Evidence map›Paper›PMID 26888085›Full record

ArticleThe Journal of biological chemistry2016

Membrane Oxidation Enables the Cytosolic Entry of Polyarginine Cell-penetrating Peptides.

Ting-Yi Wang, Yusha Sun, Nandhini Muthukrishnan, Alfredo Erazo-Oliveras, Kristina Najjar, Jean-Philippe Pellois

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

24 citing papers in PubMed, 36 citations in OpenAlex.

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  10. Peptide-based LDH5 inhibitors enter cancer cells and impair proliferation.Cellular and molecular life sciences : CMLS · 2022
    Article
  11. Review
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  20. Frontiers in plant science · 2018
    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

6 authors at 1 institution in 1 country.

Ting-Yi WangFrom the Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843-2128.
Yusha SunFrom the Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843-2128.
Nandhini MuthukrishnanFrom the Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843-2128.
Alfredo Erazo-OliverasFrom the Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843-2128.
Kristina NajjarFrom the Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843-2128.
Jean-Philippe PelloisFrom the Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843-2128 pellois@tamu.edu.
Texas A&M University · US

Funding

Mechanisms and optimization of endosomal escape for delivery applicationsR01GM110137 · NIGMS · TEXAS A&M AGRILIFE RESEARCH · PI PELLOIS, JEAN-PHILIPPE · 2015 to 2022
$2.3M
NIGMS NIH HHS R01 GM110137NIGMS NIH HHS R01GM110137
6 · The paper itself

Abstract

Arginine-rich peptides can penetrate cells and consequently be used as delivery agents in various cellular applications. The activity of these reagents is often context-dependent, and the parameters that impact cell entry are not fully understood, giving rise to variability and limiting progress toward their usage. Herein, we report that the cytosolic penetration of linear polyarginine peptides is dependent on the oxidation state of the cell. In particular, we find that hypoxia and cellular antioxidants inhibit cell penetration. In contrast, oxidants promote cytosolic cell entry with an efficiency proportional to the level of reactive oxygen species generated within membranes. Moreover, an antibody that binds to oxidized lipids inhibits cell penetration, whereas extracellularly administered pure oxidized lipids enhance peptide transport into cells. Overall, these data indicate that oxidized lipids are capable of mediating the transport of polyarginine peptides across membranes. These data may also explain variability in cell-penetrating peptide performance in different experimental conditions. These new findings therefore provide new opportunities for the rational design of future cell-permeable compounds and for the optimization of delivery protocols.

Indexed as

Biological TransportCell Culture TechniquesCell LineCell MembraneCell-Penetrating PeptidesCytosolFibroblastsHumansMembrane LipidsOxidation-ReductionOxidative StressPeptidesReactive Oxygen SpeciesCell-Penetrating PeptidesMembrane LipidsPeptidespolyarginineReactive Oxygen Speciescell culturecell-penetrating peptide (CPP)oxidation-reduction (redox)peptide transportplasma membrane

Identifiers

PMID26888085
PMCPMC4824998
OpenAlexW2274787255

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.