Evidence map›Paper›PMID 28089756›Full record

ArticleCell chemical biology2017

Glycan Alteration Imparts Cellular Resistance to a Membrane-Lytic Anticancer Peptide.

Ken Ishikawa, Scott H Medina, Joel P Schneider, Amar J S Klar

Abstract read
In one paragraph

Article in Cell chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Article
  2. Immunobiological mechanisms of action of oncolytic peptides.Journal for immunotherapy of cancer · 2026
    Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. CpACpP:ACS omega · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Ken IshikawaGene Regulation and Chromosome Biology Laboratory, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA; Chemical Biology Laboratory, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA.
Scott H MedinaChemical Biology Laboratory, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA.
Joel P SchneiderChemical Biology Laboratory, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA. Electronic address: joel.schneider@nih.gov.
Amar J S KlarGene Regulation and Chromosome Biology Laboratory, National Cancer Institute, National Institutes of Health, Frederick, MD 21702, USA. Electronic address: klara@mail.nih.gov.

Funding

Design and Utility of Novel Protienaceous BiomaterialsZIABC011313 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SCHNEIDER, JOEL · 2010 to 2025
$19.0M
Development of antibacterial agents and materialsZIABC011314 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SCHNEIDER, JOEL · 2010 to 2025
$8.9M
Intramural NIH HHS ZIA BC011313
6 · The paper itself

Abstract

Although resistance toward small-molecule chemotherapeutics has been well studied, the potential of tumor cells to avoid destruction by membrane-lytic compounds remains unexplored. Anticancer peptides (ACPs) are a class of such agents that disrupt tumor cell membranes through rapid and non-stereospecific mechanisms, encouraging the perception that cellular resistance toward ACPs is unlikely to occur. We demonstrate that eukaryotic cells can, indeed, develop resistance to the model oncolytic peptide SVS-1, which preferentially disrupts the membranes of cancer cells. Utilizing fission yeast as a model organism, we show that ACP resistance is largely controlled through the loss of cell-surface anionic saccharides. A similar mechanism was discovered in mammalian cancer cells where removal of negatively charged sialic acid residues directly transformed SVS-1-sensitive cell lines into resistant phenotypes. These results demonstrate that changes in cell-surface glycosylation play a major role in tumor cell resistance toward oncolytic peptides.

Indexed as

Antineoplastic AgentsCell Line, TumorCell MembraneDrug Resistance, FungalDrug Resistance, NeoplasmGlycosylationHumansPeptidesPolysaccharidesSaccharomyces cerevisiaeAntineoplastic AgentsPeptidesPolysaccharidesSVS-1 peptideanticancer peptidescancer cell resistancegeneticsglycosylationmembrane-lytic peptides

Identifiers

PMID28089756
PMCPMC5316350

What OpenQuestion holds

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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.