ArticleThe Biochemical journal2000
Human sphingosine kinase: purification, molecular cloning and characterization of the native and recombinant enzymes.
Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.
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Who cites it
62 citing papers in PubMed, 176 citations in OpenAlex.
- Sphingosine 1-phosphate attenuates neuronal dysfunction induced by amyloid-β oligomers through endocytic internalization of NMDA receptors.The FEBS journal · 2023Article
- A Comparative Analysis ofInsects · 2022Article
- Sphingosine 1-Phosphate Metabolism and Signaling.Advances in experimental medicine and biology · 2022Article
- Expression Profile of Sphingosine Kinase 1 Isoforms in Human Cancer Tissues and Cells: Importance and Clinical Relevance of the Neglected 1b-Isoform.Journal of oncology · 2022Article
- A Comprehensive Review on the Interplay betweenCells · 2021Review
- Bioactive sphingolipids: Advancements and contributions from the laboratory of Dr. Lina M. Obeid.Cellular signalling · 2021Review
- A Novel Function of Sphingosine Kinase 2 in the Metabolism of Sphinga-4,14-Diene Lipids.Metabolites · 2020Article
- Molecular mechanisms of regulation of sphingosine kinase 1.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2018Review
- Sphingolipid biosynthesis in man and microbes.Natural product reports · 2018Review
- "Dicing and Splicing" Sphingosine Kinase and Relevance to Cancer.International journal of molecular sciences · 2017Review
- Mammalian sphingosine kinase (SphK) isoenzymes and isoform expression: challenges for SphK as an oncotarget.Oncotarget · 2017Review
- Validation of commercially available sphingosine kinase 2 antibodies for use in immunoblotting, immunoprecipitation and immunofluorescence.F1000Research · 2016Article
- Sphingosine 1-phosphate is a ligand for peroxisome proliferator-activated receptor-γ that regulates neoangiogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- A novel role of sphingosine kinase-1 in the invasion and angiogenesis of VHL mutant clear cell renal cell carcinoma.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- A selective ATP-competitive sphingosine kinase inhibitor demonstrates anti-cancer properties.Oncotarget · 2015Article
- Mouse Sphingosine Kinase 1a Is Negatively Regulated through Conventional PKC-Dependent Phosphorylation at S373 Residue.PloS one · 2015Article
- Sphingosine-1-phosphate metabolism: A structural perspective.Critical reviews in biochemistry and molecular biology · 2015Review
- Crystal Structure of Sphingosine Kinase 1 with PF-543.ACS medicinal chemistry letters · 2014Article
- Enhanced expression of transferrin receptor 1 contributes to oncogenic signalling by sphingosine kinase 1.Oncogene · 2014Article
- Sphingosine kinase 1 isoform-specific interactions in breast cancer.Molecular endocrinology (Baltimore, Md.) · 2014Article
2 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sphingosine 1-phosphate (S1P) is a novel lipid messenger that has important roles in a wide variety of mammalian cellular processes including growth, differentiation and death. Basal levels of S1P in mammalian cells are generally low, but can increase rapidly and transiently when cells are exposed to mitogenic agents and other stimuli. This increase is largely due to increased activity of sphingosine kinase (SK), the enzyme that catalyses its formation. In the current study we have purified, cloned and characterized the first human SK to obtain a better understanding of its biochemical activity and possible activation mechanisms. The enzyme was purified to homogeneity from human placenta using ammonium sulphate precipitation, anion-exchange chromatography, calmodulin-affinity chromatography and gel-filtration chromatography. This resulted in a purification of over 10(6)-fold from the original placenta extract. The enzyme was cloned and expressed in active form in both HEK-293T cells and Escherichia coli, and the recombinant E. coli-derived SK purified to homogeneity. To establish whether post-translational modifications lead to activation of human SK activity we characterized both the purified placental enzyme and the purified recombinant SK produced in E. coli, where such modifications would not occur. The premise for this study was that post-translational modifications are likely to cause conformational changes in the structure of SK, which may result in detectable changes in the physico-chemical or catalytic properties of the enzyme. Thus the enzymes were characterized with respect to substrate specificity and kinetics, inhibition kinetics and various other physico-chemical properties. In all cases, both the native and recombinant SKs displayed remarkably similar properties, indicating that post-translational modifications are not required for basal activity of human SK.
Indexed as
Identifiers
10947957PMC1221270W1985430829What OpenQuestion holds
Registered trials
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.