A novel anti-lymphoma protein RE26 from <Emphasis Type="Italic">Rozites emodensis</Emphasis> (Berk.) Moser |
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Authors: | Meng Gong Minjie Xia Jing Zhang Jiao Gu Xuyang Liu Jingqiu Cheng |
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Institution: | (1) Laboratory of Endocrinology and Metabolism, West China Hospital, Sichuan University, Chengdu, 610064, China;(2) Key Laboratory of Transplant Engineering and Immunology, Ministry of Health, West China Hospital, Sichuan University, Chengdu, 610064, China;(3) Department of Ophthalmology and Ophthalmic Laboratories, Torsten Wiesel Research Institute, West China Hospital, Sichuan University, Chengdu, 610064, China; |
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Abstract: | A novel antitumor protein, designated RE26, with anti-lymphoma activity was purified from a Tris–HCl buffer extract of Rozites emodensis (Berk.) Moser by three successive steps of ion exchange chromatography. SDS-PAGE and gel filtration chromatography revealed
that RE26 is a monomeric protein of 26 kDa, and isoelectrofocusing assay indicated its isoelectric point of 4.3–4.4. RE26
has high stability over a wide pH range (pH 3–11) but is sensitive to temperature and only stable under 40 °C. Partial amino
acid sequences of two RE26 peptide fragments were determined by Edman degradation as GLEEEETLLLLFFPP and GTEQE. The half-maximal
inhibitory concentration (IC50) of RE26 against tested lymphoma cell lines was around 4 μg/ml. In vitro experiments showed that RE26 could specifically
bind to lymphoma cells; activate the caspases, including caspases 3, 8, and 9 in host cells; and induce apoptosis. Experiments
in nude mice indicated local RE26 injection adjacent to tumor site could inhibit lymphoma formation. |
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