlorobenzene, dicofol, bromoxynil and tetrachlorohydroquinone. Examples from these chemical groups, e.g. pentachlorophenol, 2,4-dichlorophenoxybutyric acid, dinoseb and bromoxynil, also reduced plasma TT4 levels in rats. In addition, bromoxynil decreased plasma TT3 levels. The results suggest the existence of a number of halogenated industrial chemicals with a potential for lowering plasma thyroid hormone levels through interference with hormone transport carriers.

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Localization of immunoreactive transthyretin (prealbumin) and of transthyretin mRNA in fetal and adult rat brain

Cited by 49 publications

References 29 publications

Retinol-binding protein and transthyretin mRNA levels in visceral yolk sac and liver during fetal development in the rat.

Retinol-binding protein and transthyretin mRNA levels in visceral yolk sac and liver during fetal development in the rat.

Expression of the insulin-like growth factor II gene in the choroid plexus and the leptomeninges of the adult rat central nervous system.

Interactions of halogenated industrial chemicals with transthyretin and effects on thyroid hormone levels in vivo

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