Evidence map›Paper›PMID 17325653›Full record

ArticleBritish journal of pharmacology2007

The 'specific' tyrosine kinase inhibitor genistein inhibits the enzymic hydrolysis of anandamide: implications for anandamide uptake.

L Thors, K Alajakku, C J Fowler

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in British journal of pharmacology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
3.3field-weighted citation impact, top 9% 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

12 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
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  5. Contributions of nonhematopoietic cells and mediators to immune responses: implications for immunotoxicology.Toxicological sciences : an official journal of the Society of Toxicology · 2015
    Review
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  12. Biochanin-A attenuates neuropathic pain in diabetic rats.Journal of Ayurveda and integrative medicine
    Article
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

3 authors at 1 institution in 1 country.

L ThorsDepartment of Pharmacology and Clinical Neuroscience, Umeå University, Umeå, Sweden. lina.thors@pharm.umu.se
K Alajakku
C J Fowler
Umeå University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

background and purposeThe cellular uptake of anandamide is reduced by inhibitors of fatty acid amide hydrolase (FAAH) and by agents disrupting endocytotic mechanisms. However, it is not clear if these events occur over the same time frame and if they occur to the same extent in different cells. We have therefore investigated the effects of such compounds in three cell lines of different origins using different assay incubation times and temperatures. EXPERIMENTAL APPROACH: FAAH activity and cellular uptake of anandamide was measured using anandamide, radio-labelled either in the ethanolamine or arachidonoyl part of the molecule. KEY

resultsThe FAAH inhibitor URB597 inhibited the uptake of anandamide into C6 glioma, RBL2H3 basophilic leukaemia cells and P19 embryonic carcinoma cells at incubation time 4 min. However, a time-dependent and temperature-sensitive residual uptake remained after URB597 treatment. The combination of progesterone and nystatin reduced the uptake, but also decreased the amount of anandamide retained by the wells. Genistein inhibited anandamide uptake in a manner that was not additive to that of URB597. However, genistein was a potent competitive inhibitor of FAAH (K(i) value 8 microM). CONCLUSIONS AND IMPLICATIONS: The reduction of anandamide uptake by genistein can be explained by its ability to inhibit FAAH with a potency which overlaps that for inhibition of tyrosine kinase. The FAAH- resistant but time-dependent uptake of anandamide is seen in all three cell lines studied and is thus presumably a generally occurring process.

Indexed as

AmidohydrolasesAnimalsArachidonic AcidsBenzamidesBrainCarbamatesCell Line, TumorEndocannabinoidsFatty Acid Amide HydrolasesGenisteinHydrolysisMiceNystatinPolyunsaturated AlkamidesProgesteroneProtein Kinase InhibitorsAmidohydrolasesanandamideArachidonic AcidsBenzamidesCarbamatescyclohexyl carbamic acid 3'-carbamoylbiphenyl-3-yl esterEndocannabinoidsFatty Acid Amide HydrolasesGenisteinNystatinPolyunsaturated AlkamidesProgesteroneProtein Kinase InhibitorsProtein-Tyrosine Kinases

Identifiers

PMID17325653
PMCPMC2013877
OpenAlexW2078893824

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.