期刊
CHEMICO-BIOLOGICAL INTERACTIONS
卷 176, 期 2-3, 页码 204-211出版社
ELSEVIER IRELAND LTD
DOI: 10.1016/j.cbi.2008.08.004
关键词
Saporin; Saponin; Clathrin-mediated endocytosis
资金
- German Research Foundation [FU 408/3-1]
Saporin, a type I ribosome-inactivating protein (RIP), removes adenine residues from the 28S ribosomal RNA as part of a process that leads to inhibition of protein synthesis. However, as shown in this study, neither saporin nor his-tagged saporin (both 0.6-6pM) exert toxicity on several human cell lines including H-2171, SK-N-SH, HEP-G2, MOLT-3, THP-1, HL-60 and ECV-304. Saporin and his-tagged saporin became highly cytotoxic when they were used in a combined treatment with Soapwort saponins (SA). When combined with SA (2-4 mu g/ml) saporin became as cytotoxic as the highly toxic type II RIP rViscumin reflected by an IC50 of 42.5 x 10(-12) M for saporin and 21.5 x 10(-12) M for rViscumin. We demonstrated that saporin was internalized via clathrin-mediated endocytosis, followed by the release into the endosomal transport system. Our results indicate that SA triggers this endocytic event rendering the otherwise cell membrane impermeable type I RIP saporin a potent cytotoxin. This effect was not cell line-specific suggesting that saporin exploits a common SA-dependent mechanism to enter cells. (C) 2008 Elsevier Ireland Ltd. All rights reserved.
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