High prealbumin and transferrin mRNA levels in the choroid plexus of rat brain

Dickson, Phillip W.; Aldred, Angela R.; Marley, Philip D.; Tu, Guo-Fen; Howlett, Geoffrey J.; Schreiber, Gerhard

doi:10.1016/s0006-291x(85)80027-9

Cited by 177 publications

(61 citation statements)

References 13 publications

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“…Similar peptides such as cholecystokinin and gastrin, exist in both brain parenchyma and gut, although they may play different functional roles depending on the organs where they are present, namely as neuromodulators in the brain and as hormones in the gut. In this context a novel concept "brain-liver proteins" may be proposed based upon our finding on AFP in conjunction with previous reports by others on the presence of prealbumin (4,6,13), transferrin (2,6) and ceruloplasmin (3). However, it should be noted that positive immunoreactivity for AFP shown here does not imply synthesis of AFP in the choroid plexus epithelium.…”

Section: Lettersupporting

confidence: 64%

.ALPHA.-Fetoprotein Immunoreactivity in Human Choroid Plexus.

Fushiki¹,

Yamazaki²,

Fujita

1994

Acta Histochem. Cytochem

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Section: Lettersupporting

confidence: 64%

.ALPHA.-Fetoprotein Immunoreactivity in Human Choroid Plexus.

Fushiki¹,

Yamazaki²,

Fujita

1994

Acta Histochem. Cytochem

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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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“…TTR is mainly synthesized in the liver and the choroid plexus of the brain, which contribute, respectively, to the plasma and CSF pool of the protein (2,3).…”

Section: Introductionmentioning

confidence: 99%

Aboard transthyretin: From transport to cleavage

et al. 2010

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SummaryTransthyretin (TTR) is a plasma and cerebrospinal fluid protein mainly recognized as the transporter of thyroxine (T 4 ) and retinol. Mutated TTR leads to familial amyloid polyneuropathy, a neurodegenerative disorder characterized by TTR amyloid deposition particularly in peripheral nerves. Beside its transport activities, TTR is a cryptic protease and participates in the biology of the nervous system. Several studies have been directed at finding new ligands of TTR to further explore the biology of the protein. From the identified ligands, some were in fact TTR protease substrates. In this review, we will discuss the existent information concerning TTR ligands/substrates. 2010 IUBMB IUBMB Life, 62(6): [429][430][431][432][433][434][435] 2010

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High prealbumin and transferrin mRNA levels in the choroid plexus of rat brain

Cited by 177 publications

References 13 publications

.ALPHA.-Fetoprotein Immunoreactivity in Human Choroid Plexus.

.ALPHA.-Fetoprotein Immunoreactivity in Human Choroid Plexus.

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

Aboard transthyretin: From transport to cleavage

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