Evidence map›Paper›PMID 9271398›Full record

ArticleMolecular and cellular biology1997

Posttranscriptional regulation of collagen alpha1(I) mRNA in hepatic stellate cells.

B Stefanovic, C Hellerbrand, M Holcik, M Briendl, S Aliebhaber, D A Brenner

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

89 citing papers in PubMed, 202 citations in OpenAlex.

  1. Article
  2. Article
  3. EPRS1 Controls the TGF-Molecular and cellular biology · 2023
    Article
  4. Article
  5. Review
  6. Proteomic Changes of Activated Hepatic Stellate Cells.International journal of molecular sciences · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Origin of myofibroblasts in the fibrotic liver in mice.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  19. Structural determinants of human ζ-globin mRNA stability.Journal of hematology & oncology · 2014
    Article
  20. Article

29 more citing papers are in PubMed but not listed here.

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

6 authors at 2 institutions in 2 countries.

B StefanovicDepartment of Medicine, The University of North Carolina, Chapel Hill 27599-7080, USA.
C Hellerbrand
M Holcik
M Briendl
S Aliebhaber
D A Brenner
University of North Carolina at Chapel Hill · USHoward Hughes Medical Institute · US

Funding

PILOT AND FEASIBILITY STUDIESP30DK034987 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ROBERT S. SANDLER · 1985 to 2026
$30.5M
TNF ALPHA AND IMPAIRED WOUND HEALING OF CACHEXIA XIAR01GM041804 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI BRENNER, DAVID A. · 1989 to 2013
$3.4M
NHLBI NIH HHS P60-HL3832NIDDK NIH HHS P30-DK34987NIGMS NIH HHS R01-GM41804
6 · The paper itself

Abstract

The hepatic stellate cell (HSC) is the primary cell responsible for the dramatic increase in the synthesis of type I collagen in the cirrhotic liver. Quiescent HSCs contain a low level of collagen alpha1(I) mRNA, while activated HSCs contain about 60- to 70-fold more of this mRNA. The transcription rate of the collagen alpha1(I) gene is only two fold higher in activated HSCs than in quiescent HSCs. In assays using actinomycin D or 5,6-dichlorobenzimidazole riboside collagen alpha1(I) mRNA has estimated half-lives of 1.5 h in quiescent HSCs and 24 h in activated HSCs. Thus, this 16-fold change in mRNA stability is primarily responsible for the increase in collagen alpha1(I) mRNA steady-state level in activated HSCs. We have identified a novel RNA-protein interaction targeted to the C-rich sequence in the collagen alpha1(I) mRNA 3' untranslated region (UTR). This sequence is localized 24 nucleotides 3' to the stop codon. In transient transfection experiments, mutation of this sequence diminished accumulation of an mRNA transcribed from a collagen alpha1(I) minigene and in stable transfections decreased the half-life of collagen alpha1(I) minigene mRNA. Binding to the collagen alpha1(I) 3' UTR is present in cytoplasmic extracts of activated but not quiescent HSCs. It contains as a subunit alphaCP, which is also found in the complex involved in stabilization of alpha-globin mRNA. The auxiliary factors necessary to promote binding of alphaCP to the collagen 3' UTR are distinct from the factors necessary for binding to the alpha-globin sequence. Since alphaCP is expressed in both quiescent and activated HSCs, these auxiliary factors are responsible for the differentially expressed RNA-protein interaction at the collagen alpha1(I) mRNA 3' UTR.

Indexed as

Protein Processing, Post-TranslationalAnimalsCollagenGlobinsLiverMaleRatsRats, Sprague-DawleyRNA-Binding ProteinsRNA, MessengerCollagenGlobinsRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID9271398
PMCPMC232371
OpenAlexW2137367647

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.