Antitumor antibiotic fostriecin covalently binds to cysteine-269 residue of protein phosphatase 2A catalytic subunit in mammalian cells
Toshifumi Takeuchi
1
,
Noriyuki Takahashi
1
,
Kazutomo Ishi
2
,
Tomoe Kusayanagi
1
,
Kouji Kuramochi
1
,
Fumio Sugawara
2
Тип публикации: Journal Article
Дата публикации: 2009-12-01
scimago Q2
wos Q1
БС1
SJR: 0.608
CiteScore: 6.7
Impact factor: 3.0
ISSN: 09680896, 14643391
PubMed ID:
19857968
Organic Chemistry
Drug Discovery
Biochemistry
Molecular Biology
Pharmaceutical Science
Clinical Biochemistry
Molecular Medicine
Краткое описание
Fostriecin is a phosphate monoester with excellent antitumor activity against mouse leukemia, and it is a potent inhibitor of protein phosphatase (PP) 2A. This compound has been predicted to covalently bind to the Cys269 residue of the PP2A catalytic subunit (PP2Ac) at the α,β-unsaturated lactone via a conjugate addition reaction. However, this binding has not yet been experimentally proven. To confirm such binding, we synthesized biotin-labeled fostriecin (bio-Fos), which has an inhibitory activity against the proliferation of mouse leukemia cells. We showed that fostriecin directly binds to PP2Ac in HeLa S3 cells by pull-down assays using bio-Fos. Moreover, we directly demonstrated that fostriecin covalently binds to the Cys269 residue of PP2Ac by matrix assisted laser desorption/ionization time-of-flight mass spectrometry analysis. From these results, the inhibitory mechanism of fostriecin on PP2A activity is discussed.
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Takeuchi T. et al. Antitumor antibiotic fostriecin covalently binds to cysteine-269 residue of protein phosphatase 2A catalytic subunit in mammalian cells // Bioorganic and Medicinal Chemistry. 2009. Vol. 17. No. 23. pp. 8113-8122.
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Takeuchi T., Takahashi N., Ishi K., Kusayanagi T., Kuramochi K., Sugawara F. Antitumor antibiotic fostriecin covalently binds to cysteine-269 residue of protein phosphatase 2A catalytic subunit in mammalian cells // Bioorganic and Medicinal Chemistry. 2009. Vol. 17. No. 23. pp. 8113-8122.
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TY - JOUR
DO - 10.1016/j.bmc.2009.09.050
UR - https://doi.org/10.1016/j.bmc.2009.09.050
TI - Antitumor antibiotic fostriecin covalently binds to cysteine-269 residue of protein phosphatase 2A catalytic subunit in mammalian cells
T2 - Bioorganic and Medicinal Chemistry
AU - Takeuchi, Toshifumi
AU - Takahashi, Noriyuki
AU - Ishi, Kazutomo
AU - Kusayanagi, Tomoe
AU - Kuramochi, Kouji
AU - Sugawara, Fumio
PY - 2009
DA - 2009/12/01
PB - Elsevier
SP - 8113-8122
IS - 23
VL - 17
PMID - 19857968
SN - 0968-0896
SN - 1464-3391
ER -
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@article{2009_Takeuchi,
author = {Toshifumi Takeuchi and Noriyuki Takahashi and Kazutomo Ishi and Tomoe Kusayanagi and Kouji Kuramochi and Fumio Sugawara},
title = {Antitumor antibiotic fostriecin covalently binds to cysteine-269 residue of protein phosphatase 2A catalytic subunit in mammalian cells},
journal = {Bioorganic and Medicinal Chemistry},
year = {2009},
volume = {17},
publisher = {Elsevier},
month = {dec},
url = {https://doi.org/10.1016/j.bmc.2009.09.050},
number = {23},
pages = {8113--8122},
doi = {10.1016/j.bmc.2009.09.050}
}
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MLA
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Takeuchi, Toshifumi, et al. “Antitumor antibiotic fostriecin covalently binds to cysteine-269 residue of protein phosphatase 2A catalytic subunit in mammalian cells.” Bioorganic and Medicinal Chemistry, vol. 17, no. 23, Dec. 2009, pp. 8113-8122. https://doi.org/10.1016/j.bmc.2009.09.050.