Evidence map›Paper›PMID 28934328›Full record

ArticlePloS one2017

The human VGF-derived bioactive peptide TLQP-21 binds heat shock 71 kDa protein 8 (HSPA8)on the surface of SH-SY5Y cells.

Shamim Akhter, Sandipan Chakraborty, Daniela Moutinho, Elia Álvarez-Coiradas, Isaac Rosa, Juan Viñuela, Eduardo Domínguez, Angel García, Jesús R Requena

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.0field-weighted citation impact, top 29% 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

9 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The molecular identity of the TLQP-21 peptide receptor.Cellular and molecular life sciences : CMLS · 2021
    Review
  5. ACTH(6-9)PGP Peptide Protects SH-SY5Y Cells from HMolecules (Basel, Switzerland) · 2021
    Article
  6. Review
  7. Article
  8. Review
  9. 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

9 authors at 3 institutions in 3 countries.

Shamim AkhterCIMUS Biomedical Research Institute, University of Santiago de Compostela-IDIS, Santiago de Compostela, Spain.
Sandipan ChakrabortyDepartment of Microbiology, University of Calcutta, Kolkata, India.
Daniela MoutinhoCIMUS Biomedical Research Institute, University of Santiago de Compostela-IDIS, Santiago de Compostela, Spain.
Elia Álvarez-CoiradasBioFarma Research Group, CIMUS, University of Santiago de Compostela-IDIS, Santiago de Compostela, Spain.
Isaac RosaCIMUS Biomedical Research Institute, University of Santiago de Compostela-IDIS, Santiago de Compostela, Spain.
Juan ViñuelaImmunology Laboratory, Santiago University Hospital, Santiago de Compostela, Spain.
Eduardo DomínguezBioFarma Research Group, CIMUS, University of Santiago de Compostela-IDIS, Santiago de Compostela, Spain.
Angel GarcíaCIMUS Biomedical Research Institute, University of Santiago de Compostela-IDIS, Santiago de Compostela, Spain.
Jesús R RequenaCIMUS Biomedical Research Institute, University of Santiago de Compostela-IDIS, Santiago de Compostela, Spain.ORCID http://orcid.org/0000-0003-1954-4975
Universidade de Santiago de Compostela · ESKhulna University · BDUniversity of Calcutta · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

VGF (non-acronymic)is a secreted chromogranin/secretogranin that gives rise to a number of bioactive peptides by a complex proteolysis mechanism. VGF-derived peptides exert an extensive array of biological effects in energy metabolism, mood regulation, pain, gastric secretion function, reproduction and, perhaps, cancer. It is therefore surprising that very little is known about receptors and binding partners of VGF-derived peptides and their downstream molecular mechanisms of action. Here, using affinity chromatography and mass spectrometry-based protein identification, we have identified the heat shock cognate 71 kDa protein A8 (HSPA8)as a binding partner of human TLQP-21 on the surface of human neuroblastomaSH-SY5Y cells. Binding of TLQP-21 to membrane associated HSPA8 in live SH-SY5Y cells was further supported by cross-linking to live cells. Interaction between HSPA8 and TLQP-21 was confirmed in vitro by label-free Dynamic Mass Redistribution (DMR) studies. Furthermore, molecular modeling studies show that TLQP-21 can be docked into the HSPA8 peptide binding pocket. Identification of HSPA8 as a cell surface binding partner of TLQP-21 opens new avenues to explore the molecular mechanisms of its physiological actions, and of pharmacological modulation thereof.

Indexed as

BiotinylationCell Line, TumorCell MembraneHSC70 Heat-Shock ProteinsHumansMolecular Docking SimulationNeuropeptidesPeptide FragmentsProtein BindingProtein ConformationSurface PropertiesHSC70 Heat-Shock ProteinsHSPA8 protein, humanNeuropeptidesPeptide FragmentsTLQP-21 peptideVGF peptide

Identifiers

PMID28934328
PMCPMC5608341
OpenAlexW2760094082

What OpenQuestion holds

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LicenceCC BY
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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.