Mammalian sphingosine kinase (SphK) isoenzymes and isoform expression: challenges for SphK as an oncotarget.
- Publisher:
- IMPACT JOURNALS LLC
- Publication Type:
- Journal Article
- Citation:
- Oncotarget, 2017, 8, (22), pp. 36898-36929
- Issue Date:
- 2017-05-30
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Full metadata record
| Field | Value | Language |
|---|---|---|
| dc.contributor.author | Hatoum, D | |
| dc.contributor.author | Haddadi, N | |
| dc.contributor.author | Lin, Y | |
| dc.contributor.author | Nassif, NT | |
| dc.contributor.author | McGowan, EM | |
| dc.date.accessioned | 2020-05-21T05:51:55Z | |
| dc.date.available | 2017-03-02 | |
| dc.date.available | 2020-05-21T05:51:55Z | |
| dc.date.issued | 2017-05-30 | |
| dc.identifier.citation | Oncotarget, 2017, 8, (22), pp. 36898-36929 | |
| dc.identifier.issn | 1949-2553 | |
| dc.identifier.issn | 1949-2553 | |
| dc.identifier.uri | http://hdl.handle.net/10453/140870 | |
| dc.description.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. | |
| dc.format | ||
| dc.language | eng | |
| dc.publisher | IMPACT JOURNALS LLC | |
| dc.relation.ispartof | Oncotarget | |
| dc.relation.isbasedon | 10.18632/oncotarget.16370 | |
| dc.rights | info:eu-repo/semantics/openAccess | |
| dc.subject | 1112 Oncology and Carcinogenesis | |
| dc.subject.mesh | Animals | |
| dc.subject.mesh | Humans | |
| dc.subject.mesh | Mice | |
| dc.subject.mesh | Neoplasms | |
| dc.subject.mesh | Cell Transformation, Neoplastic | |
| dc.subject.mesh | Disease Susceptibility | |
| dc.subject.mesh | Serine Endopeptidases | |
| dc.subject.mesh | Proprotein Convertases | |
| dc.subject.mesh | Isoenzymes | |
| dc.subject.mesh | Phosphotransferases (Alcohol Group Acceptor) | |
| dc.subject.mesh | Receptors, Lysosphingolipid | |
| dc.subject.mesh | Gene Expression Regulation | |
| dc.subject.mesh | Protein Binding | |
| dc.subject.mesh | Drug Resistance, Neoplasm | |
| dc.subject.mesh | Multigene Family | |
| dc.subject.mesh | Drug Discovery | |
| dc.subject.mesh | Molecular Targeted Therapy | |
| dc.subject.mesh | Biomarkers, Tumor | |
| dc.subject.mesh | Animals | |
| dc.subject.mesh | Biomarkers, Tumor | |
| dc.subject.mesh | Cell Transformation, Neoplastic | |
| dc.subject.mesh | Disease Susceptibility | |
| dc.subject.mesh | Drug Discovery | |
| dc.subject.mesh | Drug Resistance, Neoplasm | |
| dc.subject.mesh | Gene Expression Regulation | |
| dc.subject.mesh | Humans | |
| dc.subject.mesh | Isoenzymes | |
| dc.subject.mesh | Mice | |
| dc.subject.mesh | Molecular Targeted Therapy | |
| dc.subject.mesh | Multigene Family | |
| dc.subject.mesh | Neoplasms | |
| dc.subject.mesh | Phosphotransferases (Alcohol Group Acceptor) | |
| dc.subject.mesh | Proprotein Convertases | |
| dc.subject.mesh | Protein Binding | |
| dc.subject.mesh | Receptors, Lysosphingolipid | |
| dc.subject.mesh | Serine Endopeptidases | |
| dc.title | Mammalian sphingosine kinase (SphK) isoenzymes and isoform expression: challenges for SphK as an oncotarget. | |
| dc.type | Journal Article | |
| utslib.citation.volume | 8 | |
| utslib.location.activity | United States | |
| utslib.for | 0601 Biochemistry and Cell Biology | |
| utslib.for | 1112 Oncology and Carcinogenesis | |
| pubs.organisational-group | /University of Technology Sydney/Faculty of Science | |
| pubs.organisational-group | /University of Technology Sydney/Faculty of Science/School of Life Sciences | |
| pubs.organisational-group | /University of Technology Sydney | |
| pubs.organisational-group | /University of Technology Sydney/Strength - CHT - Health Technologies | |
| pubs.organisational-group | /University of Technology Sydney/Students | |
| utslib.copyright.status | open_access | * |
| pubs.consider-herdc | true | |
| dc.date.updated | 2020-05-21T05:51:22Z | |
| pubs.issue | 22 | |
| pubs.publication-status | Published | |
| pubs.volume | 8 | |
| utslib.start-page | 36898 | |
| utslib.citation.issue | 22 |
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.
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