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Sphingosine 1-Phosphate Rapidly Activates the Mitogen-activated Protein Kinase Pathway by a G Protein-dependent Mechanism
Open accessAbstract
Addition of sphingosine 1-phosphate induces proliferation of quiescent Swiss 3T3 fibroblasts by unknown mechanisms. To identify the pathways involved, the ability of sphingosine 1-phosphate to activate mitogen-activated protein (MAP) kinase was studied. Sphingosine 1-phosphate rapidly activated the Raf/MAP kinase kinase (MKK)/MAP kinase pathway, and the concentration dependence for MAP kinase activation correlated with that for induction of DNA synthesis. Both MKK1 and MKK2 were activated by sphingosine 1-phosphate, assessed by specific immune complex kinase assays. Prior treatment of the Swiss 3T3 cells with pertussis toxin inhibited 70-80% of the sphingosine 1-phosphate-stimulated MAP kinase activity. Thus, one of the direct or indirect targets of exogenous sphingosine 1-phosphate appears to be a G(i)/G(o) protein.
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Cited by
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van BIESEN, T., LUTTRELL, L. M., HAWES, B. E., & LEFKOWITZ, R. J. (1996) · Endocrine Reviews · doi:10.1210/edrv-17-6-698 · Cited by 361
Edsall, L. C., Pirianov, G. G., & Spiegel, S. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-18-06952.1997 · Cited by 275
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Metadata
- Authors
- Wu, J., Spiegel, S., & Sturgill, T. W.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1995-05
- Volume
- 270
- Issue
- 19
- Pages
- 11484-11488
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1996532068
- Cited by
- 177
- References
- 0
- FWCI
- 8.29
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Sphingosine 1-Phosphate Rapidly Activates the Mitogen-activated Protein Kinase Pathway by a G Protein-dependent Mechanism. https://app.cochat.ai/papers/10.1074/jbc.270.19.11484
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- Wu, J., Spiegel, S., & Sturgill, T. W. (1995). Sphingosine 1-Phosphate Rapidly Activates the Mitogen-activated Protein Kinase Pathway by a G Protein-dependent Mechanism. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.270.19.11484
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