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SP600125, an anthrapyrazolone inhibitor of Jun N-terminal kinase
Open accessAbstract
Jun N-terminal kinase (JNK) is a stress-activated protein kinase that can be induced by inflammatory cytokines, bacterial endotoxin, osmotic shock, UV radiation, and hypoxia. We report the identification of an anthrapyrazolone series with significant inhibition of JNK1, -2, and -3 ( K i = 0.19 μM). SP600125 is a reversible ATP-competitive inhibitor with >20-fold selectivity vs. a range of kinases and enzymes tested. In cells, SP600125 dose dependently inhibited the phosphorylation of c-Jun, the expression of inflammatory genes COX-2 , IL-2 , IFN -γ, TNF -α, and prevented the activation and differentiation of primary human CD4 cell cultures. In animal studies, SP600125 blocked (bacterial) lipopolysaccharide-induced expression of tumor necrosis factor-α and inhibited anti-CD3-induced apoptosis of CD4 + CD8 + thymocytes. Our study supports targeting JNK as an important strategy in inflammatory disease, apoptotic cell death, and cancer.
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“In in vivo studies in mice, SP600125 inhibited lipopolysaccharide-induced expression of TNFa and prevented anti-CD3-mediated thymocyte apoptosis (Bennett et al , 2001).”
From Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125 (2004) · cites this paper as Bennett et al , 2001
In the citing paper
“In cells, SP600125 dose-dependently inhibited the phosphorylation of c-jun, the expression of inflammatory genes COX-2, IL2, IHNg , and TNFa , and prevented the activation and differentiation of human CD4 cell.”
From Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125 (2004) · cites this paper as Bennett et al , 2001
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“This result is very consistent with the previous structure-activity relationship studies, which revealed that all of the derivatives having N-alkyl substituents instead of the free NH group at the 2-position showed significant loss in inhibitory activity (Bennett et al , 2001).”
From Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125 (2004) · cites this paper as Bennett et al , 2001
In the citing paper
“SP600125 is a reversible ATPcompetitive inhibitor with more than 20-fold selectivity over other kinases including Erk, p38 MAPKs, MKKs, and PKCs.”
From Structural basis for the selective inhibition of JNK1 by the scaffolding protein JIP1 and SP600125 (2004) · cites this paper as Bennett et al , 2001
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Metadata
- Authors
- Bennett, B. L., Sasaki, D. T., Murray, B. W., O'Leary, E. C., Sakata, S. T., Xu, W., Leisten, J. C., Motiwala, A., Pierce, S., Satoh, Y., Bhagwat, S. S., Manning, A. M., & Anderson, D. W.
- Affiliations
- Signal Research Division, Celgene Corporation, 5555 Oberlin Drive, San Diego, CA 92121
- Yale University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2001-11-20
- Volume
- 98
- Issue
- 24
- Pages
- 13681-13686
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC61101
- OpenAlex
- W2096931514
- Cited by
- 2,558
- References
- 46
- Citations by year
- 2026: 40 · 2025: 49 · 2024: 77 · 2023: 66 · 2022: 51 · 2021: 69 · 2020: 71 · 2019: 52 · 2018: 60 · 2017: 91 · 2016: 97 · 2015: 80 · 2014: 100 · 2013: 107 · 2012: 132
- FWCI
- 47.43
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Melanoma and MAPK Pathways
- Keywords
- SP600125, Jun N-terminal kinase, ATP-competitive kinase inhibitors, c-Jun phosphorylation, inflammatory gene expression, cyclooxygenase-2, TNF-α, lipopolysaccharide, CD4+ T cell activation, apoptosis, thymocytes, inflammatory diseases, cancer
- MeSH terms
- Adenosine Triphosphate, Animals, Anthracenes, Anthraquinones, Binding, Competitive, Cell Differentiation, Cells, Cultured, Enzyme Inhibitors, Female, Humans, Lymphocyte Activation, Mice, Inbred C57BL, Monocytes, Pyrazoles, Structure-Activity Relationship, Tumor Necrosis Factor-alpha, Molecular Structure, CD4-Positive T-Lymphocytes, Gene Expression, Cytokines, Jurkat Cells, Mitogen-Activated Protein Kinases, Pyrazolones, Protein Kinase Inhibitors, JNK Mitogen-Activated Protein Kinases, Mice
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