Evidence map›Paper›PMID 9497388›Full record

ArticleThe Journal of biological chemistry1998

Characterization of a cytosolic heat-shock protein-caveolin chaperone complex. Involvement in cholesterol trafficking.

A Uittenbogaard, Y Ying, E J Smart

RetractedOpen access · hybridAbstract readRetracted Publication
PubMed Publisher
In one paragraph

Article in The Journal of biological chemistry, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
11.0field-weighted citation impact, top 1% 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

83 citing papers in PubMed, 302 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Review
  6. From embryonic development to human diseases: The functional role of caveolae/caveolin.Birth defects research. Part C, Embryo today : reviews · 2016
    Review
  7. Article
  8. Article
  9. Article
  10. Caveolin-1 in oral squamous cell carcinoma microenvironment: an overview.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014
    Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Regulation of cholesterol homeostasis.Cellular and molecular life sciences : CMLS · 2012
    Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

A UittenbogaardUniversity of Kentucky Medical School, Department of Physiology, MS 508, Lexington, Kentucky 40536, USA.
Y Ying
E J Smart
The University of Texas Southwestern Medical Center · USUniversity of Kentucky · US

Funding

CAVEOLAE MEDIATED REGULATION OF ATHEROGENESISR29HL058475 · NHLBI · UNIVERSITY OF KENTUCKY · PI SMART, ERIC J · 1997 to 1998
–
NHLBI NIH HHS R29HL58475-01
6 · The paper itself

Abstract

Caveolin is a 22-kDa protein that appears to play a critical role in regulating the cholesterol concentration of caveolae. Even though caveolin is thought to be a membrane protein, several reports suggest that this peculiar protein can traffic independently of membrane vesicles. We now present evidence that a cytosolic pool of caveolin is part of a heat-shock protein-immunophilin chaperone complex consisting of caveolin, heat-shock protein 56, cyclophilin 40, cyclophilin A, and cholesterol. Treatment of NIH 3T3 cells with 1 microM cyclosporin A or 100 nM rapamycin disrupted the putative transport complex and prevented rapid (10-20 min) transport of cholesterol to caveolae. The lymphoid cell line, L1210-JF, does not express caveolin, does not form an immunophilin-caveolin complex, and does not transport newly synthesized cholesterol to caveolae. Transfection of caveolin cDNA into L1210-JF cells allowed the assembly of a transport complex identical to that found in NIH 3T3 cells. In addition, newly synthesized cholesterol in transfected cells was rapidly (10-20 min) and specifically transported to caveolae. These data strongly suggest that a caveolin-chaperone complex is a mechanism by which newly synthesized cholesterol is transported from the endoplasmic reticulum through the cytoplasm to caveolae.

Indexed as

CaveolinsCyclophilinsAnimalsBiological TransportCarrier ProteinsCaveolin 1Cell CompartmentationCells, CulturedCholesterolCyclosporineCytosolDNA-Binding ProteinsHeat-Shock ProteinsMembrane ProteinsMiceMolecular ChaperonesCarrier ProteinsCav1 protein, mouseCaveolin 1CaveolinsCholesterolCyclophilinsCyclosporineDNA-Binding ProteinsHeat-Shock ProteinsMembrane ProteinsMolecular ChaperonesPeptidylprolyl IsomerasePeptidyl-Prolyl Isomerase FPolyenesPPIF protein, mouseSirolimusTacrolimus Binding Proteins

Identifiers

PMID9497388
OpenAlexW2088432812

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.