Evidence map›Paper›PMID 33002062›Full record

ArticlePloS one2020

Biological activities of a recombinant fortilin from Fenneropenaeus merguiensis.

Ureporn Kedjarune-Leggat, Uraipan Saetan, Anchana Khongsaengkaeo, Sudarat Suwannarat, Panchalika Deachamag, Monwadee Wonglapsuwan, Rawiwan Pornprasit, Wanwisa Thongkamwitoon, Parujee Phumklai, Jirapan Chaichanan and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. 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

11 authors at 2 institutions in 1 country.

Ureporn Kedjarune-LeggatDepartment of Oral Biology, Faculty of Dentistry, Prince of Songkla University, Hatyai, Songkhla, Thailand.
Uraipan SaetanDepartment of Molecular Biotechnology and Bioinformatics, Faculty of Science, Prince of Songkla University, Hatyai, Songkhla, Thailand.ORCID 0000-0003-0554-0543
Anchana KhongsaengkaeoDepartment of Molecular Biotechnology and Bioinformatics, Faculty of Science, Prince of Songkla University, Hatyai, Songkhla, Thailand.
Sudarat SuwannaratDepartment of Molecular Biotechnology and Bioinformatics, Faculty of Science, Prince of Songkla University, Hatyai, Songkhla, Thailand.
Panchalika DeachamagDepartment of Molecular Biotechnology and Bioinformatics, Faculty of Science, Prince of Songkla University, Hatyai, Songkhla, Thailand.
Monwadee WonglapsuwanDepartment of Molecular Biotechnology and Bioinformatics, Faculty of Science, Prince of Songkla University, Hatyai, Songkhla, Thailand.
Rawiwan PornprasitMahidol University-Bio Innovation Building, Mahidol University, Nakhon Pathom, Thailand.
Wanwisa ThongkamwitoonMahidol University-Bio Innovation Building, Mahidol University, Nakhon Pathom, Thailand.
Parujee PhumklaiMahidol University-Bio Innovation Building, Mahidol University, Nakhon Pathom, Thailand.
Jirapan ChaichananMahidol University-Bio Innovation Building, Mahidol University, Nakhon Pathom, Thailand.
Wilaiwan ChotigeatDepartment of Molecular Biotechnology and Bioinformatics, Faculty of Science, Prince of Songkla University, Hatyai, Songkhla, Thailand.ORCID 0000-0003-0812-1934
Prince of Songkla University · THMahidol University · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human Fortilin, an antiapoptotic protein, has also been implicated in several diseases; however, several potential uses of fortilin have also been proposed. Bearing the implications of fortilin in mind, fortilin analog, which has no complication with diseases, is required. Since a recombinant full-length fortilin from Fenneropenaeus merguiensis (rFm-Fortilin (FL)) reported only 44% (3e-27) homologous to human fortilin, therefore the biological activities of the Fm-Fortilin (FL) and its fragments (F2, F12, and F23) were investigated for potential use against HEMA toxicity from filling cement to pulp cell. The rFm-Fortilin FL, F2, 12, and F23 were expressed and assayed for proliferation activity. The rFm-Fortilin (FL) showed proliferation activity on human dental pulp cells (HDPCs) and protected the cells from 2-hydroxy-ethyl methacrylate (HEMA) at 1-20 ng/ml. In contrast, none of the rFm-Fortilin fragments promoted HDPC growth that may be due to a lack of three conserved amino acid residues together for binding with the surface of Rab GTPase for proliferative activity. In addition, rFm-Fortilin (FL) activated mineralization and trend to suppressed production of proinflammatory cytokines, including histamine (at 10 ng/ml) and TNF-α (at 100 ng/ml). Besides, the rFm-Fortilin (FL) did not mutate the Chinese hamster ovary (CHO) cell. Therefore, the rFm-Fortilin (FL) has the potential use as a supplementary medical material to promote cell proliferation in patients suffering severe tooth decay and other conditions.

Indexed as

AnimalsArthropod ProteinsCells, CulturedDental PulpHistamineMethacrylatesPenaeidaeRecombinant ProteinsSequence AlignmentTumor Necrosis Factor-alphaArthropod ProteinsHistaminehydroxyethyl methacrylateMethacrylatesRecombinant ProteinsTumor Necrosis Factor-alpha

Identifiers

PMID33002062
PMCPMC7529305
OpenAlexW3091061391

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.