Evidence map›Paper›PMID 27486976›Full record

ArticleOncotarget2016

Neuropilin-1 is a receptor for extracellular miRNA and AGO2/miRNA complexes and mediates the internalization of miRNAs that modulate cell function.

Gerald J Prud'homme, Yelena Glinka, Zsuzsanna Lichner, George M Yousef

Open access · diamondAbstract read
In one paragraph

Article in Oncotarget, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

37 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. A Novel Pathway of Functional microRNA Uptake and Mitochondria Delivery.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Modulation of VEGFA Signaling During Heart Regeneration in Zebrafish.Methods in molecular biology (Clifton, N.J.) · 2022
    Review
  13. Review
  14. Review
  15. Toward an Understanding of Extracellular tRNA Biology.Frontiers in molecular biosciences · 2021
    Article
  16. Influence of microRNAs and exosomes in muscle health and diseases.Journal of muscle research and cell motility · 2020
    Article
  17. Review
  18. Article
  19. Review
  20. miR-378a: a new emerging microRNA in metabolism.Cellular and molecular life sciences : CMLS · 2020
    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

4 authors at 2 institutions in 1 country.

Gerald J Prud'hommeKeenan Research Centre for Biomedical Science, St. Michael's Hospital, Toronto, ON M5B 1W8, Canada.
Yelena GlinkaKeenan Research Centre for Biomedical Science, St. Michael's Hospital, Toronto, ON M5B 1W8, Canada.
Zsuzsanna LichnerKeenan Research Centre for Biomedical Science, St. Michael's Hospital, Toronto, ON M5B 1W8, Canada.
George M YousefKeenan Research Centre for Biomedical Science, St. Michael's Hospital, Toronto, ON M5B 1W8, Canada.
St. Michael's Hospital · CAUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Extracellular miRNAs are increasingly studied as markers for specific diseases. They are released in biological fluids in a remarkably stable form, and may play a role in intercellular communication. They are thought to be protected against degradation by either encapsulation within microparticles, or by binding to proteins (mostly AGO2). The particulate forms may be internalized by endocytosis or membrane fusion, but the protein-bound forms require a receptor mechanism for their uptake. A major question is whether there are natural cell-membrane receptors that capture and internalize protein-bound functional miRNAs. We examined neuropilin-1 (NRP1), in view of its properties as a receptor for many ligands, including growth factors such as vascular endothelial growth factor (VEGF), and efficiency at mediating ligand internalization. It is expressed by endothelial cells, many other normal cell types, and cancer cells. Here, we report that NRP1 binds miRNAs with high affinity, and promotes their entry into the cell. Furthermore, the internalized miRNAs remain functional, as they specifically regulate proliferation and migration of cancer cells, as well as tube formation by human endothelial cells. Anti-NRP1 antibodies or NRP1 siRNA knockdown block miRNA effects, further confirming NRP1-mediated uptake. VEGF does not compete with miRNAs for binding to NRP1. In addition, NRP1 binds extracellular AGO2 (carrying miRNA or not), and internalizes AGO2/miRNA complexes. Because miRNA bound to AGO2 appears to the most abundant form in body fluids, this may have important physiological and pathological effects.

Indexed as

EndocytosisArgonaute ProteinsCell Line, TumorCell MovementCell ProliferationCells, CulturedEndothelial CellsHumansMicroRNAsNeovascularization, PhysiologicNeuropilin-1Protein BindingRNA InterferenceSignal TransductionVascular Endothelial Growth Factor AAGO2 protein, humanArgonaute ProteinsMicroRNAsNeuropilin-1Vascular Endothelial Growth Factor Aendocytosisendothelial cellsmiRNAneuropilinrenal cell carcinoma

Identifiers

PMID27486976
PMCPMC5356539
OpenAlexW2479453351

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.