Evidence map›Paper›PMID 18715874›Full record

ArticleThe Journal of biological chemistry2008

AMP-activated protein kinase contributes to UV- and H2O2-induced apoptosis in human skin keratinocytes.

Cong Cao, Shan Lu, Rebecca Kivlin, Brittany Wallin, Elizabeth Card, Andrew Bagdasarian, Tyrone Tamakloe, Wen-ming Chu, Kun-liang Guan, Yinsheng Wan

RetractedOpen access · hybridAbstract readRetracted Publication
In one paragraph

Article in The Journal of biological chemistry, 2008. 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 It has been retracted, and should not be counted.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 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing 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

52 citing papers in PubMed, 105 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Autophagy in UV Damage Response.Photochemistry and photobiology · 2017
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Oxystressed tumor microenvironment potentiates epithelial to mesenchymal transition and alters cellular bioenergetics towards cancer progression.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 3 institutions in 1 country.

Cong CaoDepartment of Biology, Providence College, Providence, Rhode Island 02918-0001, USA.
Shan Lu
Rebecca Kivlin
Brittany Wallin
Elizabeth Card
Andrew Bagdasarian
Tyrone Tamakloe
Wen-ming Chu
Kun-liang Guan
Yinsheng Wan
Providence College · USBrown University · USUniversity of California, San Diego · US

Funding

UNDERGRADUATE RESEARCH AND SEMINARSP20RR016457 · NCRR · UNIVERSITY OF RHODE ISLAND · PI SHAKARIAN, ALISON M · 2001 to 2011
$35.5M
NCRR NIH HHS P20 RR016457
6 · The paper itself

Abstract

AMP-activated protein kinase or AMPK is an evolutionarily conserved sensor of cellular energy status, activated by a variety of cellular stresses that deplete ATP. However, the possible involvement of AMPK in UV- and H(2)O(2)-induced oxidative stresses that lead to skin aging or skin cancer has not been fully studied. We demonstrated for the first time that UV and H(2)O(2) induce AMPK activation (Thr(172) phosphorylation) in cultured human skin keratinocytes. UV and H(2)O(2) also phosphorylate LKB1, an upstream signal of AMPK, in an epidermal growth factor receptor-dependent manner. Using compound C, a specific inhibitor of AMPK and AMPK-specific small interfering RNA knockdown as well as AMPK activator, we found that AMPK serves as a positive regulator for p38 and p53 (Ser(15)) phosphorylation induced by UV radiation and H(2)O(2) treatment. We also observed that AMPK serves as a negative feedback signal against UV-induced mTOR (mammalian target of rapamycin) activation in a TSC2-dependent manner. Inhibiting mTOR and positively regulating p53 and p38 might contribute to the pro-apoptotic effect of AMPK on UV- or H(2)O(2)-treated cells. Furthermore, activation of AMPK also phosphorylates acetyl-CoA carboxylase or ACC, the pivotal enzyme of fatty acid synthesis, and PFK2, the key protein of glycolysis in UV-radiated cells. Collectively, we conclude that AMPK contributes to UV- and H(2)O(2)-induced apoptosis via multiple mechanisms in human skin keratinocytes and AMPK plays important roles in UV-induced signal transduction ultimately leading to skin photoaging and even skin cancer.

Indexed as

ApoptosisAcetyl-CoA CarboxylaseAdenylate KinaseAMP-Activated Protein KinasesCell LineEpidermal Growth FactorHumansHydrogen PeroxideKeratinocytesModels, Biologicalp38 Mitogen-Activated Protein KinasesSkinSkin NeoplasmsTumor Suppressor Protein p53Ultraviolet RaysAcetyl-CoA CarboxylaseAdenylate KinaseAMP-Activated Protein KinasesEpidermal Growth FactorHydrogen Peroxidep38 Mitogen-Activated Protein KinasesTumor Suppressor Protein p53

Identifiers

PMID18715874
PMCPMC2570892
OpenAlexW2002153971

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.