Evidence map›Paper›PMID 28415564›Full record

ReviewOncotarget2017

Mammalian sphingosine kinase (SphK) isoenzymes and isoform expression: challenges for SphK as an oncotarget.

Diana Hatoum, Nahal Haddadi, Yiguang Lin, Najah T Nassif, Eileen M McGowan

Open access · diamondAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Oncotarget, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

65 citing papers in PubMed, 95 citations in OpenAlex.

  1. Review
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  14. Fatty acid elongation by ELOVL6 hampers remyelination by promoting inflammatory foam cell formation during demyelination.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  15. Review
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  17. Review
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  19. Sphingolipids in mitochondria-from function to disease.Frontiers in cell and developmental biology · 2023
    Review
  20. Article

5 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Diana HatoumSchool of Life Sciences, University of Technology Sydney, Ultimo, Sydney, NSW 2007, Australia.
Nahal HaddadiSchool of Life Sciences, University of Technology Sydney, Ultimo, Sydney, NSW 2007, Australia.
Yiguang LinSchool of Life Sciences, University of Technology Sydney, Ultimo, Sydney, NSW 2007, Australia.
Najah T NassifSchool of Life Sciences, University of Technology Sydney, Ultimo, Sydney, NSW 2007, Australia.
Eileen M McGowanSchool of Life Sciences, University of Technology Sydney, Ultimo, Sydney, NSW 2007, Australia.
University of Technology Sydney · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The various sphingosine kinase (SphK) isoenzymes (isozymes) and isoforms, key players in normal cellular physiology, are strongly implicated in cancer and other diseases. Mutations in SphKs, that may justify abnormal physiological function, have not been recorded. Nonetheless, there is a large and growing body of evidence demonstrating the contribution of gain or loss of function and the imbalance in the SphK/S1P rheostat to a plethora of pathological conditions including cancer, diabetes and inflammatory diseases. SphK is expressed as two isozymes SphK1 and SphK2, transcribed from genes located on different chromosomes and both isozymes catalyze the phosphorylation of sphingosine to S1P. Expression of each SphK isozyme produces alternately spliced isoforms. In recent years the importance of the contribution of SpK1 expression to treatment resistance in cancer has been highlighted and, additionally, differences in treatment outcome appear to also be dependent upon SphK isoform expression. This review focuses on an exciting emerging area of research involving SphKs functions, expression and subcellular localization, highlighting the complexity of targeting SphK in cancer and also comorbid diseases. This review also covers the SphK isoenzymes and isoforms from a historical perspective, from their first discovery in murine species and then in humans, their role(s) in normal cellular function and in disease processes, to advancement of SphK as an oncotarget.

Indexed as

Gene Expression RegulationAnimalsBiomarkers, TumorCell Transformation, NeoplasticDisease SusceptibilityDrug DiscoveryDrug Resistance, NeoplasmHumansIsoenzymesMiceMolecular Targeted TherapyMultigene FamilyNeoplasmsPhosphotransferases (Alcohol Group Acceptor)Proprotein ConvertasesProtein BindingBiomarkers, TumorIsoenzymesmembrane-bound transcription factor peptidase, site 1Phosphotransferases (Alcohol Group Acceptor)Proprotein ConvertasesReceptors, LysosphingolipidSerine EndopeptidasesSphingosine Kinasecancerisoenzymesisoformssphingosine-1-phosphatesphingosine kinase

Identifiers

PMID28415564
PMCPMC5482707
OpenAlexW2596802012

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.