Evidence map›Paper›PMID 22898256›Full record

ArticlePeptides2012

Protein transduction in human cells is enhanced by cell-penetrating peptides fused with an endosomolytic HA2 sequence.

Ji-Sing Liou, Betty Revon Liu, Adam L Martin, Yue-Wern Huang, Huey-Jenn Chiang, Han-Jung Lee

Open access · greenAbstract read
In one paragraph

Article in Peptides, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.4field-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

29 citing papers in PubMed, 74 citations in OpenAlex.

  1. Review
  2. Article
  3. Nucleic acid drug vectors for diagnosis and treatment of brain diseases.Signal transduction and targeted therapy · 2023
    Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Production and clinical development of nanoparticles for gene delivery.Molecular therapy. Methods & clinical development · 2016
    Review
  18. Fusogenic-oligoarginine peptide-mediated silencing of the CIP2A oncogene suppresses oral cancer tumor growth in vivo.Journal of controlled release : official journal of the Controlled Release Society · 2015
    Article
  19. Review
  20. 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 2 countries.

Ji-Sing LiouDepartment of Natural Resources and Environmental Studies, National Dong Hwa University, No. 1, Sec. 2, Da-Hsueh Road, Shoufeng, Hualien 97401, Taiwan.
Betty Revon Liu
Adam L Martin
Yue-Wern Huang
Huey-Jenn Chiang
Han-Jung Lee
National Dong Hwa University · TWMissouri University of Science and Technology · US

Funding

Quantum Dots and Protein Transduction Domains as a Biomolecule Delivery VehicleR15EB009530 · NIBIB · MISSOURI UNIVERSITY OF SCIENCE & TECHNOLOGY · PI HUANG, YUE-WERN · 2009 to 2009
$226k
NIBIB NIH HHS R15 EB009530NIBIB NIH HHS R15EB009530
6 · The paper itself

Abstract

Endocytosis has been proposed as one of the primary mechanisms for cellular entry of cell-penetrating peptides (CPPs) and their cargoes. However, a major limitation of endocytic pathway is entrapment of the CPP-cargo in intracellular vesicles from which the cargo must escape into the cytoplasm to exert its biological activity. Here we demonstrate that a CPP tagged with an endosomolytic fusion peptide derived from the influenza virus hemagglutinin-2 (HA2) remarkably enhances the cytosolic delivery of proteins in human A549 cells. To determine the endosome-disruptive effects, recombinant DNA plasmids containing coding sequences of HA2, CPPs and red fluorescent proteins (RFPs) were constructed. The fusion proteins were purified from plasmid-transformed Escherichia coli, and their effects on protein transduction were examined using live cell imaging and flow cytometry. Our data indicate that endocytosis is the major route for cellular internalization of CPP-HA2-tagged RFP. Mechanistic studies revealed that the fusogenic HA2 peptide dramatically facilitates CPP-mediated protein entry through the release of endocytosed RFPs from endosomes into the cytoplasm. Furthermore, incorporating the HA2 fusion peptide of the CPP-HA2 fusion protein improved cytosolic uptake without causing cytotoxicity. These findings strongly suggest that the CPP-HA2 tag could be an efficient and safe carrier that overcomes endosomal entrapment of delivered therapeutic drugs.

Indexed as

Cell Line, TumorCell-Penetrating PeptidesCytoplasmEndocytosisEndosomesHemagglutinins, ViralHumansLuminescent ProteinsPlasmidsRecombinant Fusion ProteinsRed Fluorescent ProteinCell-Penetrating Peptideshemagglutinin HA-2 fusogenic peptide, Influenza virusHemagglutinins, ViralLuminescent ProteinsRecombinant Fusion ProteinsRed Fluorescent Protein

Identifiers

PMID22898256
PMCPMC9616647
OpenAlexW2154559615

What OpenQuestion holds

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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.