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Involvement of cytochrome c and caspases in apoptotic cell death of human submandibular gland ductal cells induced by concanamycin A.

Abstract
In the present study, we found that a specific inhibitor of vacuolar type H+-ATPase (V-ATPase), concanamycin A, induced apoptosis in a human submandibular gland ductal cancer cell line, HSG. Immunoblot analysis revealed that cytochrome c was released from mitochondria into the cytoplasm when HSG cells were cultured with concanamycin A for 6 h. The maximum activities of caspase-3 and -9 were reached in HSG cells after 18 and 12 h culture of concanamycin A, respectively. Both caspase-3 and -9 were cleaved to an active form in HSG cells cultured with concanamycin A. Interestingly, concanamycin A decreased the level of heat shock protein 27 (HSP27) in HSG cells. Taken together, these findings suggest that apoptosis in HSG cells induced by concanamycin A is regulated by cytochrome c released from mitochondria into cytoplasm and the subsequent activation of caspases, and that HSP27 may interfere with caspase-dependent apoptotic cell death induced by concanamycin A.
AuthorsKatsuya Aiko, Toshiyuki Tsujisawa, Takeyoshi Koseki, Shinichi Hashimoto, Yasuhiro Morimoto, Teruo Amagasa, Tatsuji Nishihara
JournalCellular signalling (Cell Signal) Vol. 14 Issue 8 Pg. 717-22 (Aug 2002) ISSN: 0898-6568 [Print] England
PMID12020772 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Anti-Bacterial Agents
  • Cytochrome c Group
  • Enzyme Inhibitors
  • HSP27 Heat-Shock Proteins
  • HSPB1 protein, human
  • Heat-Shock Proteins
  • Macrolides
  • Molecular Chaperones
  • Neoplasm Proteins
  • concanamycin A
  • Caspases
  • Vacuolar Proton-Translocating ATPases
Topics
  • Anti-Bacterial Agents (antagonists & inhibitors, toxicity)
  • Apoptosis
  • Caspases (physiology)
  • Cytochrome c Group (physiology)
  • Enzyme Inhibitors (toxicity)
  • HSP27 Heat-Shock Proteins
  • Heat-Shock Proteins
  • Heat-Shock Response
  • Humans
  • Kinetics
  • Macrolides
  • Mitochondria (metabolism)
  • Molecular Chaperones
  • Neoplasm Proteins (metabolism)
  • Submandibular Gland (cytology, enzymology, metabolism)
  • Tumor Cells, Cultured
  • Vacuolar Proton-Translocating ATPases (antagonists & inhibitors)

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