Evidence map›Paper›PMID 8668154›Full record

ArticleMolecular and cellular biology1996

Intron retention generates a novel isoform of the murine vitamin D receptor that acts in a dominant negative way on the vitamin D signaling pathway.

K Ebihara, Y Masuhiro, T Kitamoto, M Suzawa, Y Uematsu, T Yoshizawa, T Ono, H Harada, K Matsuda, T Hasegawa and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
7.0field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 83 citations in OpenAlex.

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  18. Multiple promoters direct the tissue-specific expression of novel N-terminal variant human vitamin D receptor gene transcripts.Proceedings of the National Academy of Sciences of the United States of America · 1998
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 2 institutions in 2 countries.

K EbiharaDepartment of Agricultural Chemistry, Tokyo University of Agriculture, Setagayaku, Japan.
Y Masuhiro
T Kitamoto
M Suzawa
Y Uematsu
T Yoshizawa
T Ono
H Harada
K Matsuda
T Hasegawa
S Masushige
S Kato
Tokyo University of Agriculture · JPDivision of Molecular & Cellular Biosciences · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We identified and characterized a novel rat vitamin D receptor isoform (rVDR1), which retains intron 8 of the canonical VDR (rVDR0) during alternative splicing. In this isoform protein directed by the stop codon in this newly identified exon, a part of the ligand binding domain (86 amino acids) is truncated at the C-terminal end but contains 19 extra amino acids. The rVDR1 transcript was expressed at a level 1/15 to 1/20 of that of rVDR0 in the kidney and intestine in adult rats but not in embryos. The recombinant rVDR1 protein showed no ligand binding activity. Homo- and heterodimers of the recombinant rVDR0 and rVDR1 proteins bound to a consensus vitamin D response element (VDRE) but not to consensus response elements for thyroid hormone and retinoic acid. However, unlike rVDR0, rVDR1 did not form a heterodimeric complex with RXR on the VDRE. A transient expression assay showed that this isoform acted as a dominant negative receptor against rVDR0 transactivation. Interestingly, the dominant negative activities of rVDR1 differed among VDREs. Thus, the present study indicates that this new VDR isoform negatively modulates the vitamin D signaling pathway, through a particular set of target genes.

Indexed as

Alternative SplicingIntronsAmino Acid SequenceAnimalsBase SequenceCalcitriolChloramphenicol O-AcetyltransferaseEmbryo, MammalianHeLa CellsHumansIntestinal MucosaKidneyMolecular Sequence DataOligonucleotide ProbesPolymerase Chain ReactionRatsCalcitriolChloramphenicol O-AcetyltransferaseOligonucleotide ProbesReceptors, CalcitriolReceptors, Retinoic AcidRecombinant Fusion ProteinsRetinoid X ReceptorsTranscription FactorsVitamin D

Identifiers

PMID8668154
PMCPMC231333
OpenAlexW2142384973

What OpenQuestion holds

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Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.