Evidence map›Paper›PMID 24395119›Full record

ArticleThe protein journal2014

Purification and characterization of the lectin from taro (Colocasia esculenta) and its effect on mouse splenocyte proliferation in vitro and in vivo.

Patrícia Ribeiro Pereira, Eduardo Mere Del Aguila, Maurício Afonso Verícimo, Russolina Benedeta Zingali, Vânia Margaret Flosi Paschoalin, Joab Trajano Silva

Abstract read
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In one paragraph

Article in The protein journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

11 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. An Extract of Taro (Breast cancer : basic and clinical research · 2021
    Article
  6. Anticancer and Immunomodulatory Benefits of Taro (International journal of molecular sciences · 2020
    Review
  7. Physical-Chemical Crosslinked ElectrospunInternational journal of nanomedicine · 2020
    Article
  8. Article
  9. Tarin, a Potential Immunomodulator and COX-Inhibitor Lectin Found in Taro (Comprehensive reviews in food science and food safety · 2018
    Article
  10. Article
  11. Lectins, Interconnecting Proteins with Biotechnological/Pharmacological and Therapeutic Applications.Evidence-based complementary and alternative medicine : eCAM · 2017
    Review
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 2 institutions in 1 country.

Patrícia Ribeiro PereiraInstituto de Química, Universidade Federal do Rio de Janeiro (UFRJ), Avenida Athos da Silveira Ramos, 149 Bloco A, sala 545, Cidade Universitária, Rio de Janeiro, RJ, CEP 21941-909, Brazil.
Eduardo Mere Del Aguila
Maurício Afonso Verícimo
Russolina Benedeta Zingali
Vânia Margaret Flosi Paschoalin
Joab Trajano Silva
Universidade Federal do Rio de Janeiro · BRUniversidade Federal Fluminense · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lectins are proteins found in a wide range of organisms, with the ability to bind reversibly to specific carbohydrates. They can display important biological activities, such as the activation of the cell cycle in lymphocytes. Storage proteins with lectin activity have been reported in tuberous plant species, such as Colocasia esculenta, popularly known as taro. A simple strategy based on Cibacron Blue chromatography was used to purify a 12 kDa polypeptide 1.3-fold, with a recovery of 30 %. The purified protein was identified as tarin by mass spectrometry, which indicated that it was present in G1a/G1d isoforms. Tarin exhibited both agglutinating activity against hamster erythrocytes and mitogenic activity in vitro and in vivo toward mouse splenocytes. Optimum cellular proliferation in vitro was achieved by 625 ng of the crude extract or 500 ng of the purified tarin. Total mouse splenocyte proliferation measured after 5 days of intraperitoneal inoculation of purified tarin was increased 3.3-fold in comparison to the control group. Half of the proliferating cells were identified as B lymphocytes by flow cytometry. These results show that this is an efficient and simple strategy to purify tarin and aid in establishing this protein as a new therapeutic drug, able to promote cell proliferation in a murine model.

Indexed as

AnimalsCell CycleCell ProliferationColocasiaCricetinaeGlobulinsLectinsLymphocytesMicePlant ProteinsSpleenGlobulinsLectinsPlant ProteinsTAR1 protein, Colocasia esculenta

Identifiers

PMID24395119
OpenAlexW1991595029

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.