β-lapachone induces growth inhibition and apoptosis in bladder cancer cells by modulation of BCL-2 family and activation of caspases
Aim: To study in vitro the molecular mechanism of apoptosis caused by b-lapachone, a quinone obtained from the bark of the lapacho tree (Tabebuia avellanedae). Materials and Methods: The study was carried out on human bladder carcinoma T24 cell line. Determination of cell viability was done using tr...
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| Дата: | 2006 |
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| Автори: | , , , , , , |
| Формат: | Стаття |
| Мова: | English |
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Інститут експериментальної патології, онкології і радіобіології ім. Р.Є. Кавецького НАН України
2006
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| Назва видання: | Experimental Oncology |
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| Онлайн доступ: | http://dspace.nbuv.gov.ua/handle/123456789/134525 |
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| Назва журналу: | Digital Library of Periodicals of National Academy of Sciences of Ukraine |
| Цитувати: | β-lapachone induces growth inhibition and apoptosis in bladder cancer cells by modulation of BCL-2 family and activation of caspases / J.I. Lee, D.Y. Choi, H.S. Chung, H.G. Seo, H.J. Woo, B.T. Choi, Y.H. Choi // Experimental Oncology. — 2006. — Т. 28, № 1. — С. 30-35. — Бібліогр.: 22 назв. — англ. |
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irk-123456789-1345252018-06-14T03:06:09Z β-lapachone induces growth inhibition and apoptosis in bladder cancer cells by modulation of BCL-2 family and activation of caspases Lee, J.I. Choi, D.Y. Chung, H.S. Seo, H.G. Woo, H.J. Choi, B.T. Choi, Y.H. Original contributions Aim: To study in vitro the molecular mechanism of apoptosis caused by b-lapachone, a quinone obtained from the bark of the lapacho tree (Tabebuia avellanedae). Materials and Methods: The study was carried out on human bladder carcinoma T24 cell line. Determination of cell viability was done using trypan blue exclusion method, apoptosis quantitative estimation — by DAPI staining and agarose gel electrophoresis for DNA fragmentation. Flow cytometry analysis, RT-PCR and Western blot analysis, colorimetric assay of caspase activity were applied as well. Results: It was found that in micromolar range of concentrations b-lapachone inhibited the viability of T24 cells by inducing apoptosis, which could be proved by formation of apoptotic bodies and DNA fragmentation. Treatment of T24 cells with b-lapachone resulted in a down-regulation of Bcl-2 expression and up-regulation of Bax expression. b-lapachone-induced apoptosis was also associated with activation of caspase-3 and caspase-9, inhibition of IAP expression, and degradation of poly (ADP-ribose) polymerase, phospholipase C-g1 and b-catenin proteins. At the same time Fas and FasL levels were inhibited upon treatment with b-lapachone in a concentration-dependent manner. Conclusion: b-lapachone-induced apoptosis in T24 cells is mediated, at least in part, by the mitochondrial-signaling pathway. Цель: изучить механизмы апоптоза клеток карциномы мочевого пузыря человека Т24 при действии β-лапакона, хинона из коры дерева Tabebuia avellanedae. Материалы и методы: для определения жизнеспособности клеток использовали окраску трипановым синим; окрашивание DAPI и электрофоретический анализ фрагментации ДНК в агарозном геле, метод проточной цитометрии (для количественной оценки апоптоза); полимеразную цепную реакцию в режиме реального времени (РВ-ПЦР) и Вестерн блот-анализ (для оценки уровня экспрессии генов и белков), а также колориметрический анализ активности каспаз. Результаты: выявлено, что в микромолярных концентрациях β-лапакон понижает жизне- способность клеток линии Т24 путем активации апоптоза, что подтверждается формированием апоптотических тел и фрагментацией ДНК. Результаты РВ-ПЦР и иммуноблоттинга указывают на то, что обработка клеток β-лапаконом приводит к снижению экспрессии Bcl-2 и к активации Bax. Апоптоз, индуцированный β-лапаконом, также сопровож- дается активацией каспаз -3 и -9, ингибированием экспрессии семейства IAP, а также деградацией поли-(ADP-рибозо) полимеразы, фосфатазы C-γ1 и β-катенина. Тем не менее, уровень экспрессии Fas и FasL снижался при увеличении концентрации β-лапакона. Выводы: апоптоз, индуцированный при действии β-лапакона в клетках Т24, может быть час- тично опосредован митохондриальным сигнальным каскадом. 2006 Article β-lapachone induces growth inhibition and apoptosis in bladder cancer cells by modulation of BCL-2 family and activation of caspases / J.I. Lee, D.Y. Choi, H.S. Chung, H.G. Seo, H.J. Woo, B.T. Choi, Y.H. Choi // Experimental Oncology. — 2006. — Т. 28, № 1. — С. 30-35. — Бібліогр.: 22 назв. — англ. 1812-9269 http://dspace.nbuv.gov.ua/handle/123456789/134525 en Experimental Oncology Інститут експериментальної патології, онкології і радіобіології ім. Р.Є. Кавецького НАН України |
