Sialic acid-binding lectin (leczyme) induces caspase-dependent apoptosis-mediated mitochondrial perturbation in Jurkat cells
| Autor: | Takeo Tatsuta, Masahiro Hosono, Yukiko Kariya, Kazuo Nitta, Yukiko Ogawa, Shigeki Sugawara, Sen-itiroh Hakomori |
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| Rok vydání: | 2013 |
| Předmět: |
leczyme
Cancer Research Programmed cell death antitumor effect Blotting Western mitochondria perturbation Apoptosis Sialic acid binding Mitochondrion Real-Time Polymerase Chain Reaction Jurkat cells Amphibian Proteins Caspase-Dependent Apoptosis Jurkat Cells Ribonucleases Lectins Humans RNA Messenger Cytotoxicity Caspase Membrane Potential Mitochondrial Rana catesbeiana biology Reverse Transcriptase Polymerase Chain Reaction Articles Flow Cytometry Molecular biology Mitochondria Cell biology Oncology Caspases biology.protein lectin ribonuclease caspase pathway |
| Zdroj: | International Journal of Oncology |
| ISSN: | 1791-2423 1019-6439 |
| DOI: | 10.3892/ijo.2013.2092 |
| Popis: | Sialic acid binding lectin (SBL) isolated from Rana catesbeiana oocytes is a multifunctional protein which has lectin activity, ribonuclease activity and antitumor activity. However, the mechanism of antitumor effects of SBL is unclear to date and the validity for human leukemia cells has not been fully studied. We report here that SBL shows cytotoxicity for some human leukemia cell lines including multidrug-resistant (MDR) cells. The precise mechanisms of SBL-induced apoptotic signals were analyzed by combinational usage of specific caspase inhibitors and the mitochondrial membrane depolarization detector JC-1. It was demonstrated that SBL causes mitochondrial perturbation and the apoptotic signal is amplified by caspases and cell death is executed in a caspase-dependent manner. The efficacy of this combinational usage was shown for the first time, to distinguish the apoptotic pathway in detail. SBL selectively kills tumor cells, is able to exhibit cytotoxicity regardless of P-glycoprotein expression and has potential as an alternative to conventional DNA-damaging anticancer drugs. |
| Databáze: | OpenAIRE |
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