Enhancement of chemosensitivity toward peplomycin by calpastatin-stabilized NF-κB p65 in esophageal carcinoma cells: Possible involvement of Fas/Fas-L synergism

T. L. Liu, H. Shimada, T. Ochiai, T. Shiratori, Sey-En Lin, M. Kitagawa, K. Harigaya, M. Maki, M. Oka, T. Abe, M. Takiguchi, T. Hiwasa

研究成果: 雜誌貢獻文章

15 引文 (Scopus)

摘要

Chemosensitivity to anticancer drugs was compared between two human esophageal carcinoma cell lines, T.Tn and YES-6 cells. T.Tn cells were more resistant than YES-6 cells to peplomycin (PEP) but not to the other anticancer drugs such as camptothecin, mitomycin C and cytosine arabinoside. Western blot analysis showed higher expression levels of m-calpain and activated μ-calpain in T.Tn cells than in YES-6 cells. On the other hand, YES-6 cells showed a high expression level of calpastatin, which is a calpain-specific endogenous inhibitor. To investigate whether calpain activity was involved in the chemosensitivity, T.Tn cells were transfected with calpastatin cDNA in an inducible expression vector. The induction of calpastatin was accompanied by increased chemosensitivity to PEP. The increases in calpastatin levels were followed by serial increases in the expression levels of NF-κB p65 and Fas. Since purified m- or μ-calpain degraded NF-κB p65 in vitro, it is possible that calpastatin suppressed calpain-mediated degradation of NF-κB p65. Fas ligand (Fas-L) protein levels increased after treatment of the parental T.Tn and calpastatin-transfected cells with PEP, suggesting the synergism between calpastatin-induced Fas and PEP-induced Fas-L. These results suggest that calpain/calpastatin expression levels are effective markers for predicting the sensitivity of human esophageal carcinoma cells to PEP.

原文英語
頁(從 - 到)1025-1037
頁數13
期刊Apoptosis
11
發行號6
DOIs
出版狀態已發佈 - 六月 1 2006
對外發佈Yes

指紋

Peplomycin
Fas Ligand Protein
Calpain
Cells
Carcinoma
Camptothecin
calpastatin
Cytarabine
Mitomycin
Pharmaceutical Preparations
Complementary DNA
Western Blotting
Degradation

ASJC Scopus subject areas

  • Pharmacology
  • Pharmaceutical Science
  • Clinical Biochemistry
  • Cell Biology
  • Biochemistry, medical
  • Cancer Research

引用此文

Enhancement of chemosensitivity toward peplomycin by calpastatin-stabilized NF-κB p65 in esophageal carcinoma cells : Possible involvement of Fas/Fas-L synergism. / Liu, T. L.; Shimada, H.; Ochiai, T.; Shiratori, T.; Lin, Sey-En; Kitagawa, M.; Harigaya, K.; Maki, M.; Oka, M.; Abe, T.; Takiguchi, M.; Hiwasa, T.

於: Apoptosis, 卷 11, 編號 6, 01.06.2006, p. 1025-1037.

研究成果: 雜誌貢獻文章

Liu, TL, Shimada, H, Ochiai, T, Shiratori, T, Lin, S-E, Kitagawa, M, Harigaya, K, Maki, M, Oka, M, Abe, T, Takiguchi, M & Hiwasa, T 2006, 'Enhancement of chemosensitivity toward peplomycin by calpastatin-stabilized NF-κB p65 in esophageal carcinoma cells: Possible involvement of Fas/Fas-L synergism', Apoptosis, 卷 11, 編號 6, 頁 1025-1037. https://doi.org/10.1007/s10495-006-6353-y
Liu, T. L. ; Shimada, H. ; Ochiai, T. ; Shiratori, T. ; Lin, Sey-En ; Kitagawa, M. ; Harigaya, K. ; Maki, M. ; Oka, M. ; Abe, T. ; Takiguchi, M. ; Hiwasa, T. / Enhancement of chemosensitivity toward peplomycin by calpastatin-stabilized NF-κB p65 in esophageal carcinoma cells : Possible involvement of Fas/Fas-L synergism. 於: Apoptosis. 2006 ; 卷 11, 編號 6. 頁 1025-1037.
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title = "Enhancement of chemosensitivity toward peplomycin by calpastatin-stabilized NF-κB p65 in esophageal carcinoma cells: Possible involvement of Fas/Fas-L synergism",
abstract = "Chemosensitivity to anticancer drugs was compared between two human esophageal carcinoma cell lines, T.Tn and YES-6 cells. T.Tn cells were more resistant than YES-6 cells to peplomycin (PEP) but not to the other anticancer drugs such as camptothecin, mitomycin C and cytosine arabinoside. Western blot analysis showed higher expression levels of m-calpain and activated μ-calpain in T.Tn cells than in YES-6 cells. On the other hand, YES-6 cells showed a high expression level of calpastatin, which is a calpain-specific endogenous inhibitor. To investigate whether calpain activity was involved in the chemosensitivity, T.Tn cells were transfected with calpastatin cDNA in an inducible expression vector. The induction of calpastatin was accompanied by increased chemosensitivity to PEP. The increases in calpastatin levels were followed by serial increases in the expression levels of NF-κB p65 and Fas. Since purified m- or μ-calpain degraded NF-κB p65 in vitro, it is possible that calpastatin suppressed calpain-mediated degradation of NF-κB p65. Fas ligand (Fas-L) protein levels increased after treatment of the parental T.Tn and calpastatin-transfected cells with PEP, suggesting the synergism between calpastatin-induced Fas and PEP-induced Fas-L. These results suggest that calpain/calpastatin expression levels are effective markers for predicting the sensitivity of human esophageal carcinoma cells to PEP.",
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T1 - Enhancement of chemosensitivity toward peplomycin by calpastatin-stabilized NF-κB p65 in esophageal carcinoma cells

