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Proteomic characterization of the cytotoxic mechanism of gold (III) porphyrin 1a, a potential anticancer drug.

Abstract
There has been increasing interest in the potential applications of gold (III) complexes as anticancer drugs with higher cytotoxicity and fewer side effects than existing metal anticancer drugs. Our previous findings demonstrated that gold (III) porphyrin 1a preferentially induced apoptosis in a cancer cell line (SUNE1). In this study, we identified differentially expressed proteins related to the drug's cytotoxic action by comparing the protein alterations induced by gold (III) porphyrin 1a and cisplatin treatments. Several clusters of altered proteins were identified, including cellular structure and stress-related chaperone proteins, proteins involved in reactive oxygen species and enzyme proteins, translation factors, proteins that mediate cell proliferation or differentiation, and proteins participating in the internal degradation systems. Our results indicated that multiple factors leading to apoptosis were involved in drug cytotoxicity in SUNE1 cells. The balance between pro-apoptotic and anti-apoptotic signals determined the final fate of cancer cells.
AuthorsYing Wang, Qing-Yu He, Chi-Ming Che, Jen-Fu Chiu
JournalProteomics (Proteomics) Vol. 6 Issue 1 Pg. 131-42 (Jan 2006) ISSN: 1615-9853 [Print] Germany
PMID16287165 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Antineoplastic Agents
  • Metalloporphyrins
  • Proteome
  • gold (III) porphyrin 1a
  • Cisplatin
Topics
  • Antineoplastic Agents (pharmacology)
  • Apoptosis (drug effects)
  • Blotting, Western
  • Cell Line, Tumor
  • Cisplatin (pharmacology)
  • Electrophoresis, Gel, Two-Dimensional
  • Flow Cytometry
  • Humans
  • Metalloporphyrins (pharmacology)
  • Microscopy, Confocal
  • Proteome

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