Cytocidal Actions of Parasporin-2, an Anti-tumor Crystal Toxin from Bacillus Thuringiensis.
From: Department of Chemistry, Faculty of Science, Kyushu University, Fukuoka 812-8581, Japan. s.kitscc@mbox.nc.kyushu-u.ac.jp
The Journal of biological chemistry
- Publish Date: Sep 2006
- ISSN: 0021-9258
- Volume: 281
- Issue: 36
- Pages: 26350-60
- Medium: Print
- Language: English
- Citation (JAMA): Kitada Sakae, Abe Yuichi, Shimada Hiroyasu, et al. Cytocidal Actions of Parasporin-2, an Anti-tumor Crystal Toxin from Bacillus Thuringiensis.. J. Biol. Chem. Sep 2006;281:26350-60
Abstract
Parasporin-2, a new crystal protein derived from noninsecticidal and nonhemolytic Bacillus thuringiensis, recognizes and kills human liver and colon cancer cells as well as some classes of human cultured cells. Here we report that a potent proteinase K-resistant parasporin-2 toxin shows specific binding to and a variety of cytocidal effects against human hepatocyte cancer cells. Cleavage of the N-terminal region of parasporin-2 was essential for the toxin activity, whereas C-terminal digestion was required for rapid cell injury. Protease-activated parasporin-2 induced remarkable morphological alterations, cell blebbing, cytoskeletal alterations, and mitochondrial and endoplasmic reticulum fragmentation. The plasma membrane permeability was increased immediately after the toxin treatment and most of the cytoplasmic proteins leaked from the cells, whereas mitochondrial and endoplasmic reticulum proteins remained in the intoxicated cells. Parasporin-2 selectively bound to cancer cells in slices of liver tumor tissues and susceptible human cultured cells and became localized in the plasma membrane until the cells were damaged. Thus, parasporin-2 acts as a cytolysin that permeabilizes the plasma membrane with target cell specificity and subsequently induces cell decay.
Mesh Headings (Keywords): Animals, Antineoplastic Agents, Bacillus thuringiensis, Bacterial Toxins, Cell Membrane, Cell Shape, Cells, Cultured, Cytoskeleton, Endopeptidase K, Endotoxins, Humans, Liver, Liver Neoplasms, Peptide Fragments, Recombinant Proteins
Check for Full Text / PubMed Unique Identifier (PMID): 16809341
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