Evidence map›Paper›PMID 29748898›Full record

ReviewCancer immunology, immunotherapy : CII2018

Cystatin F as a regulator of immune cell cytotoxicity.

Janko Kos, Milica Perišić Nanut, Mateja Prunk, Jerica Sabotič, Esmeralda Dautović, Anahid Jewett

Open access · greenAbstract readReview
In one paragraph

Review in Cancer immunology, immunotherapy : CII, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed, 1 pooled it
1.2field-weighted citation impact, top 25% 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

27 citing papers in PubMed, 1 synthesis or guideline pooled it, 49 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Cystatin F Depletion inInternational journal of molecular sciences · 2024
    Article
  9. Article
  10. Article
  11. Activation of CD8American journal of respiratory and critical care medicine · 2023
    Article
  12. Review
  13. T-cell phenotype including CD57Blood cancer journal · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. 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 3 institutions in 3 countries.

Janko KosDepartment of Biotechnology, Jožef Stefan Institute, Ljubljana, Slovenia. janko.kos@ffa.uni-lj.sim.
Milica Perišić NanutDepartment of Biotechnology, Jožef Stefan Institute, Ljubljana, Slovenia.
Mateja PrunkDepartment of Biotechnology, Jožef Stefan Institute, Ljubljana, Slovenia.
Jerica SabotičDepartment of Biotechnology, Jožef Stefan Institute, Ljubljana, Slovenia.
Esmeralda DautovićFaculty of Pharmacy, University of Tuzla, Tuzla, Bosnia and Herzegovina.
Anahid JewettThe Jane and Jerry Weintraub Center for Reconstructive Biotechnology, School of Dentistry, University of California-Los Angeles, Los Angeles, USA.
Jožef Stefan Institute · SIUniversity of California, Los Angeles · USUniversity of Tuzla · BA

Funding

Javna Agencija za Raziskovalno Dejavnost RS J4 6811Javna Agencija za Raziskovalno Dejavnost RS P4 0127
6 · The paper itself

Abstract

Cysteine cathepsins are lysosomal peptidases involved in the regulation of innate and adaptive immune responses. Among the diverse processes, regulation of granule-dependent cytotoxicity of cytotoxic T-lymphocytes (CTLs) and natural killer (NK) cells during cancer progression has recently gained significant attention. The function of cysteine cathepsins is regulated by endogenous cysteine protease inhibitors-cystatins. Whereas other cystatins are generally cytosolic or extracellular proteins, cystatin F is present in endosomes and lysosomes and is thus able to regulate the activity of its target directly. It is delivered to endosomal/lysosomal vesicles as an inactive, disulphide-linked dimer. Proteolytic cleavage of its N-terminal part leads to the monomer, the only form that is a potent inhibitor of cathepsins C, H and L, involved in the activation of granzymes and perforin. In NK cells and CTLs the levels of active cathepsin C and of granzyme B are dependent on the concentration of monomeric, active cystatin F. In tumour microenvironment, inactive dimeric cystatin F can be secreted from tumour cells or immune cells and further taken up by the cytotoxic cells. Subsequent monomerization and inhibition of cysteine cathepsins within the endosomal/lysosomal vesicles impairs granzyme and perforin activation, and provokes cell anergy. Further, the glycosylation pattern has been shown to be important in controlling secretion of cystatin F from target cells, as well as internalization by cytotoxic cells and trafficking to endosomal/lysosomal vesicles. Cystatin F is therefore an important mediator used by bystander cells to reduce NK and T-cell cytotoxicity.

Indexed as

Cytotoxicity, ImmunologicImmunomodulationAnimalsCystatinsHumansImmunityKiller Cells, NaturalLymphocyte ActivationCystatinsCathepsinsCell cytotoxicityCITIM 2017Cystatin FNatural killer cellsT cells

Identifiers

PMID29748898
PMCPMC11028163
OpenAlexW2801569271

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.