T2 - Possible involvement of Fas/Fas-L synergism

AU - Liu, T. L.

AU - Shimada, H.

AU - Ochiai, T.

AU - Shiratori, T.

AU - Lin, Sey-En

AU - Kitagawa, M.

AU - Harigaya, K.

AU - Maki, M.

AU - Oka, M.

AU - Abe, T.

AU - Takiguchi, M.

AU - Hiwasa, T.

PY - 2006/6/1

Y1 - 2006/6/1

N2 - Chemosensitivity to anticancer drugs was compared between two human esophageal carcinoma cell lines, T.Tn and YES-6 cells. T.Tn cells were more resistant than YES-6 cells to peplomycin (PEP) but not to the other anticancer drugs such as camptothecin, mitomycin C and cytosine arabinoside. Western blot analysis showed higher expression levels of m-calpain and activated μ-calpain in T.Tn cells than in YES-6 cells. On the other hand, YES-6 cells showed a high expression level of calpastatin, which is a calpain-specific endogenous inhibitor. To investigate whether calpain activity was involved in the chemosensitivity, T.Tn cells were transfected with calpastatin cDNA in an inducible expression vector. The induction of calpastatin was accompanied by increased chemosensitivity to PEP. The increases in calpastatin levels were followed by serial increases in the expression levels of NF-κB p65 and Fas. Since purified m- or μ-calpain degraded NF-κB p65 in vitro, it is possible that calpastatin suppressed calpain-mediated degradation of NF-κB p65. Fas ligand (Fas-L) protein levels increased after treatment of the parental T.Tn and calpastatin-transfected cells with PEP, suggesting the synergism between calpastatin-induced Fas and PEP-induced Fas-L. These results suggest that calpain/calpastatin expression levels are effective markers for predicting the sensitivity of human esophageal carcinoma cells to PEP.

AB - Chemosensitivity to anticancer drugs was compared between two human esophageal carcinoma cell lines, T.Tn and YES-6 cells. T.Tn cells were more resistant than YES-6 cells to peplomycin (PEP) but not to the other anticancer drugs such as camptothecin, mitomycin C and cytosine arabinoside. Western blot analysis showed higher expression levels of m-calpain and activated μ-calpain in T.Tn cells than in YES-6 cells. On the other hand, YES-6 cells showed a high expression level of calpastatin, which is a calpain-specific endogenous inhibitor. To investigate whether calpain activity was involved in the chemosensitivity, T.Tn cells were transfected with calpastatin cDNA in an inducible expression vector. The induction of calpastatin was accompanied by increased chemosensitivity to PEP. The increases in calpastatin levels were followed by serial increases in the expression levels of NF-κB p65 and Fas. Since purified m- or μ-calpain degraded NF-κB p65 in vitro, it is possible that calpastatin suppressed calpain-mediated degradation of NF-κB p65. Fas ligand (Fas-L) protein levels increased after treatment of the parental T.Tn and calpastatin-transfected cells with PEP, suggesting the synergism between calpastatin-induced Fas and PEP-induced Fas-L. These results suggest that calpain/calpastatin expression levels are effective markers for predicting the sensitivity of human esophageal carcinoma cells to PEP.

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KW - Esophageal carcinoma

KW - Fas

KW - NF-κB

KW - Peplomycin

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