Evidence map›Paper›PMID 11139445›Full record

ArticleBritish journal of pharmacology2000

Ecto-alkaline phosphatase in NG108-15 cells : a key enzyme mediating P1 antagonist-sensitive ATP response.

S Ohkubo, J Kimura, I Matsuoka

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In one paragraph

Article in British journal of pharmacology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

21 citing papers in PubMed, 62 citations in OpenAlex.

  1. Compromised Muscle Properties in a Severe Hypophosphatasia Murine Model.International journal of molecular sciences · 2023
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  7. Purinergic signalling and cancer.Purinergic signalling · 2013
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  11. AMP is an adenosine A1 receptor agonist.The Journal of biological chemistry · 2012
    Article
  12. Article
  13. Article
  14. Ectonucleotidases in the kidney.Purinergic signalling · 2009
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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.

S OhkuboDepartment of Pharmacology, School of Medicine, Fukushima Medical University, Hikarigaoka-1, Fukushima 960-1295, Japan.
J Kimura
I Matsuoka
Fukushima Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We previously demonstrated that extracellular adenine nucleotides induced cyclic AMP elevation through local adenosine production at the membrane surface and subsequent activation of adenosine A(2A) receptors in NG108-15 cells. Furthermore, the adenosine formation was found to be mediated by an ecto-enzyme distinct from the ecto-5'-nucleotidase (CD73). In this study, we investigated the properties of the ecto-AMP phosphohydrolase activity in NG108-15 cells. NG108-15 cells hydrolyzed AMP to adenosine with the K:(M:) value of 18.8+/-2.2 microM and V(max) of 5.3+/-1.6 nmol min(-1) 10(6) cells(-1). This activity was suppressed at pH 6.5, but markedly increased at pH 8.5. The AMP hydrolysis was blocked by levamisole, an alkaline phosphatase (ALP) inhibitor. NG108-15 cells released orthophosphate from 2'- and 3'-AMP as well as from ribose-5-phosphate and ss-glycerophosphate, indicating that NG108-15 cells express ecto-ALP. The cyclic AMP accumulation induced by several adenine nucleotides was inhibited by levamisole, p-nitrophenylphosphate and ss-glycerophosphate, with a parallel decrease in the extracellular adenosine formation. Reverse transcriptase polymerase chain reaction analysis revealed that NG108-15 cells express mRNA for the tissue-nonspecific isozyme of ALP. These results demonstrate that AMP phosphohydrolase activity in NG108-15 cells is due to ecto-ALP, and suggest that this enzyme plays an essential role for the P1 antagonist-sensitive ATP-induced cyclic AMP accumulation in NG108-15 cells.

Indexed as

AdenosineAdenosine MonophosphateAdenosine TriphosphateAlkaline PhosphataseAnimalsCyclic AMPGene Expression Regulation, EnzymologicGlycerophosphatesHydrogen-Ion ConcentrationHydrolysisLevamisoleMiceOrganophosphatesPurinergic P1 Receptor AntagonistsPyridoxal PhosphateRats5'-adenylyl (beta,gamma-methylene)diphosphonateAdenosineAdenosine MonophosphateAdenosine TriphosphateAlkaline Phosphatasealpha,beta-methyleneadenosine 5'-triphosphatebeta-glycerophosphoric acidCyclic AMPGlycerophosphatesLevamisoleOrganophosphatesPurinergic P1 Receptor AntagonistsPyridoxal Phosphatepyridoxal phosphate-6-azophenyl-2',4'-disulfonic acidRNA, Messenger

Identifiers

PMID11139445
PMCPMC1572508
OpenAlexW2066349956

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.