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陈竺是个好样的！老海归官至副国级却仍真搞科研
陈竺是个好样的！老海归官至副国级却仍真搞科研
昨晚看到科学网下面一篇报道《研究证实：影响蛋白通路砒霜可抗肿瘤》，见到“老熟人” 陈竺是这篇在线发表于美国《国家科学院院刊》（PNAS）论文的通讯作者。回想起我2013年回中国大陆参加大学毕业30年同学聚会，利用非常紧的时间（来回只有一周）在北京、武汉、上海三地进行“报效祖国系列演讲”，在北京的讲座结束后直接去陈竺那与他一起吃工作午餐，谈中国科学大事，到上海的讲座则是在陈赛娟的实验室进行，讲座中还重点论述了糖酵解增强对癌细胞超强生长繁殖的贡献并由此是抗癌药的重要靶点。并指出iPS细胞就是人造癌细胞，可以当作活靶子来筛选抗癌药（此发明已通国美国专利局严格审查，即将授权给与知识产权保护）。
如今，陈竺等人的最新研究终于把一个古老的中药成份的抗癌作用的机理有明辨了一些，他在前人基础上的深入钻研，必将为华科在这一领域赢得诺奖做出重要的贡献。
所以，真正的科学家就是应当这个样子：虽然官至副国级却仍真的搞科研。不像有些所谓的“赛先生”，从做助理教授起就不自己做实验，以后就只忙乎着拉关系、搞经费、占山头、结帮派，还动不动就要革中国文化的命，甚至于不惜以“知识分子”的身段耍流氓，自己江郎才尽出不了科研成果，就不要脸地抢他人的成果，抢不到就恶人先高状并倒打一耙，把真正的科学家诋毁为学术不端分子。
看来，中国的科学要发展，还真得分清谁是真想搞科学，谁是政客科学家或科学家政客！
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http://news.sciencenet.cn/htmlnews/2015/12/332933.shtm
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作者：黄辛 来源：中国科学报 发布时间：2015/12/1 9:20:23 选择字号：小 中 大 |
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本报讯（记者黄辛）上海交通大学和山东大学的一项合作研究证实，砒霜（三氧化二砷，As2O3）可以明显抑制肿瘤细胞中糖酵解通路限速酶己糖激酶2（HK2）的活性而影响细胞代谢，最终导致肿瘤细胞的凋亡。相关研究成果近日在线发表于美国《国家科学院院刊》。 As2O3在治疗APL（急性早幼粒细胞白血病）上已获成功，现有研究也表明，它在其他多种恶性肿瘤的治疗方面也有较大的潜力，但相关机制不清楚。 利用包含1.7万个重组人蛋白质的蛋白质组芯片，研究人员发展了一套基于蛋白质组芯片的小分子相互作用蛋白质快速发现技术，发现了360个As2O3直接作用蛋白。而此前全世界研究者发现的砷直接相互作用蛋白质总数不超过20个。进一步分析发现As2O3能影响一系列通路，其中最显著的是糖酵解通路，研究表明As2O3能与糖酵解通路中的绝大部分蛋白质发生直接相互作用，进而影响代谢并最终促使肿瘤细胞的凋亡。 此次发现表明了蛋白质芯片平台是快速、全局寻找药物靶标的强有力工具。专家表示，这项研究中找到的众多As2O3靶标蛋白也将为后续As2O3在除APL外的其它肿瘤治疗上的应用提供指引。 该论文共同第一作者分别为上海交通大学系统生物医学研究院博士张海南、杨丽娜以及山东大学教授凌建亚。上海交通大学研究员陶生策与该校医学院附属瑞金医院陈竺院士为本文通讯作者。 《中国科学报》 (2015-12-01 第1版 要闻) |
Systematic identification of arsenic-binding proteins reveals that hexokinase-2 is inhibited by arsenic
1. Hai-nan Zhanga,b,c,1,
3. Jian-ya Lingd,1,
5. Jing-Fang Wanga,
6. Xiao-Wei Zhange,
7. Yi-Ming Zhouf,
9. Ming-kun Yangg,
10. Qian Xiongg,
11. Shu-Juan Guoa,
12. Huang-Ying Lea,
13. Song-Fang Wua,
15. Bingya Liuh,
1. Contributed by Zhu Chen, October 31, 2015 (sent for review September 16, 2015; reviewed by Jun O. Liu and Michael P. Snyder)
1. Abstract
Arsenic holds promise for treating a wide range of tumors. To understand arsenic's antitumor mechanism further, we identified 360 arsenic-binding proteins using a human proteome microarray and found proteins of glycolysis to be highly enriched. In-depth in vitro and in vivo analysis revealed that glycolysis in general and the rate-limiting enzyme hexokinase-2 of the glycolytic pathway in particular play a key role in mediating the anticancer activity of arsenic. These findings shed light on the mode of action of arsenic, and the newly identified arsenic-binding proteins may serve as a rich resource for future studies.
