Evidence map›Paper›PMID 8692835›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1996

Targeting of nitric oxide synthase to endothelial cell caveolae via palmitoylation: implications for nitric oxide signaling.

G García-Cardeña, P Oh, J Liu, J E Schnitzer, W C Sessa

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 209 papers.

0numbers the graph read from it
0cells of the map it votes in
209citing papers in PubMed
15.9field-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

209 citing papers in PubMed, 678 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. The Ever-Expanding Influence of the Endothelial Nitric Oxide Synthase.Basic & clinical pharmacology & toxicology · 2025
    Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Subcellular Localization Guides eNOS Function.International journal of molecular sciences · 2024
    Review
  10. Article
  11. Review
  12. Review
  13. Review
  14. Review
  15. Review
  16. Review
  17. Article
  18. Review
  19. Review
  20. Article

149 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

5 authors at 1 institution in 1 country.

G García-CardeñaMolecular Cardiobiology Program and Department of Pharmacology, Yale University School of Medicine, New Haven, CT 06536, USA.
P Oh
J Liu
J E Schnitzer
W C Sessa
Yale University · US

Funding

N-MYRISTOYLATION OF ENDOTHELIAL NITRIC OXIDE SYNTHASEF32HL009224 · NHLBI · YALE UNIVERSITY · PI LIU, JIANWEI · 1994 to 1997
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ALBUMIN-ENDOTHELIUM INTER. IN NORMAL &DIABETIC COND.R29HL043278 · NHLBI · YALE UNIVERSITY · PI SCHNITZER, JAN E · 1989 to 1993
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ENDOTHELIAL NITRIC OXIDE SYNTHASE--MEMBRANE ASSOCIATIONR29HL051948 · NHLBI · YALE UNIVERSITY · PI SESSA, WILLIAM C. · 1995 to 1998
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NHLBI NIH HHS F32-HL09224NHLBI NIH HHS HL43278NHLBI NIH HHS HL 51948
6 · The paper itself

Abstract

The membrane association of endothelial nitric oxide synthase (eNOS) plays an important role in the biosynthesis of nitric oxide (NO) in vascular endothelium. Previously, we have shown that in cultured endothelial cells and in intact blood vessels, eNOS is found primarily in the perinuclear region of the cells and in discrete regions of the plasma membrane, suggesting trafficking of the protein from the Golgi to specialized plasma membrane structures. Here, we show that eNOS is found in Triton X-100-insoluble membranes prepared from cultured bovine aortic endothelial cells and colocalizes with caveolin, a coat protein of caveolae, in cultured bovine lung microvascular endothelial cells as determined by confocal microscopy. To examine if eNOS is indeed in caveolae, we purified luminal endothelial cell plasma membranes and their caveolae directly from intact, perfused rat lungs. eNOS is found in the luminal plasma membranes and is markedly enriched in the purified caveolae. Because palmitoylation of eNOS does not significantly influence its membrane association, we next examined whether this modification can affect eNOS targeting to caveolae. Wild-type eNOS, but not the palmitoylation mutant form of the enzyme, colocalizes with caveolin on the cell surface in transfected NIH 3T3 cells, demonstrating that palmitoylation of eNOS is necessary for its targeting into caveolae. These data suggest that the subcellular targeting of eNOS to caveolae can restrict NO signaling to specific targets within a limited microenvironment at the cell surface and may influence signal transduction through caveolae.

Indexed as

Signal Transduction3T3 CellsAnimalsCattleCell CompartmentationCell LineCell MembraneDNA, ComplementaryEndothelium, VascularMiceNitric Oxide SynthasePalmitic AcidPalmitic AcidsRatsDNA, ComplementaryNitric Oxide SynthasePalmitic AcidPalmitic Acids

Identifiers

PMID8692835
PMCPMC39043
OpenAlexW2022568707

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.