Small, novel proteins from the mistletoe Phoradendron tomentosum exhibit highly selective cytotoxicity to human breast cancer cells
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Four novel proteins (phoratoxins C–F) have been isolated from the North American mistletoe Phoradendron tomentosum. The amino acid sequences of these phoratoxins were determined unambiguously using a combination of Edman degradation and trypsin enzymatic digestion, and by electrospray ionization tandem mass spectrometry sequencing. Phoratoxins C, E and F consist of 46 amino acid residues; and phoratoxin D of 41. All proteins had six cysteines, similar to the earlier described phoratoxins A and B, which are thionins. The cytotoxicity of each protein was evaluated in a human cell line panel that represented several cytotoxic drug-resistance mechanisms. For the half-maximal inhibitory concentrations (IC50 values) of the different cell lines in the panel, correlation with those of standard drugs was low. The most potent cytotoxic phoratoxin C was further tested on primary cultures of human tumor cells from patients. The solid tumor samples from breast cancer cells were 18 times more sensitive to phoratoxin C than the tested hematological tumor samples.
- Small, novel proteins from the mistletoe Phoradendron tomentosum exhibit highly selective cytotoxicity to human breast cancer cells
Cellular and Molecular Life Sciences CMLS
Volume 60, Issue 1 , pp 165-175
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- Birkhäuser Verlag
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- Key words. Breast cancer; cytotoxicity drug screening; mistletoe proteins; Phoradendron tomentosum; phoratoxins; thionins; tumor cell lines.
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- Author Affiliations
- A1. Division of Pharmacognosy, Department of Medicinal Chemistry, Biomedical Centre, Uppsala University, PO Box 574, 751 23 Uppsala (Sweden), Fax: + 46 18 509101, e-mail: firstname.lastname@example.org, SE
- A2. Division of Clinical Pharmacology, University Hospital, Uppsala University, Uppsala (Sweden), SE
- A3. Uppsala Genetic Center, Department of Plant Biology, Swedish University of Agricultural Science, Uppsala (Sweden), SE