Evidence map›Paper›PMID 7568126›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1995

12(S)-hydroxyeicosatetraenoic acid and 13(S)-hydroxyoctadecadienoic acid regulation of protein kinase C-alpha in melanoma cells: role of receptor-mediated hydrolysis of inositol phospholipids.

B Liu, W A Khan, Y A Hannun, J Timar, J D Taylor, S Lundy, I Butovich, K V Honn

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

30 citing papers in PubMed, 114 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Who is the real 12-HETrE?Prostaglandins & other lipid mediators · 2017
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Minireview: 12-Lipoxygenase and Islet β-Cell Dysfunction in Diabetes.Molecular endocrinology (Baltimore, Md.) · 2015
    Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Revisiting CB1 receptor as drug target in human melanoma.Pathology oncology research : POR · 2012
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

B LiuDepartment of Radiation Oncology, Wayne State University, Detroit, MI 48202, USA.
W A Khan
Y A Hannun
J Timar
J D Taylor
S Lundy
I Butovich
K V Honn
Duke University · US

Funding

THROMBOXANES: ROLE IN TUMOR GROWTH AND METASTASISR01CA029997 · NCI · WAYNE STATE UNIVERSITY · PI HONN, KENNETH V · 1985 to 2008
$1.7M
NCI NIH HHS CA29997NHLBI NIH HHS HL43702
6 · The paper itself

Abstract

Protein kinase C (PKC) isoenzymes are essential components of cell signaling. In this study, we investigated the regulation of PKC-alpha in murine B16 amelanotic melanoma (B16a) cells by the monohydroxy fatty acids 12(S)-hydroxyeicosatetraenoic acid [12(S)-HETE] and 13(S)-hydroxyoctadecadienoic acid [13(S)-HODE]. 12(S)-HETE induced a translocation of PKC-alpha to the plasma membrane and focal adhesion plaques, leading to enhanced adhesion of B16a cells to the matrix protein fibronectin. However, 13(S)-HODE inhibited these 12(S)-HETE effects on PKC-alpha. A receptor-mediated mechanism of action for 12(S)-HETE and 13(S)-HODE is supported by the following findings. First, 12(S)-HETE triggered a rapid increase in cellular levels of diacylglycerol and inositol trisphosphate in B16a cells. 13(S)-HODE blocked the 12(S)-HETE-induced bursts of both second messengers. Second, the 12(S)-HETE-increased adhesion of B16a cells to fibronectin was sensitive to inhibition by a phospholipase C inhibitor and pertussis toxin. Finally, a high-affinity binding site (Kd = 1 nM) for 12(S)-HETE was detected in B16a cells, and binding of 12(S)-HETE to B16a cells was effectively inhibited by 13(S)-HODE (IC50 = 4 nM). In summary, our data provide evidence that regulation of PKC-alpha by 12(S)-HETE and 13(S)-HODE may be through a guanine nucleotide-binding protein-linked receptor-mediated hydrolysis of inositol phospholipids.

Indexed as

Signal Transduction12-Hydroxy-5,8,10,14-eicosatetraenoic AcidAnimalsBinding SitesBrainCell AdhesionCell LineCell MembraneCytosolDiglyceridesFibronectinsHydrolysisHydroxyeicosatetraenoic AcidsInositol 1,4,5-TrisphosphateIsoenzymesKinetics12-Hydroxy-5,8,10,14-eicosatetraenoic Acid13-hydroxy-9,11-octadecadienoic acidDiglyceridesFibronectinsHydroxyeicosatetraenoic AcidsInositol 1,4,5-TrisphosphateIsoenzymesLinoleic AcidsPertussis ToxinPhosphatidylinositolsProtein Kinase CReceptors, Cell SurfaceRecombinant ProteinsTetradecanoylphorbol AcetateVirulence Factors, Bordetella

Identifiers

PMID7568126
PMCPMC40977
OpenAlexW2000912603

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.