Evidence map›Paper›PMID 17786543›Full record

ArticleMolecular and cellular biochemistry2007

Biochemical characterization of ecto-nucleotide pyrophosphatase/phosphodiesterase (E-NPP, E.C. 3.1.4.1) from rat heart left ventricle.

Bárbara Rücker, Manoela E Almeida, Towia A Libermann, Luiz F Zerbini, Márcia R Wink, João José Freitas Sarkis

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Article in Molecular and cellular biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.2field-weighted citation impact, top 25% 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

7 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Jarid2 is among a set of genes differentially regulated by Nkx2.5 during outflow tract morphogenesis.Developmental dynamics : an official publication of the American Association of Anatomists · 2010
    Article
  6. Cystic fibrosis remodels the regulation of purinergic signaling by NTPDase1 (CD39) and NTPDase3.American journal of physiology. Lung cellular and molecular physiology · 2010
    Article
  7. Kinetic analysis of substrate utilization by native and TNAP-, NPP1-, or PHOSPHO1-deficient matrix vesicles.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2010
    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

6 authors at 4 institutions in 2 countries.

Bárbara RückerDepartamento de Bioquímica, Instituto de Ciências Básicas da Saúde, Universidade Federal do Rio Grande do Sul - UFRGS, Rua Ramiro Barcelos, 2600 - Prédio ANEXO, Porto Alegre, RS CEP 90035-003, Brazil.
Manoela E Almeida
Towia A Libermann
Luiz F Zerbini
Márcia R Wink
João José Freitas Sarkis
Universidade Federal do Rio Grande do Sul · BRDana-Farber/Harvard Cancer Center · USFundação Faculdade de Medicina · BRHarvard University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the present study we investigate the biochemical properties of the members of NPP family in synaptosomes prepared from rat heart left ventricles. Using p-nitrophenyl-5'-thymidine monophosphate (p-Nph-5'-TMP) as substrate for E-NPPs in rat cardiac synaptosomes, we observed an alkaline pH dependence, divalent cation dependence and the K ( M ) value corresponded to 91.42 +/- 13.97 microM and the maximal velocity (V ( max )) value calculated was 63.79 +/- 3.59 nmol p-nitrophenol released/min/mg of protein (mean +/- SD, n = 4). Levamisole (1 mM), was ineffective as inhibitor of p-Nph-5'-TMP hydrolysis in pH 8.9 (optimum pH for the enzyme characterized). Suramin (0.25 mM) strongly reduced the hydrolysis of p-Nph-5'-TMP by about 46%. Sodium azide (10 and 20 mM) and gadolinium chloride (0.3 and 0.5 mM), E-NTPases inhibitors, had no effects on p-Nph-5'-TMP hydrolysis. RT-PCR analysis of left ventricle demonstrated the expression of NPP2 and NPP3 enzymes, but excluded the presence of NPP1 member. By quantitative real-time PCR we identified the NPP3 as the enzyme with the highest expression in rat left ventricle. The demonstration of the presence of the E-NPP family in cardiac system, suggest that these enzymes could contribute with the fine-tuning control of the nucleotide levels at the nerve terminal endings of left ventricles that are involved in several cardiac pathologies.

Indexed as

AnimalsAntineoplastic AgentsEnzyme InhibitorsHeart VentriclesHydrolysisMaleNitrophenolsPhosphoric Diester HydrolasesPyrophosphatasesRatsRats, WistarReverse Transcriptase Polymerase Chain ReactionRNA, MessengerSodium AzideSuraminSynaptosomes4-nitrophenolAntineoplastic Agentsectonucleotide pyrophosphatase phosphodiesterase 1Enpp3 protein, ratEnzyme InhibitorsNitrophenolsPhosphoric Diester HydrolasesPyrophosphatasesRNA, MessengerSodium AzideSuraminThymidine Monophosphate

Identifiers

PMID17786543
OpenAlexW1981668915

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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.