the discodermia calyx toxin calyculin a enhances cyclin d1 phosphorylation and degradation, and arrests cell cycle progression in human breast cancer cellsdiscodermia花萼毒素calyculin有提高细胞周期蛋白d1磷酸化和退化,人类乳腺癌细胞细胞周期进程和逮捕.pdfVIP

下载本文档

15
0
约5.06万字
约 15页
2017-09-12 发布于上海
举报
版权申诉

the discodermia calyx toxin calyculin a enhances cyclin d1 phosphorylation and degradation, and arrests cell cycle progression in human breast cancer cellsdiscodermia花萼毒素calyculin有提高细胞周期蛋白d1磷酸化和退化,人类乳腺癌细胞细胞周期进程和逮捕.pdf

1、原创力文档（book118）网站文档一经付费（服务费），不意味着购买了该文档的版权，仅供个人/单位学习、研究之用，不得用于商业用途，未经授权，严禁复制、发行、汇编、翻译或者网络传播等，侵权必究。。
2、本站所有内容均由合作方或网友上传，本站不对文档的完整性、权威性及其观点立场正确性做任何保证或承诺！文档内容仅供研究参考，付费前请自行鉴别。如您付费，意味着您自己接受本站规则且自行承担风险，本站不退款、不进行额外附加服务；查看《如何避免下载的几个坑》。如果您已付费下载过本站文档，您可以点击这里二次下载。
3、如文档侵犯商业秘密、侵犯著作权、侵犯人身权等，请点击“版权申诉”（推荐），也可以打举报电话：400-050-0827(电话支持时间：9:00-18:30)。
4、该文档为VIP文档，如果想要下载，成为VIP会员后，下载免费。
5、成为VIP后，下载本文档将扣除1次下载权益。下载后，不支持退款、换文档。如有疑问请联系我们。
6、成为VIP后，您将拥有八大权益，权益包括：VIP文档下载权益、阅读免打扰、文档格式转换、高级专利检索、专属身份标志、高级客服、多端互通、版权登记。
7、VIP文档为合作方或网友上传，每下载1次，网站将根据用户上传文档的质量评分、类型等，对文档贡献者给予高额补贴、流量扶持。如果你也想贡献VIP文档。上传文档

the discodermia calyx toxin calyculin a enhances cyclin d1 phosphorylation and degradation, and arrests cell cycle progression in human breast cancer cellsdiscodermia花萼毒素calyculin有提高细胞周期蛋白d1磷酸化和退化,人类乳腺癌细胞细胞周期进程和逮捕

Toxins 2011, 3, 105-119; doi:10.3390/toxins3010105 OPEN ACCESS toxins ISSN 2072-6651 /journal/toxins Article The Discodermia calyx Toxin Calyculin A Enhances Cyclin D1 Phosphorylation and Degradation, and Arrests Cell Cycle Progression in Human Breast Cancer Cells Jessica R. Edelson and David L. Brautigan * Center for Cell Signaling and Department of Microbiology, University of Virginia School of Medicine, Charlottesville, VA 22908, USA; E-Mail: jrh9x@ * Author to whom correspondence should be addressed; E-Mail: db8g@; Tel.: +1-434-924-5892; Fax: +1-434-924-1236. Received: 8 October 2010; in revised form: 8 January 2011 / Accepted: 21 January 2011 / Published: 24 January 2011 Abstract: Cyclin D1 is a key regulator of the cell cycle that is over expressed in more than half of breast cancer patients. The levels of cyclin D1 are controlled primarily through post-translational mechanisms and phosphorylation of cyclin D1 at T286 induces its proteasomal degradation. To date, no studies have explored the involvement of phosphatases in this process. Here we treated human breast cancer cells with the structurally distinct toxins calyculin A, okadaic acid, and cantharidin, which are known to inhibit Ser/Thr phosphatases of the PPP family. At low nanomolar concentrations calyculin A induced T286 phosphorylation and degradation of cyclin D1 via the proteosome in MDA-MB-468 and MDA-MB-231 cells. Cyclin D1 degr