AbstractArsenic is highly effective for treating acute promyelocytic leukemia (APL) and has shown significant promise against many other tumors. However, although its mechanistic effects in APL are established, its broader anticancer mode of action is not understood. In this study, using a human proteome microarray, we identified 360 proteins that specifically bind arsenic. Among the most highly enriched proteins in this set are those in the glycolysis pathway, including the rate-limiting enzyme in glycolysis, hexokinase-1. Detailed biochemical and metabolomics analyses of the highly homologous hexokinase-2 (HK2), which is overexpressed in many cancers, revealed significant inhibition by arsenic. Furthermore, overexpression of HK2 rescued cells from arsenic-induced apoptosis. Our results thus strongly implicate glycolysis, and HK2 in particular, as a key target of arsenic. Moreover, the arsenic-binding proteins identified in this work are expected to serve as a valuable resource for the development of synergistic antitumor therapeutic strategies.
Footnotes
· 1H.-n.Z., L.Y., and J.-y.L. contributed equally to this work.
· 2To whom correspondence may be addressed. Email: [email protected] or [email protected].
· Author contributions: Z.C. and S.-c.T. designed research; H.-n.Z., L.Y., J.-y.L., J.-F.W., X.-W.Z., F.G., M.-k.Y., Q.X., S.-J.G., H.-Y.L., S.-F.W., W.Y., and S.-c.T. performed research; X.-W.Z., Y.-M.Z., F.G., M.-k.Y., Q.X., H.-Y.L., S.-F.W., W.Y., B.L., and H.Z. contributed new reagents/analytic tools; H.-n.Z., L.Y., J.-y.L., D.M.C., J.-F.W., Y.-M.Z., F.G., S.-J.G., B.L., H.Z., Z.C., and S.-c.T. analyzed data; and D.M.C., Z.C., and S.-c.T. wrote the paper.
· Reviewers: J.O.L., John Hopkins School of Medicine; and M.P.S., Stanford University.
· The authors declare no conflict of interest.
· This article contains supporting information online at www.pnas.org/lookup/suppl/doi:10.1073/pnas.1521316112/-/DCSupplemental.
http://en.sjtu.edu.cn/news/sjtu-researchers-revealed-the-anti-cancer-mechanism-of-as2o3/
SJTU Researchers Revealed the Anti-Cancer Mechanism of As2O3
November 25, 2015 Author: Tao Shengce
Researchers from Shanghai Jiao Tong University have confirmed that As2O3 can obviously restrain the activity of HK2: hexokinase-20 in tumor cells so as to influence the cell metabolism, resulting in apoptosis of tumor cells. This research achievement has been published on PNAS on November 23.
With concerted efforts of several generations of scientists, As2O3 has made an obvious success on the treatment of APL, the target spot and molecular mechanism of the drug have been illuminated. Except for APL, plenty of existing researches has proved that As2O3 has great potentiality in treating various malignancies, but relevant mechanism is not clear yet. As2O3 may play various roles in cells, so with High-Throughput Technology, it would be an effective strategy if the mechanism can be revealed at the system level.
This research is supported by National High Technology Research and Development Program of China (863 Plan) and natural science funds. Dr. Zhang Hainan, Dr. Yang Lina from School of System Biomedicine, SJTU and Professor Ling Jianya fromShandong University are all the first authors of this paper. Tao Shengce, a researcher from School of System Biomedicine, SJTU, and Chen Zhu, an academician from Ruijin Hospital, are corresponding authors of this article. Tao's primary domain of research is the exploitation and application of protein chip and a technology platform for series of protein chips has been established and applied to systematic study of relevant major scientific problems in medicine and clinical medicine.
Translated by Li Ying Reviewed by Wang Bingyu
