| Autor: |
Hong J; Laboratory of Pathophysiological Biochemistry, Graduate School of Pharmaceutical Sciences, Tohoku University, 6-3 Aoba Aramaki, Sendai, Miyagi 980-8578, Japan., Yokomakura A, Nakano Y, Ishihara K, Kaneda M, Onodera M, Nakahama K, Morita I, Niikura K, Ahn JW, Zee O, Ohuchi K |
| Jazyk: |
angličtina |
| Zdroj: |
FEBS letters [FEBS Lett] 2006 May 15; Vol. 580 (11), pp. 2723-30. Date of Electronic Publication: 2006 Apr 21. |
| DOI: |
10.1016/j.febslet.2006.04.031 |
| Abstrakt: |
Apicularen A and the known vacuolar-type (H(+))-ATPase (V-ATPase) inhibitor bafilomycin A(1) induced apoptosis of RAW 264.7 cells, while apicularen B, an N-acetyl-glucosamine glycoside of apicularen A, was far less effective. Apicularen A inhibited vital staining with acridine orange of the intracellular organelles of RAW 264.7 cells, inhibited the ATP-dependent proton transport into inside-out microsome vesicles, and inhibited the bafilomycin A(1)-sensitive ATP hydrolysis. The IC(50) values of the proton transport were 0.58 nM for apicularen A, 13 nM for apicularen B, and 0.95 nM for bafilomycin A(1). Furthermore, apicularen A inhibited the bafilomycin A(1)-sensitive ATP hydrolysis more potently than apicularen B. F-ATPase and P-ATPase were not inhibited by apicularen A. We concluded that apicularen A inhibits V-ATPase, and thus induces apoptosis in RAW 264.7 cells. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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