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Digital Library of Periodicals of National Academy of Sciences of Ukraine |
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DSpace DC |
| language |
English |
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Original contributions Original contributions |
| spellingShingle |
Original contributions Original contributions Lee, J.I. Choi, D.Y. Chung, H.S. Seo, H.G. Woo, H.J. Choi, B.T. Choi, Y.H. β-lapachone induces growth inhibition and apoptosis in bladder cancer cells by modulation of BCL-2 family and activation of caspases Experimental Oncology |
| description |
Aim: To study in vitro the molecular mechanism of apoptosis caused by b-lapachone, a quinone obtained from the bark of the lapacho tree (Tabebuia avellanedae). Materials and Methods: The study was carried out on human bladder carcinoma T24 cell line. Determination of cell viability was done using trypan blue exclusion method, apoptosis quantitative estimation — by DAPI staining and agarose gel electrophoresis for DNA fragmentation. Flow cytometry analysis, RT-PCR and Western blot analysis, colorimetric assay of caspase activity were applied as well. Results: It was found that in micromolar range of concentrations b-lapachone inhibited the viability of T24 cells by inducing apoptosis, which could be proved by formation of apoptotic bodies and DNA fragmentation. Treatment of T24 cells with b-lapachone resulted in a down-regulation of Bcl-2 expression and up-regulation of Bax expression. b-lapachone-induced apoptosis was also associated with activation of caspase-3 and caspase-9, inhibition of IAP expression, and degradation of poly (ADP-ribose) polymerase, phospholipase C-g1 and b-catenin proteins. At the same time Fas and FasL levels were inhibited upon treatment with b-lapachone in a concentration-dependent manner. Conclusion: b-lapachone-induced apoptosis in T24 cells is mediated, at least in part, by the mitochondrial-signaling pathway. |
| format |
Article |
| author |
Lee, J.I. Choi, D.Y. Chung, H.S. Seo, H.G. Woo, H.J. Choi, B.T. Choi, Y.H. |
| author_facet |
Lee, J.I. Choi, D.Y. Chung, H.S. Seo, H.G. Woo, H.J. Choi, B.T. Choi, Y.H. |
| author_sort |
Lee, J.I. |
| title |
β-lapachone induces growth inhibition and apoptosis in bladder cancer cells by modulation of BCL-2 family and activation of caspases |
| title_short |
β-lapachone induces growth inhibition and apoptosis in bladder cancer cells by modulation of BCL-2 family and activation of caspases |
| title_full |
β-lapachone induces growth inhibition and apoptosis in bladder cancer cells by modulation of BCL-2 family and activation of caspases |
| title_fullStr |
β-lapachone induces growth inhibition and apoptosis in bladder cancer cells by modulation of BCL-2 family and activation of caspases |
| title_full_unstemmed |
β-lapachone induces growth inhibition and apoptosis in bladder cancer cells by modulation of BCL-2 family and activation of caspases |
| title_sort |
β-lapachone induces growth inhibition and apoptosis in bladder cancer cells by modulation of bcl-2 family and activation of caspases |
| publisher |
Інститут експериментальної патології, онкології і радіобіології ім. Р.Є. Кавецького НАН України |
| publishDate |
2006 |
| topic_facet |
Original contributions |
| url |
http://dspace.nbuv.gov.ua/handle/123456789/134525 |
| citation_txt |
β-lapachone induces growth inhibition and apoptosis in bladder cancer cells by modulation of BCL-2 family and activation of caspases / J.I. Lee, D.Y. Choi, H.S. Chung, H.G. Seo, H.J. Woo, B.T. Choi, Y.H. Choi // Experimental Oncology. — 2006. — Т. 28, № 1. — С. 30-35. — Бібліогр.: 22 назв. — англ. |
| series |
Experimental Oncology |
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